NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|13325064|ref|NP_001399|]
View 

cadherin EGF LAG seven-pass G-type receptor 2 precursor [Homo sapiens]

Protein Classification

Cadherin_repeat and GAIN domain-containing protein (domain architecture ID 11588033)

protein containing domains Cadherin_repeat, LamG, GAIN, and GPS

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
2373-2626 3.04e-133

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


The actual alignment was detected with superfamily member cd15992:

Pssm-ID: 333717  Cd Length: 255  Bit Score: 421.54  E-value: 3.04e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2373 ILPLKTLTYVALGVTLAALLLTFFFLTLLRILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLC 2452
Cdd:cd15992    1 ILPLKTLTWSSVGVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVIAILLHFFYLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2453 TFSWALLEALHLYRALTEVRDVNTGPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVS 2532
Cdd:cd15992   81 TFSWLFLEGLHIYRMLSEVRDINYGPMRFYYLIGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2533 MSVFLYILAARASCAAQRQGFEKK-GPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVV 2611
Cdd:cd15992  161 MNVFLYILSSRASCSAQQQSFEKKkGPVSGLRTAFTVLLLVSVTCLLALLSVNSDVILFHYLFAGFNCLQGPFIFLSHVV 240
                        250
                 ....*....|....*
gi 13325064 2612 LSKEVRKALKLACSR 2626
Cdd:cd15992  241 LLKEVRKALKTLCGP 255
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
2051-2289 1.66e-63

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organisms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


:

Pssm-ID: 318649  Cd Length: 205  Bit Score: 219.42  E-value: 1.66e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2051 RSQQLALLLRNATQHTAgYFGSDVKVAYQLATRLlahestqrgFGLSATQDV----HFTENLLRVGSALLDTANKRHWEL 2126
Cdd:pfam16489    1 GAKELARELRNATSHKP-LYGGDVLTAVELLSRL---------FDLLATQDAtlsnEFLENLVQTVSNLLDPENRESWED 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2127 IQQTEGGTAW--LLQHYEAYASALAQNMRhtYLSPFTIVTPNIVISVVRLDKGNFAGAKLPRYEALRGEQPPDLETTVIL 2204
Cdd:pfam16489   71 LQQTERGTAAtkLLRTLEEYALLLAQNMK--YLTPFVIVTPNIVLSVDVLDSPNFKGARHPRFPMKGERGPRDSEDSVKL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2205 PESVFRetppvvrpagpgeaqepeelarrqrrhPELSQGEAVASVIIYRTLAGLLPHNYDPDKRSLRVPKRpIINTPVVS 2284
Cdd:pfam16489  149 PPKALK---------------------------PPNSNGEVVVVFVLYRSLGSLLPPSYDTDRRSLRLPRR-VVNSPVVS 200

                   ....*
gi 13325064   2285 ISVHD 2289
Cdd:pfam16489  201 ASVHS 205
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
404-501 5.10e-36

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637  Cd Length: 98  Bit Score: 136.29  E-value: 5.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  404 YVVQVREDVTPGAPVLRVTASDRDKGSNAVVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRVRAQDGGRPP 483
Cdd:cd11304    2 YEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPP 81
                         90
                 ....*....|....*...
gi 13325064  484 LSNvSGLVTVQVLDINDN 501
Cdd:cd11304   82 LSS-TATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
509-606 5.26e-34

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637  Cd Length: 98  Bit Score: 130.51  E-value: 5.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  509 PFQATVLESVPLGYLVLHVQAIDADAGDNARLEYRLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTP 588
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                         90
                 ....*....|....*...
gi 13325064  589 ALTASASVSVTVLDVNDN 606
Cdd:cd11304   81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
185-285 6.56e-34

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637  Cd Length: 98  Bit Score: 130.13  E-value: 6.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  185 SYQATVPENQPAGTPVASLRAIDPDEGEAGRLEYTmdaLFDSRSNQFFSLDPVTGAVTTAEELDRETKSTHVFRVTAQDH 264
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYS---IVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77
                         90       100
                 ....*....|....*....|.
gi 13325064  265 GMPRRSALATLTILVTDTNDH 285
Cdd:cd11304   78 GGPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
293-395 2.63e-32

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637  Cd Length: 98  Bit Score: 125.50  E-value: 2.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  293 EYKESLRENLEVGYEVLTVRATDGDAPPNANILYRLLegsGGSPSEVFEIDPRSGVIRTRGPVDREEVESYQLTVEASDQ 372
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIV---SGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77
                         90       100
                 ....*....|....*....|...
gi 13325064  373 GrdPGPRSTTAAVFLSVEDDNDN 395
Cdd:cd11304   78 G--GPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
716-811 8.91e-32

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637  Cd Length: 98  Bit Score: 123.96  E-value: 8.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  716 HYTVNVNEDRPAGTTVVLISATDEDTGENARITYFMEDSIPQ--FRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIP 793
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDglFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                         90
                 ....*....|....*...
gi 13325064  794 QKSDTTYLEILVNDVNDN 811
Cdd:cd11304   81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
819-917 1.36e-30

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637  Cd Length: 98  Bit Score: 120.50  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  819 SYQGSVYEDVPPFTSVLQISATDRDSGLNGRVFYTFQGGDDGDGdFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGM 898
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGL-FSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGG 79
                         90
                 ....*....|....*....
gi 13325064  899 PPARTPMEVTVTVLDVNDN 917
Cdd:cd11304   80 PPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
925-1019 9.58e-30

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637  Cd Length: 98  Bit Score: 118.18  E-value: 9.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  925 EFDVFVEENSPIGLAVARVTATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQAT---SA 1001
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATdggGP 80
                         90
                 ....*....|....*...
gi 13325064 1002 PLVSRATVHVRLLDRNDN 1019
Cdd:cd11304   81 PLSSTATVTITVLDVNDN 98
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1369-1552 4.55e-29

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058  Cd Length: 151  Bit Score: 117.90  E-value: 4.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1369 TRSFPAHSFITFRGLR-QRFHFTLALSFATKERDGLLLYNGRFNeKHDFVALEVIQEQVQLTFSAGESTTTVSPFVPggV 1447
Cdd:cd00110    1 GVSFSGSSYVRLPTLPaPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--L 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1448 SDGQWHTVQLKYYNkpllgqtglpqgpseqKVAVVTVDGCDTgvalrfgsvlgnyscaAQGTQGGSKKSLDLTGPLLLGG 1527
Cdd:cd00110   78 NDGQWHSVSVERNG----------------RSVTLSVDGERV----------------VESGSPGGSALLNLDGPLYLGG 125
                        170       180
                 ....*....|....*....|....*.
gi 13325064 1528 VPDLPESFPVRMRQ-FVGCMRNLQVD 1552
Cdd:cd00110  126 LPEDLKSPGLPVSPgFVGCIRDLKVN 151
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
614-708 1.68e-22

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637  Cd Length: 98  Bit Score: 97.00  E-value: 1.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  614 EYTVRLNEDAAVGTSVVTVSAVDRD--AHSVITYQITSGNTRNRFSITSQSggGLVSLALPLDYKLERQYVLAVTASDG- 690
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDsgENGEVTYSIVSGNEDGLFSIDPST--GEITTAKPLDREEQSSYTLTVTATDGg 78
                         90       100
                 ....*....|....*....|
gi 13325064  691 --TRQDTAQIVVNVTDANTH 708
Cdd:cd11304   79 gpPLSSTATVTITVLDVNDN 98
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1618-1767 1.16e-19

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


:

Pssm-ID: 238058  Cd Length: 151  Bit Score: 90.56  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1618 HFLGSSLVAWHGLSLPiSQPWYLSLMFRTRQADGVLLQAITRGRS-TITLQLREGHVMLSVEGTglqASSLRLEPGRA-N 1695
Cdd:cd00110    3 SFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLG---SGSLVLSSKTPlN 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13325064 1696 DGDWHHAQLALGASggpgHAILSFDyGQQRAEGNLGPRLHGLHL-SNITVGGIPG----PAGGVARGFRGCLQGVRV 1767
Cdd:cd00110   79 DGQWHSVSVERNGR----SVTLSVD-GERVVESGSPGGSALLNLdGPLYLGGLPEdlksPGLPVSPGFVGCIRDLKV 150
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
2315-2368 2.97e-19

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


:

Pssm-ID: 197639  Cd Length: 49  Bit Score: 86.29  E-value: 2.97e-19
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 13325064    2315 TKPICVFWNHSilvsgTGGWSARGCEVVFRNESHVSCQCNHMTSFAVLMDVSRR 2368
Cdd:smart00303    1 FNPICVFWDES-----SGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
HormR smart00008
Domain present in hormone receptors;
1972-2034 1.86e-16

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 78.71  E-value: 1.86e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    1972 NYDSCPRAIEAGIWWPRTRFGLPAAAPCPKGSFG-----TAVRHCDEHRGWLP--PNLFNCTSITFSELK 2034
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGfsyktGASRNCTENGGWSPpfPNYSNCTSNDYEELK 70
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1924-1969 2.35e-14

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 71.96  E-value: 2.35e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 13325064    1924 CDCYPTGSLSRVCDPEDGQCPCKPGVIGRQCDRCDNPFAEVTTNGC 1969
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
1042-1120 4.24e-10

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


:

Pssm-ID: 206637  Cd Length: 98  Bit Score: 60.79  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1042 PGGAIGRVPAHDPDISD--SLTYSFERGNELSLVLLNASTGELKLSRALDNNRPLEAIMSVLVSD-GVHSVTAQCALRVT 1118
Cdd:cd11304   12 PGTVVLTVSATDPDSGEngEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDgGGPPLSSTATVTIT 91

                 ..
gi 13325064 1119 II 1120
Cdd:cd11304   92 VL 93
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1289-1324 7.21e-09

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 56.11  E-value: 7.21e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 13325064 1289 VDLCYSR-PCGPHGRCRSREGGYTCLCRDGYTGEHCE 1324
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1795-1829 1.88e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 1.88e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 13325064 1795 DPCDS-NPCPANSYCSNDWDSYSCSCDPGYYGDNCT 1829
Cdd:cd00054    3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1578-1609 2.11e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 2.11e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 13325064 1578 CDS-NTCHNGGTCVNQWDAFSCECPLGFGGKSC 1609
Cdd:cd00054    5 CASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1333-1366 1.61e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.09  E-value: 1.61e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 13325064 1333 TPGVCKNGGTCVNlLVGGFKCDCPSGdFEKPYCQ 1366
Cdd:cd00054    7 SGNPCQNGGTCVN-TVGSYRCSCPPG-YTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1832-1865 1.38e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 306513  Cd Length: 31  Bit Score: 40.44  E-value: 1.38e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13325064   1832 CDLNPCEHQSVCTRKPsapHGYTCECPPNYLGPY 1865
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP---GGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
7tmB2_CELSR2 cd15992
Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of ...
2373-2626 3.04e-133

Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320658  Cd Length: 255  Bit Score: 421.54  E-value: 3.04e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2373 ILPLKTLTYVALGVTLAALLLTFFFLTLLRILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLC 2452
Cdd:cd15992    1 ILPLKTLTWSSVGVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVIAILLHFFYLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2453 TFSWALLEALHLYRALTEVRDVNTGPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVS 2532
Cdd:cd15992   81 TFSWLFLEGLHIYRMLSEVRDINYGPMRFYYLIGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2533 MSVFLYILAARASCAAQRQGFEKK-GPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVV 2611
Cdd:cd15992  161 MNVFLYILSSRASCSAQQQSFEKKkGPVSGLRTAFTVLLLVSVTCLLALLSVNSDVILFHYLFAGFNCLQGPFIFLSHVV 240
                        250
                 ....*....|....*
gi 13325064 2612 LSKEVRKALKLACSR 2626
Cdd:cd15992  241 LLKEVRKALKTLCGP 255
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
2051-2289 1.66e-63

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organisms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


Pssm-ID: 318649  Cd Length: 205  Bit Score: 219.42  E-value: 1.66e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2051 RSQQLALLLRNATQHTAgYFGSDVKVAYQLATRLlahestqrgFGLSATQDV----HFTENLLRVGSALLDTANKRHWEL 2126
Cdd:pfam16489    1 GAKELARELRNATSHKP-LYGGDVLTAVELLSRL---------FDLLATQDAtlsnEFLENLVQTVSNLLDPENRESWED 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2127 IQQTEGGTAW--LLQHYEAYASALAQNMRhtYLSPFTIVTPNIVISVVRLDKGNFAGAKLPRYEALRGEQPPDLETTVIL 2204
Cdd:pfam16489   71 LQQTERGTAAtkLLRTLEEYALLLAQNMK--YLTPFVIVTPNIVLSVDVLDSPNFKGARHPRFPMKGERGPRDSEDSVKL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2205 PESVFRetppvvrpagpgeaqepeelarrqrrhPELSQGEAVASVIIYRTLAGLLPHNYDPDKRSLRVPKRpIINTPVVS 2284
Cdd:pfam16489  149 PPKALK---------------------------PPNSNGEVVVVFVLYRSLGSLLPPSYDTDRRSLRLPRR-VVNSPVVS 200

                   ....*
gi 13325064   2285 ISVHD 2289
Cdd:pfam16489  201 ASVHS 205
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
2402-2605 1.18e-40

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs).They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteristic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 306508  Cd Length: 244  Bit Score: 154.72  E-value: 1.18e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQ---------ADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVR 2472
Cdd:pfam00002   30 RKLHCTRNYIHLNLFASFILRAILFLVGDAVlfngedldhCSWKVGCKVVAVFLHYFFLANFFWMLVEGLYLYTLLVEVF 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2473 DVNTGPMRFYYMLGWGVPAFITGLAVGLDpeGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYILAARASCAAQRQG 2552
Cdd:pfam00002  110 FSERLYLWWYLLIGWGVPALVVGIWAGVK--GYGEDDGCWLSNENGLWWIIKGPVLLVILVNFIIFINIVRILVQKLRET 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13325064   2553 FEKKG---------------PVSGLQPS-FAVllllsatwllalLSVNSDTLLFHYLFATCNCIQGPFI 2605
Cdd:pfam00002  188 NMGESdlyqrrlakstllllPLLGITWVlFAF------------NPDNVLRVVFLYLFLILNSFQGFFV 244
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
404-501 5.10e-36

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 136.29  E-value: 5.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  404 YVVQVREDVTPGAPVLRVTASDRDKGSNAVVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRVRAQDGGRPP 483
Cdd:cd11304    2 YEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPP 81
                         90
                 ....*....|....*...
gi 13325064  484 LSNvSGLVTVQVLDINDN 501
Cdd:cd11304   82 LSS-TATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
509-606 5.26e-34

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 130.51  E-value: 5.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  509 PFQATVLESVPLGYLVLHVQAIDADAGDNARLEYRLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTP 588
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                         90
                 ....*....|....*...
gi 13325064  589 ALTASASVSVTVLDVNDN 606
Cdd:cd11304   81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
185-285 6.56e-34

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 130.13  E-value: 6.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  185 SYQATVPENQPAGTPVASLRAIDPDEGEAGRLEYTmdaLFDSRSNQFFSLDPVTGAVTTAEELDRETKSTHVFRVTAQDH 264
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYS---IVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77
                         90       100
                 ....*....|....*....|.
gi 13325064  265 GMPRRSALATLTILVTDTNDH 285
Cdd:cd11304   78 GGPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
293-395 2.63e-32

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 125.50  E-value: 2.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  293 EYKESLRENLEVGYEVLTVRATDGDAPPNANILYRLLegsGGSPSEVFEIDPRSGVIRTRGPVDREEVESYQLTVEASDQ 372
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIV---SGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77
                         90       100
                 ....*....|....*....|...
gi 13325064  373 GrdPGPRSTTAAVFLSVEDDNDN 395
Cdd:cd11304   78 G--GPPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
716-811 8.91e-32

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 123.96  E-value: 8.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  716 HYTVNVNEDRPAGTTVVLISATDEDTGENARITYFMEDSIPQ--FRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIP 793
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDglFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                         90
                 ....*....|....*...
gi 13325064  794 QKSDTTYLEILVNDVNDN 811
Cdd:cd11304   81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
819-917 1.36e-30

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 120.50  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  819 SYQGSVYEDVPPFTSVLQISATDRDSGLNGRVFYTFQGGDDGDGdFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGM 898
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGL-FSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGG 79
                         90
                 ....*....|....*....
gi 13325064  899 PPARTPMEVTVTVLDVNDN 917
Cdd:cd11304   80 PPLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
925-1019 9.58e-30

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 118.18  E-value: 9.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  925 EFDVFVEENSPIGLAVARVTATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQAT---SA 1001
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATdggGP 80
                         90
                 ....*....|....*...
gi 13325064 1002 PLVSRATVHVRLLDRNDN 1019
Cdd:cd11304   81 PLSSTATVTITVLDVNDN 98
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1369-1552 4.55e-29

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058  Cd Length: 151  Bit Score: 117.90  E-value: 4.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1369 TRSFPAHSFITFRGLR-QRFHFTLALSFATKERDGLLLYNGRFNeKHDFVALEVIQEQVQLTFSAGESTTTVSPFVPggV 1447
Cdd:cd00110    1 GVSFSGSSYVRLPTLPaPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--L 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1448 SDGQWHTVQLKYYNkpllgqtglpqgpseqKVAVVTVDGCDTgvalrfgsvlgnyscaAQGTQGGSKKSLDLTGPLLLGG 1527
Cdd:cd00110   78 NDGQWHSVSVERNG----------------RSVTLSVDGERV----------------VESGSPGGSALLNLDGPLYLGG 125
                        170       180
                 ....*....|....*....|....*.
gi 13325064 1528 VPDLPESFPVRMRQ-FVGCMRNLQVD 1552
Cdd:cd00110  126 LPEDLKSPGLPVSPgFVGCIRDLKVN 151
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
422-503 3.02e-27

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 110.52  E-value: 3.02e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     422 TASDRDKGSNAVVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRVRAQDGGRPPLSNVSgLVTVQVLDINDN 501
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTA-TVTITVLDVNDN 79

                    ..
gi 13325064     502 AP 503
Cdd:smart00112   80 AP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
528-608 1.14e-26

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 108.59  E-value: 1.14e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     528 QAIDADAGDNARLEYRLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTPALTASASVSVTVLDVNDNN 607
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80

                    .
gi 13325064     608 P 608
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
404-496 3.65e-26

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 107.39  E-value: 3.65e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    404 YVVQVREDVTPGAPVLRVTASDRDKGSNAVVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRVRAQDGGRPP 483
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|...
gi 13325064    484 LSNVsGLVTVQVL 496
Cdd:pfam00028   81 LSST-ATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
735-813 7.40e-26

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 106.28  E-value: 7.40e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     735 SATDEDTGENARITYFMEDSIPQ--FRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIPQKSDTTYLEILVNDVNDNA 812
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDglFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80

                    .
gi 13325064     813 P 813
Cdd:smart00112   81 P 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
312-397 6.00e-24

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 100.89  E-value: 6.00e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     312 RATDGDAPPNANILYRLLegsGGSPSEVFEIDPRSGVIRTRGPVDREEVESYQLTVEASDQGrdPGPRSTTAAVFLSVED 391
Cdd:smart00112    1 SATDADSGENGKVTYSIL---SGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGG--GPPLSSTATVTITVLD 75

                    ....*.
gi 13325064     392 DNDNAP 397
Cdd:smart00112   76 VNDNAP 81
Cadherin pfam00028
Cadherin domain;
510-601 8.62e-24

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 100.84  E-value: 8.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    510 FQATVLESVPLGYLVLHVQAIDADAGDNARLEYRLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTPA 589
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|..
gi 13325064    590 LTASASVSVTVL 601
Cdd:pfam00028   81 LSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
838-919 9.68e-24

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 100.12  E-value: 9.68e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     838 SATDRDSGLNGRVFYTFqGGDDGDGDFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGMPPARTPMEVTVTVLDVNDN 917
Cdd:smart00112    1 SATDADSGENGKVTYSI-LSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDN 79

                    ..
gi 13325064     918 PP 919
Cdd:smart00112   80 AP 81
LamG smart00282
Laminin G domain;
1390-1554 1.87e-23

Laminin G domain;


Pssm-ID: 214598  Cd Length: 132  Bit Score: 100.88  E-value: 1.87e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    1390 TLALSFATKERDGLLLYNGrFNEKHDFVALEVIQEQVQLTFSAGESTTTVSPfVPGGVSDGQWHTVQLKYynkpllgqtg 1469
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTS-DPTPLNDGQWHRVAVER---------- 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    1470 lpqgpsEQKVAVVTVDGCDtgvalrfgsvlgnyscAAQGTQGGSKKSLDLTGPLLLGGVPDLPESFPVRMRQ-FVGCMRN 1548
Cdd:smart00282   69 ------NGRSVTLSVDGGN----------------RVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPgFRGCIRN 126

                    ....*.
gi 13325064    1549 LQVDSR 1554
Cdd:smart00282  127 LKVNGK 132
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
204-287 2.53e-23

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 98.96  E-value: 2.53e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     204 RAIDPDEGEAGRLEYTmdaLFDSRSNQFFSLDPVTGAVTTAEELDRETKSTHVFRVTAQDHGMPRRSALATLTILVTDTN 283
Cdd:smart00112    1 SATDADSGENGKVTYS---ILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVN 77

                    ....
gi 13325064     284 DHDP 287
Cdd:smart00112   78 DNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
944-1021 3.71e-23

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 98.58  E-value: 3.71e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     944 TATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQAT---SAPLVSRATVHVRLLDRNDNP 1020
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATdggGPPLSSTATVTITVLDVNDNA 80

                    .
gi 13325064    1021 P 1021
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
297-390 1.22e-22

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 97.37  E-value: 1.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    297 SLRENLEVGYEVLTVRATDGDAPPNANILYRLLegsGGSPSEVFEIDPRSGVIRTRGPVDREEVESYQLTVEASDQGrdP 376
Cdd:pfam00028    4 SVPENAPVGTEVLTVTATDPDLGPNGRIFYSIL---GGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSG--G 78
                           90
                   ....*....|....
gi 13325064    377 GPRSTTAAVFLSVE 390
Cdd:pfam00028   79 PPLSSTATVTITVL 92
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
614-708 1.68e-22

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 97.00  E-value: 1.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  614 EYTVRLNEDAAVGTSVVTVSAVDRD--AHSVITYQITSGNTRNRFSITSQSggGLVSLALPLDYKLERQYVLAVTASDG- 690
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDsgENGEVTYSIVSGNEDGLFSIDPST--GEITTAKPLDREEQSSYTLTVTATDGg 78
                         90       100
                 ....*....|....*....|
gi 13325064  691 --TRQDTAQIVVNVTDANTH 708
Cdd:cd11304   79 gpPLSSTATVTITVLDVNDN 98
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1395-1554 1.30e-21

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 308045  Cd Length: 126  Bit Score: 95.58  E-value: 1.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   1395 FATKERDGLLLYNGrfNEKHDFVALEVIQEQVQLTFSAGESTTTVSPFvPGGVSDGQWHTVQLKYynkpllgqtglpqgp 1474
Cdd:pfam02210    1 FRTTQPNGLLLYAG--GGGSDFLALELVDGRLVLRYDLGSGPVSLLSS-GKPLNDGQWHRVRVSR--------------- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   1475 sEQKVAVVTVDGCDTgvalrfgsvlgnyscaAQGTQGGSKKSLDLTGPLLLGGVP-DLPESFPVRMRQFVGCMRNLQVDS 1553
Cdd:pfam02210   63 -NGRTLTLSVDGQTV----------------VSALPPGESLLLNLNGPLYLGGLPpLLLLPALPVTEGFVGCIRDVRVNG 125

                   .
gi 13325064   1554 R 1554
Cdd:pfam02210  126 E 126
Cadherin pfam00028
Cadherin domain;
186-280 1.67e-21

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 93.90  E-value: 1.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    186 YQATVPENQPAGTPVASLRAIDPDEGEAGRLEYTMdaLFDSRSNQFfSLDPVTGAVTTAEELDRETKSTHVFRVTAQDHG 265
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSI--LGGGPGGNF-RIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77
                           90
                   ....*....|....*
gi 13325064    266 MPRRSALATLTILVT 280
Cdd:pfam00028   78 GPPLSSTATVTITVL 92
Cadherin pfam00028
Cadherin domain;
717-805 2.80e-21

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 93.52  E-value: 2.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    717 YTVNVNEDRPAGTTVVLISATDEDTGENARITYFM--EDSIPQFRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIPQ 794
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSIlgGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|.
gi 13325064    795 KSDTTYLEILV 805
Cdd:pfam00028   81 LSSTATVTITV 91
Cadherin pfam00028
Cadherin domain;
820-912 8.40e-21

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 91.98  E-value: 8.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    820 YQGSVYEDVPPFTSVLQISATDRDSGLNGRVFYTFQGGDDGDGdFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGMP 899
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGN-FRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGP 79
                           90
                   ....*....|...
gi 13325064    900 PARTPMEVTVTVL 912
Cdd:pfam00028   80 PLSSTATVTITVL 92
Cadherin pfam00028
Cadherin domain;
926-1014 4.52e-20

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 90.05  E-value: 4.52e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    926 FDVFVEENSPIGLAVARVTATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQATSA---P 1002
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSggpP 80
                           90
                   ....*....|..
gi 13325064   1003 LVSRATVHVRLL 1014
Cdd:pfam00028   81 LSSTATVTITVL 92
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1618-1767 1.16e-19

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058  Cd Length: 151  Bit Score: 90.56  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1618 HFLGSSLVAWHGLSLPiSQPWYLSLMFRTRQADGVLLQAITRGRS-TITLQLREGHVMLSVEGTglqASSLRLEPGRA-N 1695
Cdd:cd00110    3 SFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLG---SGSLVLSSKTPlN 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13325064 1696 DGDWHHAQLALGASggpgHAILSFDyGQQRAEGNLGPRLHGLHL-SNITVGGIPG----PAGGVARGFRGCLQGVRV 1767
Cdd:cd00110   79 DGQWHSVSVERNGR----SVTLSVD-GERVVESGSPGGSALLNLdGPLYLGGLPEdlksPGLPVSPGFVGCIRDLKV 150
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
2315-2368 2.97e-19

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 86.29  E-value: 2.97e-19
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 13325064    2315 TKPICVFWNHSilvsgTGGWSARGCEVVFRNESHVSCQCNHMTSFAVLMDVSRR 2368
Cdd:smart00303    1 FNPICVFWDES-----SGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
LamG smart00282
Laminin G domain;
1639-1767 1.38e-18

Laminin G domain;


Pssm-ID: 214598  Cd Length: 132  Bit Score: 86.62  E-value: 1.38e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    1639 YLSLMFRTRQADGVLLQAITRGRS-TITLQLREGHVMLSVEgTGLQASSLRLEPGRANDGDWHHAQLALGASggpgHAIL 1717
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYD-LGSGPARLTSDPTPLNDGQWHRVAVERNGR----SVTL 75
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 13325064    1718 SFDYG-QQRAEGNLGPRLHGLHlSNITVGGIPG----PAGGVARGFRGCLQGVRV 1767
Cdd:smart00282   76 SVDGGnRVSGESPGGLTILNLD-GPLYLGGLPEdlklPPLPVTPGFRGCIRNLKV 129
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1644-1770 3.22e-17

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 308045  Cd Length: 126  Bit Score: 82.48  E-value: 3.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   1644 FRTRQADGVLLQAITRGRSTITLQLREGHVMLSVEgTGLQASSLRLEPGRANDGDWHHAQLALgasgGPGHAILSFDYGQ 1723
Cdd:pfam02210    1 FRTTQPNGLLLYAGGGGSDFLALELVDGRLVLRYD-LGSGPVSLLSSGKPLNDGQWHRVRVSR----NGRTLTLSVDGQT 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13325064   1724 QRAEGNLGPRLHGLHLSNITVGGIPGP----AGGVARGFRGCLQGVRVSDT 1770
Cdd:pfam02210   76 VVSALPPGESLLLNLNGPLYLGGLPPLlllpALPVTEGFVGCIRDVRVNGE 126
Cadherin pfam00028
Cadherin domain;
615-703 4.48e-17

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 81.19  E-value: 4.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    615 YTVRLNEDAAVGTSVVTVSAVDRD--AHSVITYQITSGNTRNRFSITSQSggGLVSLALPLDYKLERQYVLAVTASDG-- 690
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDlgPNGRIFYSILGGGPGGNFRIDPDT--GDISTTKPLDRESIGEYELTVEATDSgg 78
                           90
                   ....*....|....
gi 13325064    691 -TRQDTAQIVVNVT 703
Cdd:pfam00028   79 pPLSSTATVTITVL 92
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
2317-2362 1.81e-16

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


Pssm-ID: 307782  Cd Length: 46  Bit Score: 78.18  E-value: 1.81e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 13325064   2317 PICVFWNHSILvSGTGGWSARGCEVVF-RNESHVSCQCNHMTSFAVL 2362
Cdd:pfam01825    1 PQCVFWDFDTG-SGTGGWSTEGCELVTsSNDTHTVCSCNHLTSFAVL 46
HormR smart00008
Domain present in hormone receptors;
1972-2034 1.86e-16

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 78.71  E-value: 1.86e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    1972 NYDSCPRAIEAGIWWPRTRFGLPAAAPCPKGSFG-----TAVRHCDEHRGWLP--PNLFNCTSITFSELK 2034
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGfsyktGASRNCTENGGWSPpfPNYSNCTSNDYEELK 70
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1924-1969 2.35e-14

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 71.96  E-value: 2.35e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 13325064    1924 CDCYPTGSLSRVCDPEDGQCPCKPGVIGRQCDRCDNPFAEVTTNGC 1969
Cdd:smart00180    1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
633-710 1.29e-13

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 70.84  E-value: 1.29e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     633 SAVDRD--AHSVITYQITSGNTRNRFSITSQSggGLVSLALPLDYKLERQYVLAVTASDG---TRQDTAQIVVNVTDANT 707
Cdd:smart00112    1 SATDADsgENGKVTYSILSGNDDGLFSIDPET--GEITTTKPLDREEQPEYTLTVEATDGggpPLSSTATVTITVLDVND 78

                    ...
gi 13325064     708 HRP 710
Cdd:smart00112   79 NAP 81
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
1924-1961 5.49e-13

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 68.15  E-value: 5.49e-13
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 13325064 1924 CDCYPTGSLSRVCDPEDGQCPCKPGVIGRQCDRCDNPF 1961
Cdd:cd00055    2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
1924-1957 4.28e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 278482  Cd Length: 49  Bit Score: 65.45  E-value: 4.28e-12
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13325064   1924 CDCYPTGSLSRVCDPEDGQCPCKPGVIGRQCDRC 1957
Cdd:pfam00053    1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRC 34
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
1042-1120 4.24e-10

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 60.79  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1042 PGGAIGRVPAHDPDISD--SLTYSFERGNELSLVLLNASTGELKLSRALDNNRPLEAIMSVLVSD-GVHSVTAQCALRVT 1118
Cdd:cd11304   12 PGTVVLTVSATDPDSGEngEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDgGGPPLSSTATVTIT 91

                 ..
gi 13325064 1119 II 1120
Cdd:cd11304   92 VL 93
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
1973-2028 2.46e-09

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 308439  Cd Length: 64  Bit Score: 57.78  E-value: 2.46e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13325064   1973 YDSCPRAIEAGIWWPRTRFGLPAAAPCPKGSF-----GTAVRHCDEHRGWL---PPNLFNCTSI 2028
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFSgfdyrGNASRNCTEDGTWSehpPTNYSNCTSN 64
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1289-1324 7.21e-09

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 56.11  E-value: 7.21e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 13325064 1289 VDLCYSR-PCGPHGRCRSREGGYTCLCRDGYTGEHCE 1324
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1795-1829 1.88e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 1.88e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 13325064 1795 DPCDS-NPCPANSYCSNDWDSYSCSCDPGYYGDNCT 1829
Cdd:cd00054    3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1578-1609 2.11e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 2.11e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 13325064 1578 CDS-NTCHNGGTCVNQWDAFSCECPLGFGGKSC 1609
Cdd:cd00054    5 CASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1578-1607 5.25e-07

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 306513  Cd Length: 31  Bit Score: 50.46  E-value: 5.25e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 13325064   1578 CDSNTCHNGGTCVNQWDAFSCECPLGFGGK 1607
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF_CA smart00179
Calcium-binding EGF-like domain;
1288-1324 1.61e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 49.17  E-value: 1.61e-06
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 13325064    1288 EVDLCYSR-PCGPHGRCRSREGGYTCLCRDGYT-GEHCE 1324
Cdd:smart00179    1 DIDECASGnPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1333-1366 1.61e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.09  E-value: 1.61e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 13325064 1333 TPGVCKNGGTCVNlLVGGFKCDCPSGdFEKPYCQ 1366
Cdd:cd00054    7 SGNPCQNGGTCVN-TVGSYRCSCPPG-YTGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
1578-1609 2.20e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 45.70  E-value: 2.20e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 13325064    1578 CDS-NTCHNGGTCVNQWDAFSCECPLGF-GGKSC 1609
Cdd:smart00179    5 CASgNPCQNGGTCVNTVGSYRCECPPGYtDGRNC 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
1333-1366 3.73e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 45.32  E-value: 3.73e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 13325064    1333 TPGVCKNGGTCVNLlVGGFKCDCPSGDFEKPYCQ 1366
Cdd:smart00179    7 SGNPCQNGGTCVNT-VGSYRCECPPGYTDGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1292-1322 2.11e-04

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 306513  Cd Length: 31  Bit Score: 42.76  E-value: 2.11e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13325064   1292 CYSRPCGPHGRCRSREGGYTCLCRDGYTGEH 1322
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
1795-1829 4.84e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 41.85  E-value: 4.84e-04
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 13325064    1795 DPCDS-NPCPANSYCSNDWDSYSCSCDPGYY-GDNCT 1829
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1797-1827 1.03e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 306513  Cd Length: 31  Bit Score: 40.83  E-value: 1.03e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13325064   1797 CDSNPCPANSYCSNDWDSYSCSCDPGYYGDN 1827
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1832-1865 1.38e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 306513  Cd Length: 31  Bit Score: 40.44  E-value: 1.38e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 13325064   1832 CDLNPCEHQSVCTRKPsapHGYTCECPPNYLGPY 1865
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP---GGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
1332-1362 2.32e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 306513  Cd Length: 31  Bit Score: 39.67  E-value: 2.32e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 13325064   1332 CTPGVCKNGGTCVNLLvGGFKCDCPSGDFEK 1362
Cdd:pfam00008    1 CAPNPCSNGGTCVDTP-GGYTCICPEGYTGK 30
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
1051-1120 4.90e-03

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 39.26  E-value: 4.90e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13325064    1051 AHDPDISDS--LTYSFERGNELSLVLLNASTGELKLSRALDNNRPLEAIMSVLVSD-GVHSVTAQCALRVTII 1120
Cdd:smart00112    2 ATDADSGENgkVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDgGGPPLSSTATVTITVL 74
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
1826-1867 5.95e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.77  E-value: 5.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 13325064 1826 DNCTnvcDLNPCEHQSVCTRKPSaphGYTCECPPNYLGPYCE 1867
Cdd:cd00054    3 DECA---SGNPCQNGGTCVNTVG---SYRCSCPPGYTGRNCE 38
 
Name Accession Description Interval E-value
7tmB2_CELSR2 cd15992
Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of ...
2373-2626 3.04e-133

Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320658  Cd Length: 255  Bit Score: 421.54  E-value: 3.04e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2373 ILPLKTLTYVALGVTLAALLLTFFFLTLLRILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLC 2452
Cdd:cd15992    1 ILPLKTLTWSSVGVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVIAILLHFFYLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2453 TFSWALLEALHLYRALTEVRDVNTGPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVS 2532
Cdd:cd15992   81 TFSWLFLEGLHIYRMLSEVRDINYGPMRFYYLIGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2533 MSVFLYILAARASCAAQRQGFEKK-GPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVV 2611
Cdd:cd15992  161 MNVFLYILSSRASCSAQQQSFEKKkGPVSGLRTAFTVLLLVSVTCLLALLSVNSDVILFHYLFAGFNCLQGPFIFLSHVV 240
                        250
                 ....*....|....*
gi 13325064 2612 LSKEVRKALKLACSR 2626
Cdd:cd15992  241 LLKEVRKALKTLCGP 255
7tmB2_CELSR_Adhesion_IV cd15441
cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 ...
2373-2626 9.36e-106

cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuron migration and axon guidance in the CNS.


Pssm-ID: 320557  Cd Length: 254  Bit Score: 342.69  E-value: 9.36e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2373 ILPLKTLTYVALGVTLAALLLTFFFLTLLRILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLC 2452
Cdd:cd15441    1 VLLLKIVTYIGIGISLVLLVIAFLVLSCLRGLQSNSNSIHKNLVACLLLAELLFLLGINQTENLFPCKLIAILLHYFYLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2453 TFSWALLEALHLYRALTEVRDVNTGPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVS 2532
Cdd:cd15441   81 AFSWLLVESLHLYRMLTEPRDINHGHMRFYYLLGYGIPAIIVGLSVGLRPDGYGNPDFCWLSVNETLIWSFAGPIAFVIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2533 MSVFLYILAARASCAAQRQGFEKKGPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVL 2612
Cdd:cd15441  161 ITLIIFILALRASCTLKRHVLEKASVRTDLRSSFLLLPLLGATWVFGLLAVNEDSELLHYLFAGLNFLQGLFIFLFYCIF 240
                        250
                 ....*....|....
gi 13325064 2613 SKEVRKALKLACSR 2626
Cdd:cd15441  241 NKKVRRELKNALLR 254
7tmB2_CELSR1 cd15991
Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of ...
2373-2621 2.45e-96

Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320657  Cd Length: 254  Bit Score: 316.02  E-value: 2.45e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2373 ILPLKTLTYVALGVTLAALLLTFFFLTLLRILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLC 2452
Cdd:cd15991    1 VLPLKIITYTTVSLSLVALLITFILLVLIRTLRSNLHSIHKNLVAALFFSELIFLIGINQTENPFVCTVVAILLHYFYMS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2453 TFSWALLEALHLYRALTEVRDVNTGPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVS 2532
Cdd:cd15991   81 TFAWMFVEGLHIYRMLTEVRNINTGHMRFYYVVGWGIPAIITGLAVGLDPQGYGNPDFCWLSVQDTLIWSFAGPIGIVVI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2533 MSVFLYILAARASCAAQRQGFEKKGPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVL 2612
Cdd:cd15991  161 INTVIFVLAAKASCGRRQRYFEKSGVISMLRTAFLLLLLISATWLLGLMAVNSDTLSFHYLFAIFSCLQGIFIFFFHCIF 240

                 ....*....
gi 13325064 2613 SKEVRKALK 2621
Cdd:cd15991  241 NKEVRKHLK 249
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
2376-2624 8.03e-78

Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuronal migration and axon guidance in the CNS. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320659  Cd Length: 254  Bit Score: 262.47  E-value: 8.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2376 LKTLTYVALGVTLAALLLTFFFLTLLRILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFS 2455
Cdd:cd15993    4 LAIVTYSSVSASLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVVAILLHYFFLSTFA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2456 WALLEALHLYRALTEVRDVNTGPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSV 2535
Cdd:cd15993   84 WLFVQGLHIYRMQTEARNVNFGAMRFYYAIGWGVPAIITGLAVGLDPEGYGNPDFCWISIHDKLVWSFAGPIVVVIVMNG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2536 FLYILAARASCAAQRQGFEKKGPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKE 2615
Cdd:cd15993  164 VMFLLVARMSCSPGQKETKKTSVLMTLRSSFLLLLLISATWLFGLLAVNNSVLAFHYLHAILCCLQGLAVLLLFCVLNEE 243

                 ....*....
gi 13325064 2616 VRKALKLAC 2624
Cdd:cd15993  244 VQEAWKLAC 252
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
2051-2289 1.66e-63

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organisms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


Pssm-ID: 318649  Cd Length: 205  Bit Score: 219.42  E-value: 1.66e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2051 RSQQLALLLRNATQHTAgYFGSDVKVAYQLATRLlahestqrgFGLSATQDV----HFTENLLRVGSALLDTANKRHWEL 2126
Cdd:pfam16489    1 GAKELARELRNATSHKP-LYGGDVLTAVELLSRL---------FDLLATQDAtlsnEFLENLVQTVSNLLDPENRESWED 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2127 IQQTEGGTAW--LLQHYEAYASALAQNMRhtYLSPFTIVTPNIVISVVRLDKGNFAGAKLPRYEALRGEQPPDLETTVIL 2204
Cdd:pfam16489   71 LQQTERGTAAtkLLRTLEEYALLLAQNMK--YLTPFVIVTPNIVLSVDVLDSPNFKGARHPRFPMKGERGPRDSEDSVKL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2205 PESVFRetppvvrpagpgeaqepeelarrqrrhPELSQGEAVASVIIYRTLAGLLPHNYDPDKRSLRVPKRpIINTPVVS 2284
Cdd:pfam16489  149 PPKALK---------------------------PPNSNGEVVVVFVLYRSLGSLLPPSYDTDRRSLRLPRR-VVNSPVVS 200

                   ....*
gi 13325064   2285 ISVHD 2289
Cdd:pfam16489  201 ASVHS 205
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
2404-2619 1.01e-53

adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors; The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320168  Cd Length: 253  Bit Score: 192.79  E-value: 1.01e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2404 LRSNQHG-IRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEV-RDVNTGPMRF 2481
Cdd:cd15040   32 LRKRKPTkILLNLCLALLLANLLFLFGINSTDNPVLCTAVAALLHYFLLASFMWMLVEALLLYLRLVKVfGTYPRHFILK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYMLGWGVPAFITGLAVGLDPEGYGN-PDFCWLSIYDTLIWSFAGPVAF--AVSMSVFLYILAARASCAAQRQGFEKKGP 2558
Cdd:cd15040  112 YALIGWGLPLIIVIITLAVDPDSYGNsSGYCWLSNGNGLYYAFLGPVLLiiLVNLVIFVLVLRKLLRLSAKRNKKKRKKT 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13325064 2559 VSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRKA 2619
Cdd:cd15040  192 KAQLRAAVSLFFLLGLTWIFGILAIFGARVVFQYLFAIFNSLQGFFIFIFHCLRNKEVRKA 252
7tmB2_GPR133-like_Adhesion_V cd15933
orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of ...
2375-2620 6.11e-53

orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group V adhesion GPCRs include orphan receptors GPR133, GPR144, and closely related proteins. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the G(s) protein, leading to activation of adenylate cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320599  Cd Length: 252  Bit Score: 190.62  E-value: 6.11e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2375 PLKTLTYVALGVTLAALLLTFFFLTLLRILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTF 2454
Cdd:cd15933    3 ALSIISYIGCGISIACLALTLIIFLVLRVLSSDRFQIHKNLCVALLLAQILLLAGEWAEGNKVACKVVAILLHFFFMAAF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2455 SWALLEALHLYRALTEVrdVNTGP-MRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSM 2533
Cdd:cd15933   83 SWMLVEGLHLYLMIVKV--FNYKSkMRYYYFIGWGLPAIIVAISLAILFDDYGSPNVCWLSLDDGLIWAFVGPVIFIITV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2534 SVFLYILAARASCAAQRQGFEKKG-----------------PVSGLQPSFAVllllsatwllalLSVNSDTLLFHYLFAT 2596
Cdd:cd15933  161 NTVILILVVKITVSLSTNDAKKSQgtlaqikstakasvvllPILGLTWLFGV------------LVVNSQTIVFQYIFVI 228
                        250       260
                 ....*....|....*....|....
gi 13325064 2597 CNCIQGPFIFLSYVVLSKEVRKAL 2620
Cdd:cd15933  229 LNSLQGLMIFLFHCVLNSEVRSAF 252
7tm_classB cd13952
class B family of seven-transmembrane G protein-coupled receptors; The class B of ...
2404-2620 1.03e-52

class B family of seven-transmembrane G protein-coupled receptors; The class B of seven-transmembrane GPCRs is classified into three major subfamilies: subfamily B1 (secretin-like receptor family), B2 (adhesion family), and B3 (Methuselah-like family). The class B receptors have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi or prokaryotes. The B1 subfamily comprises receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the subfamily B1 receptors preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The subfamily B2 consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Furthermore, the subfamily B3 includes Methuselah (Mth) protein, which was originally identified in Drosophila as a GPCR affecting stress resistance and aging, and its closely related proteins.


Pssm-ID: 320090  Cd Length: 253  Bit Score: 190.09  E-value: 1.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2404 LRSNQHG-IRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTG-PMRF 2481
Cdd:cd13952   32 LRKRKRTkILLNLCLSLLLANLLFLVGISSTDNPVGCTAVAALLHYFLLASFMWMLVEALLLYLRLVKVFGTYPRhFILK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYMLGWGVPAFITGLAVGLDPEGYGN-PDFCWLSIYDTLIWSFAGPVAF--AVSMSVFLYILAARASCAAQRQGFEKKGP 2558
Cdd:cd13952  112 YSLIGWGLPLIIVIITAAVDPDSYGGsSGYCWLSNGNGLYYAFLGPVLLiiLINLVIFVLILRKLLRLSAKRNKSERKKT 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13325064 2559 VSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRKAL 2620
Cdd:cd13952  192 KRQLRAALSLFFLLGLTWIFGILAILGARVVFQYLFAIFNSLQGFFIFIFYCLRNKEVRKAW 253
7tmB2_latrophilin-like_invertebrate cd15440
invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane ...
2373-2621 4.36e-51

invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; This subgroup includes latrophilim-like proteins that are found in inveterbrates such as insects and worms. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of vertebrate latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320556  Cd Length: 259  Bit Score: 185.54  E-value: 4.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2373 ILPLKTLTYVALGVTLAALLLTFFFLTLLRILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLC 2452
Cdd:cd15440    1 QSALTFITYIGCIISIVCLLLAFITFTCFRNLQCDRNTIHKNLCLCLLIAEIVFLLGIDQTENRTLCGVIAGLLHYFFLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2453 TFSWALLEALHLYRALTEVRDVNTGPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVS 2532
Cdd:cd15440   81 AFSWMLLEGFQLYVMLVEVFEPEKSRIKWYYLFGYGLPALIVAVSAGVDPTGYGTEDHCWLSTENGFIWSFVGPVIVVLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2533 MSVFLYILAARASCAAQRQGFEK-------------KGPVS-----GLQPSFAVLLllsatwllallsVNSDTLLFHYLF 2594
Cdd:cd15440  161 ANLVFLGMAIYVMCRHSSRSASKkdasklknirgwlKGSIVlvvllGLTWTFGLLF------------INQESIVMAYIF 228
                        250       260
                 ....*....|....*....|....*..
gi 13325064 2595 ATCNCIQGPFIFLSYVVLSKEVRKALK 2621
Cdd:cd15440  229 TILNSLQGLFIFIFHCVLNEKVRKELR 255
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
2402-2605 1.18e-40

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs).They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteristic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 306508  Cd Length: 244  Bit Score: 154.72  E-value: 1.18e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQ---------ADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVR 2472
Cdd:pfam00002   30 RKLHCTRNYIHLNLFASFILRAILFLVGDAVlfngedldhCSWKVGCKVVAVFLHYFFLANFFWMLVEGLYLYTLLVEVF 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   2473 DVNTGPMRFYYMLGWGVPAFITGLAVGLDpeGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYILAARASCAAQRQG 2552
Cdd:pfam00002  110 FSERLYLWWYLLIGWGVPALVVGIWAGVK--GYGEDDGCWLSNENGLWWIIKGPVLLVILVNFIIFINIVRILVQKLRET 187
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13325064   2553 FEKKG---------------PVSGLQPS-FAVllllsatwllalLSVNSDTLLFHYLFATCNCIQGPFI 2605
Cdd:pfam00002  188 NMGESdlyqrrlakstllllPLLGITWVlFAF------------NPDNVLRVVFLYLFLILNSFQGFFV 244
7tmB2_Latrophilin_Adhesion_I cd15252
Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of ...
2402-2618 4.30e-37

Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; Group I adhesion GPCRs consist of latrophilins (also called lectomedins or latrotoxin receptors) and ETL (EGF-TM7-latrophilin-related protein. These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320380  Cd Length: 257  Bit Score: 144.57  E-value: 4.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTGPMRF 2481
Cdd:cd15252   30 RGLQSDRTTIHKNLCISLFLAELVFLIGINTTTNKIFCSVIAGLLHYFFLAAFAWMFIEGIQLYLMLVEVFENEGSRHKN 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLY------------ILAARASCAAQ 2549
Cdd:cd15252  110 FYIFGYGSPAVIVGVSAALGYRYYGTTKVCWLSTENYFIWSFIGPATLIILLNLIFLgvaiykmfrhtaGLKPEVSCLEN 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13325064 2550 RQGFeKKGPVS-----GLQPSFAVLLllsatwllallsVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRK 2618
Cdd:cd15252  190 IRSW-ARGAIAllfllGLTWIFGVLH------------INHASVVMAYLFTVSNSLQGMFIFLFHCVLSRKVRK 250
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
404-501 5.10e-36

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 136.29  E-value: 5.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  404 YVVQVREDVTPGAPVLRVTASDRDKGSNAVVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRVRAQDGGRPP 483
Cdd:cd11304    2 YEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGPP 81
                         90
                 ....*....|....*...
gi 13325064  484 LSNvSGLVTVQVLDINDN 501
Cdd:cd11304   82 LSS-TATVTITVLDVNDN 98
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
2402-2621 7.69e-35

epidermal growth factor-like module-containing mucin-like hormone receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4) and the leukocyte cell-surface antigen CD97, are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying number of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of EMR2, alternative splicing results in four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320555  Cd Length: 263  Bit Score: 138.24  E-value: 7.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLY---RALTEVRDVNTG- 2477
Cdd:cd15439   30 RSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSIIAGFLHYLFLACFAWMFLEAVHLFltvRNLKVVNYFSSHr 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2478 -PMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPV-AFAVSMSVF----LYILAAR-ASCAAQr 2550
Cdd:cd15439  110 fKKRFMYPVGYGLPAVIVAISAAVNPQGYGTPKHCWLSMEKGFIWSFLGPVcVIIVINLVLfcltLWILREKlSSLNAE- 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13325064 2551 qgfekkgpVSGLQPSFAVLLLLSATWLLALLS-------VNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRKALK 2621
Cdd:cd15439  189 --------VSTLKNTRLLTFKAIAQLFILGCTwilglfqVGPVATVMAYLFTITNSLQGVFIFLVHCLLNRQVREEYR 258
7tmB2_Latrophilin-3 cd16005
Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled ...
2402-2618 9.94e-35

Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320671  Cd Length: 258  Bit Score: 137.77  E-value: 9.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTGPMRF 2481
Cdd:cd16005   30 RGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVF-----LYILAARASCAAQRQGFEKK 2556
Cdd:cd16005  110 FYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIflgiaLYKMFHHTAILKPESGCLDN 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13325064 2557 GPvSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRK 2618
Cdd:cd16005  190 IK-SWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIFHCVLQKKVRK 250
7tmB2_CD97 cd15438
CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
2402-2617 1.84e-34

CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320554  Cd Length: 261  Bit Score: 137.20  E-value: 1.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTGPMRF 2481
Cdd:cd15438   30 RSIRGTRNTIHLHLCLSLFLAHLIFLLGINNTNNQVACAVVAGLLHYFFLAAFCWMSLEGVELYLMVVQVFNTQSLKKRY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYI-----LAARASCAAQRQGFEKK 2556
Cdd:cd15438  110 LLLIGYGVPLVIVAISAAVNSKGYGTQRHCWLSLERGFLWSFLGPVCLIILVNAIIFVitvwkLAEKFSSINPDMEKLRK 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13325064 2557 GPVSGLQpSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVR 2617
Cdd:cd15438  190 IRALTIT-AIAQLCILGCTWIFGFFQFSDSTLVMSYLFTILNSLQGLFIFLLHCLLSKQVR 249
7tmB2_Latrophilin cd15436
Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
2402-2618 2.14e-34

Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320552  Cd Length: 258  Bit Score: 136.85  E-value: 2.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTGPMRF 2481
Cdd:cd15436   30 RGLQTDRNTIHKNLCINLFIAELLFLIGINRTQYTIACPIFAGLLHFFFLAAFCWLCLEGVQLYLLLVEVFESEYSRRKY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYILA----ARASCAAQRQGFEKKG 2557
Cdd:cd15436  110 FYLCGYSFPALVVAVSAAIDYRSYGTEKACWLRVDNYFIWSFIGPVTFVITLNLVFLVITlhkmVSHSDLLKPDSSRLDN 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13325064 2558 PVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRK 2618
Cdd:cd15436  190 IKSWALGAIALLFLLGLTWSFGLMFINEESVVMAYLFTIFNAFQGVFIFIFHCALQKKVRK 250
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
2402-2618 2.21e-34

Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320673  Cd Length: 258  Bit Score: 136.98  E-value: 2.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTGPMRF 2481
Cdd:cd16007   30 RGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIFAGLLHFFFLAAFSWLCLEGVQLYLMLVEVFESEYSRKKY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMS-VFLYILAARASCAAqrqgfekkgpvS 2560
Cdd:cd16007  110 YYLCGYCFPALVVGISAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNlVFLMVTLHKMIRSS-----------S 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13325064 2561 GLQP---------SFAVLLLLSATWLLALLS-----VNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRK 2618
Cdd:cd16007  179 VLKPdssrldnikSWALGAITLLFLLGLTWAfgllfINKESVVMAYLFTTFNAFQGMFIFIFHCALQKKVHK 250
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
509-606 5.26e-34

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 130.51  E-value: 5.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  509 PFQATVLESVPLGYLVLHVQAIDADAGDNARLEYRLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTP 588
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                         90
                 ....*....|....*...
gi 13325064  589 ALTASASVSVTVLDVNDN 606
Cdd:cd11304   81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
185-285 6.56e-34

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 130.13  E-value: 6.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  185 SYQATVPENQPAGTPVASLRAIDPDEGEAGRLEYTmdaLFDSRSNQFFSLDPVTGAVTTAEELDRETKSTHVFRVTAQDH 264
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYS---IVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77
                         90       100
                 ....*....|....*....|.
gi 13325064  265 GMPRRSALATLTILVTDTNDH 285
Cdd:cd11304   78 GGPPLSSTATVTITVLDVNDN 98
7tmB2_Latrophilin-2 cd16006
Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled ...
2402-2618 1.11e-33

Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320672  Cd Length: 258  Bit Score: 134.66  E-value: 1.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTGPMRF 2481
Cdd:cd16006   30 RGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIFAGLLHFFFLAAFAWMCLEGVQLYLMLVEVFESEYSRKKY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYILA----ARASCAAQRQGFEKKG 2557
Cdd:cd16006  110 YYVAGYLFPATVVGVSAAIDYKSYGTEKACWLRVDNYFIWSFIGPVTFIILLNLIFLVITlckmVKHSNTLKPDSSRLEN 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13325064 2558 PVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRK 2618
Cdd:cd16006  190 IKSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFTIFNAFQGMFIFIFHCALQKKVRK 250
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
293-395 2.63e-32

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 125.50  E-value: 2.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  293 EYKESLRENLEVGYEVLTVRATDGDAPPNANILYRLLegsGGSPSEVFEIDPRSGVIRTRGPVDREEVESYQLTVEASDQ 372
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIV---SGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATDG 77
                         90       100
                 ....*....|....*....|...
gi 13325064  373 GrdPGPRSTTAAVFLSVEDDNDN 395
Cdd:cd11304   78 G--GPPLSSTATVTITVLDVNDN 98
7tmB2_GPR133 cd15256
orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G ...
2404-2621 7.59e-32

orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR133 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR144. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320384  Cd Length: 260  Bit Score: 129.27  E-value: 7.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2404 LRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTGPMRFYY 2483
Cdd:cd15256   35 IRNQRYHIHANLSFAVLVAQILLLISFRFEPGTLPCKIMAILLHFFFLSAFAWMLVEGLHLYSMVIKVFGSEESKHFYYY 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2484 MLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYILAARASCAAQRQGFEKKG------ 2557
Cdd:cd15256  115 GIGWGSPLLICIISLTSALDSYGESDNCWLSLENGAIWAFVAPALFVIVVNIGILIAVTRVISRISADNYKVHGdanafk 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13325064 2558 ----------PVSGLQPSFAVllllsatwllalLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRKALK 2621
Cdd:cd15256  195 ltakavavllPILGSSWVFGV------------LAVNTHALVFQYMFAIFNSLQGFFIFLFHCLLNSEVRAAFK 256
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
716-811 8.91e-32

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 123.96  E-value: 8.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  716 HYTVNVNEDRPAGTTVVLISATDEDTGENARITYFMEDSIPQ--FRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIP 793
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDglFSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGGP 80
                         90
                 ....*....|....*...
gi 13325064  794 QKSDTTYLEILVNDVNDN 811
Cdd:cd11304   81 PLSSTATVTITVLDVNDN 98
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
819-917 1.36e-30

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 120.50  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  819 SYQGSVYEDVPPFTSVLQISATDRDSGLNGRVFYTFQGGDDGDGdFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGM 898
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGL-FSIDPSTGEITTAKPLDREEQSSYTLTVTATDGGG 79
                         90
                 ....*....|....*....
gi 13325064  899 PPARTPMEVTVTVLDVNDN 917
Cdd:cd11304   80 PPLSSTATVTITVLDVNDN 98
7tmB2_EMR_Adhesion_II cd15931
EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of ...
2402-2621 9.29e-30

EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. On the other hand, EMR2 generates four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320597  Cd Length: 262  Bit Score: 123.39  E-value: 9.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTG---- 2477
Cdd:cd15931   30 RWIPKINTTAHLHLCLCLSMSHTLFLAGIEYVENELACTVMAGLLHYLFLASFVWMLLEALQLHLLVRRLTKVQVIqrdg 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2478 -PMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYIlaarASCAAQRQGFEKK 2556
Cdd:cd15931  110 lPRPLLCLIGYGVPFLIVGVSALVYSDGYGEAKMCWLSQERGFNWSFLGPVIAIIGINWILFC----ATLWCLRQTLSNM 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13325064 2557 GP-VSGLQPSFAVLLLLSATWLLALLS-------VNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRKALK 2621
Cdd:cd15931  186 NSdISQLKDTRLLTFKAVAQLFILGCTwvlglfqTNPVALVFQYLFTILNSLQGAFLFLVHCLLNKEVREEYI 258
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
925-1019 9.58e-30

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 118.18  E-value: 9.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  925 EFDVFVEENSPIGLAVARVTATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQAT---SA 1001
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDSGENGEVTYSIVSGNEDGLFSIDPSTGEITTAKPLDREEQSSYTLTVTATdggGP 80
                         90
                 ....*....|....*...
gi 13325064 1002 PLVSRATVHVRLLDRNDN 1019
Cdd:cd11304   81 PLSSTATVTITVLDVNDN 98
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1369-1552 4.55e-29

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058  Cd Length: 151  Bit Score: 117.90  E-value: 4.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1369 TRSFPAHSFITFRGLR-QRFHFTLALSFATKERDGLLLYNGRFNeKHDFVALEVIQEQVQLTFSAGESTTTVSPFVPggV 1447
Cdd:cd00110    1 GVSFSGSSYVRLPTLPaPRTRLSISFSFRTTSPNGLLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--L 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1448 SDGQWHTVQLKYYNkpllgqtglpqgpseqKVAVVTVDGCDTgvalrfgsvlgnyscaAQGTQGGSKKSLDLTGPLLLGG 1527
Cdd:cd00110   78 NDGQWHSVSVERNG----------------RSVTLSVDGERV----------------VESGSPGGSALLNLDGPLYLGG 125
                        170       180
                 ....*....|....*....|....*.
gi 13325064 1528 VPDLPESFPVRMRQ-FVGCMRNLQVD 1552
Cdd:cd00110  126 LPEDLKSPGLPVSPgFVGCIRDLKVN 151
7tmB2_GPR144 cd15255
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
2376-2621 9.25e-29

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR144 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR133. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320383  Cd Length: 263  Bit Score: 120.34  E-value: 9.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2376 LKTLTYVALGVTLAALLLTFFFLTLLRILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFS 2455
Cdd:cd15255    4 LRTLSFIGCGVSLCALIVTFILFLAVGVPKSERTTVHKNLIFALAAAEFLLMFSEWAKGNQVACWAVTALLHLFFLAAFS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2456 WALLEALHLYRALTEVRDVNTGPMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSV 2535
Cdd:cd15255   84 WMLVEGLLLWSKVVAVNMSEDRRMKFYYVTGWGLPVVIVAVTLATSFNKYVADQHCWLNVQTDIIWAFVGPVLFVLTVNT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2536 FLYILAARASCAAQRQGFEKKGPVSGLQPSFAVLLLLSATWLLALLSVNSDT----LLFH------YLFATCNCIQGPFI 2605
Cdd:cd15255  164 FVLFRVVMVTVSSARRRAKMLTPSSDLEKQIGIQIWATAKPVLVLLPVLGLTwlcgVLVHlsdvwaYVFITLNSFQGLYI 243
                        250
                 ....*....|....*.
gi 13325064 2606 FLSYVVLSKEVRKALK 2621
Cdd:cd15255  244 FLVYAIYNSEVRNAIQ 259
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
422-503 3.02e-27

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 110.52  E-value: 3.02e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     422 TASDRDKGSNAVVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRVRAQDGGRPPLSNVSgLVTVQVLDINDN 501
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTA-TVTITVLDVNDN 79

                    ..
gi 13325064     502 AP 503
Cdd:smart00112   80 AP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
528-608 1.14e-26

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 108.59  E-value: 1.14e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     528 QAIDADAGDNARLEYRLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTPALTASASVSVTVLDVNDNN 607
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80

                    .
gi 13325064     608 P 608
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
404-496 3.65e-26

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 107.39  E-value: 3.65e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    404 YVVQVREDVTPGAPVLRVTASDRDKGSNAVVHYSIMSGNARGQFYLDAQTGALDVVSPLDYETTKEYTLRVRAQDGGRPP 483
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|...
gi 13325064    484 LSNVsGLVTVQVL 496
Cdd:pfam00028   81 LSST-ATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
735-813 7.40e-26

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 106.28  E-value: 7.40e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     735 SATDEDTGENARITYFMEDSIPQ--FRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIPQKSDTTYLEILVNDVNDNA 812
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDglFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDNA 80

                    .
gi 13325064     813 P 813
Cdd:smart00112   81 P 81
7tmB2_GPR124-like_Adhesion_III cd15259
orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of ...
2402-2624 1.35e-24

orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group III adhesion GPCRs include orphan GPR123, GPR124, GPR125, and their closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. GPR123 is predominantly expressed in the CNS including thalamus, brainstem and regions containing large pyramidal cells. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 also interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Furthermore, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl.


Pssm-ID: 320387  Cd Length: 260  Bit Score: 107.85  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRrNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNTG---- 2477
Cdd:cd15259   34 RISRKGRHMLV-NLCLHLLLTCVVFVGGINRTANQLVCQAVGILLHYSTLCTLLWVGVTARNMYKQVTKTAKPPQDedqp 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2478 -----PMRFYYMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSiYDTLIWSFAGPVAFAVSMSVFLYIlaaRASCAAQRQG 2552
Cdd:cd15259  113 prppkPMLRFYLIGWGIPLIICGITAAVNLDNYSTYDYCWLA-WDPSLGAFYGPAALIVLVNCIYFL---RIYCQLKGAP 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13325064 2553 FEkkgPVSGLQPSFAVLLLLSATWLLALLSVNSD---TLLFHYLFATCNCIQGPFIFLSYVVLSKEVRKALKLAC 2624
Cdd:cd15259  189 VS---FQSQLRGAVITLFLYVAMWACGALAVSQRyflDLVFSCLYGATCSSLGLFVLIHHCLSREDVRQSWRQCC 260
7tmB2_ETL cd15437
Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; ...
2404-2617 1.38e-24

Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; member of the class B2 family of seven-transmembrane G protein-coupled receptors; ETL (EGF-TM7-latrophilin-related protein) belongs to Group I adhesion GPCRs, which also include latrophilins (also called lectomedins or latrotoxin receptors). All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. ETL, for instance, contains EGF-like repeats, which also present in other EGF-TM7 adhesion GPCRs, such as Cadherin EGF LAG seven-pass G-type receptors (CELSR1-3), EGF-like module receptors (EMR1-3), CD97, and Flamingo. ETL is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320553  Cd Length: 258  Bit Score: 107.65  E-value: 1.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2404 LRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVRdVNTGPM-RFY 2482
Cdd:cd15437   32 IQSTRTTIHKNLCCSLFLAELIFLIGINMNANKLFCSIIAGLLHYFFLAAFAWMCIEGIHLYLIVVGVI-YNKGFLhKNF 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2483 YMLGWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGP---------VAFAVSM-SVFLY--ILAARASCAAQR 2550
Cdd:cd15437  111 YIFGYGSPAVVVGISAALGYKYYGTTKVCWLSTENNFIWSFIGPacliilvnlLAFGVIIyKVFRHtaMLKPEVSCYENI 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13325064 2551 QgfekkgpvSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVR 2617
Cdd:cd15437  191 R--------SCARGALALLFLLGATWIFGVLHVVYGSVVTAYLFTISNAFQGMFIFIFLCVLSRKIQ 249
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
312-397 6.00e-24

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 100.89  E-value: 6.00e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     312 RATDGDAPPNANILYRLLegsGGSPSEVFEIDPRSGVIRTRGPVDREEVESYQLTVEASDQGrdPGPRSTTAAVFLSVED 391
Cdd:smart00112    1 SATDADSGENGKVTYSIL---SGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGG--GPPLSSTATVTITVLD 75

                    ....*.
gi 13325064     392 DNDNAP 397
Cdd:smart00112   76 VNDNAP 81
Cadherin pfam00028
Cadherin domain;
510-601 8.62e-24

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 100.84  E-value: 8.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    510 FQATVLESVPLGYLVLHVQAIDADAGDNARLEYRLAGVGHDFPFTINNGTGWISVAAELDREEVDFYSFGVEARDHGTPA 589
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|..
gi 13325064    590 LTASASVSVTVL 601
Cdd:pfam00028   81 LSSTATVTITVL 92
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
838-919 9.68e-24

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 100.12  E-value: 9.68e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     838 SATDRDSGLNGRVFYTFqGGDDGDGDFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGMPPARTPMEVTVTVLDVNDN 917
Cdd:smart00112    1 SATDADSGENGKVTYSI-LSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVNDN 79

                    ..
gi 13325064     918 PP 919
Cdd:smart00112   80 AP 81
LamG smart00282
Laminin G domain;
1390-1554 1.87e-23

Laminin G domain;


Pssm-ID: 214598  Cd Length: 132  Bit Score: 100.88  E-value: 1.87e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    1390 TLALSFATKERDGLLLYNGrFNEKHDFVALEVIQEQVQLTFSAGESTTTVSPfVPGGVSDGQWHTVQLKYynkpllgqtg 1469
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAG-SKGGGDYLALELRDGRLVLRYDLGSGPARLTS-DPTPLNDGQWHRVAVER---------- 68
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    1470 lpqgpsEQKVAVVTVDGCDtgvalrfgsvlgnyscAAQGTQGGSKKSLDLTGPLLLGGVPDLPESFPVRMRQ-FVGCMRN 1548
Cdd:smart00282   69 ------NGRSVTLSVDGGN----------------RVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPgFRGCIRN 126

                    ....*.
gi 13325064    1549 LQVDSR 1554
Cdd:smart00282  127 LKVNGK 132
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
204-287 2.53e-23

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 98.96  E-value: 2.53e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     204 RAIDPDEGEAGRLEYTmdaLFDSRSNQFFSLDPVTGAVTTAEELDRETKSTHVFRVTAQDHGMPRRSALATLTILVTDTN 283
Cdd:smart00112    1 SATDADSGENGKVTYS---ILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATDGGGPPLSSTATVTITVLDVN 77

                    ....
gi 13325064     284 DHDP 287
Cdd:smart00112   78 DNAP 81
CA smart00112
Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. ...
944-1021 3.71e-23

Cadherin repeats; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. Cadherin domains occur as repeats in the extracellular regions which are thought to mediate cell-cell contact when bound to calcium.


Pssm-ID: 214520  Cd Length: 81  Bit Score: 98.58  E-value: 3.71e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064     944 TATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQAT---SAPLVSRATVHVRLLDRNDNP 1020
Cdd:smart00112    1 SATDADSGENGKVTYSILSGNDDGLFSIDPETGEITTTKPLDREEQPEYTLTVEATdggGPPLSSTATVTITVLDVNDNA 80

                    .
gi 13325064    1021 P 1021
Cdd:smart00112   81 P 81
Cadherin pfam00028
Cadherin domain;
297-390 1.22e-22

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 97.37  E-value: 1.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    297 SLRENLEVGYEVLTVRATDGDAPPNANILYRLLegsGGSPSEVFEIDPRSGVIRTRGPVDREEVESYQLTVEASDQGrdP 376
Cdd:pfam00028    4 SVPENAPVGTEVLTVTATDPDLGPNGRIFYSIL---GGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSG--G 78
                           90
                   ....*....|....
gi 13325064    377 GPRSTTAAVFLSVE 390
Cdd:pfam00028   79 PPLSSTATVTITVL 92
Cadherin_repeat cd11304
Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell ...
614-708 1.68e-22

Cadherin tandem repeat domain; Cadherins are glycoproteins involved in Ca2+-mediated cell-cell adhesion. The cadherin repeat domains occur as tandem repeats in the extracellular regions, which are thought to mediate cell-cell contact when bound to calcium. They play numerous roles in cell fate, signalling, proliferation, differentiation, and migration; members include E-, N-, P-, T-, VE-, CNR-, proto-, and FAT-family cadherin, desmocollin, and desmoglein, a large variety of domain architectures with varying repeat copy numbers. Cadherin-repeat containing proteins exist as monomers, homodimers, or heterodimers.


Pssm-ID: 206637  Cd Length: 98  Bit Score: 97.00  E-value: 1.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064  614 EYTVRLNEDAAVGTSVVTVSAVDRD--AHSVITYQITSGNTRNRFSITSQSggGLVSLALPLDYKLERQYVLAVTASDG- 690
Cdd:cd11304    1 SYEVSVPENAPPGTVVLTVSATDPDsgENGEVTYSIVSGNEDGLFSIDPST--GEITTAKPLDREEQSSYTLTVTATDGg 78
                         90       100
                 ....*....|....*....|
gi 13325064  691 --TRQDTAQIVVNVTDANTH 708
Cdd:cd11304   79 gpPLSSTATVTITVLDVNDN 98
7tmB3_Methuselah-like cd15039
Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G ...
2404-2625 9.75e-22

Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G protein-coupled receptors; The subfamily B3 of class B GPCRs consists of Methuselah (Mth) and its closely related proteins found in bilateria. Mth was originally identified in Drosophila as a GPCR affecting stress resistance and aging. In addition to the seven transmembrane helices, Mth contains an N-terminal extracellular domain involved in ligand binding, and a third intracellular loop (IC3) required for the specificity of G-protein coupling. Drosophila Mth mutants showed an increase in average lifespan by 35% and greater resistance to a variety of stress factors, including starvation, high temperature, and paraquat-induced oxidative toxicity. Moreover, mutations in two endogenous peptide ligands of Methuselah, Stunted A and B, showed an increased in lifespan and resistance to oxidative stress induced by dietary paraquat. These results strongly suggest that the Stunted-Methuselah system plays important roles in stress response and aging.


Pssm-ID: 320167  Cd Length: 270  Bit Score: 99.22  E-value: 9.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2404 LRsNQHG-IRRNLTAALGLAQLVFLLGINQADL-PFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVR----DVNTG 2477
Cdd:cd15039   32 LR-NLHGkCLMCLVLSLFVAYLLLLIGQLLSLGdSTLCVALGILLHFFFLAAFFWLNVMSFDIWRTFRSKRssssRSKER 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2478 PMRFYYML-GWGVPAFITGLAVGLD---PEGYGNPDF----CWLSIYDTLIWSFAGPVAFAVSMSVFLYILAARASCAAQ 2549
Cdd:cd15039  111 KRFLRYSLyAWGVPLLLVAVTIIVDfspPTDSLRPGYgegsCWISNPWALLLYFYGPVALLLLFNIILFILTAIRIRKVK 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2550 R--QGFEKKGP--------------VSGLQPSFAVLLLLsatwllallsVNSDTLLFhYLFATCNCIQGPFIFLSYvVLS 2613
Cdd:cd15039  191 KetAKVQSRLRsdkqrfrlylklfvIMGVTWILEIISWF----------VGGSSVLW-YIFDILNGLQGVFIFLIF-VCK 258
                        250
                 ....*....|..
gi 13325064 2614 KEVRKALKLACS 2625
Cdd:cd15039  259 RRVLRLLKKKIR 270
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1395-1554 1.30e-21

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 308045  Cd Length: 126  Bit Score: 95.58  E-value: 1.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   1395 FATKERDGLLLYNGrfNEKHDFVALEVIQEQVQLTFSAGESTTTVSPFvPGGVSDGQWHTVQLKYynkpllgqtglpqgp 1474
Cdd:pfam02210    1 FRTTQPNGLLLYAG--GGGSDFLALELVDGRLVLRYDLGSGPVSLLSS-GKPLNDGQWHRVRVSR--------------- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   1475 sEQKVAVVTVDGCDTgvalrfgsvlgnyscaAQGTQGGSKKSLDLTGPLLLGGVP-DLPESFPVRMRQFVGCMRNLQVDS 1553
Cdd:pfam02210   63 -NGRTLTLSVDGQTV----------------VSALPPGESLLLNLNGPLYLGGLPpLLLLPALPVTEGFVGCIRDVRVNG 125

                   .
gi 13325064   1554 R 1554
Cdd:pfam02210  126 E 126
Cadherin pfam00028
Cadherin domain;
186-280 1.67e-21

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 93.90  E-value: 1.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    186 YQATVPENQPAGTPVASLRAIDPDEGEAGRLEYTMdaLFDSRSNQFfSLDPVTGAVTTAEELDRETKSTHVFRVTAQDHG 265
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSI--LGGGPGGNF-RIDPDTGDISTTKPLDRESIGEYELTVEATDSG 77
                           90
                   ....*....|....*
gi 13325064    266 MPRRSALATLTILVT 280
Cdd:pfam00028   78 GPPLSSTATVTITVL 92
Cadherin pfam00028
Cadherin domain;
717-805 2.80e-21

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 93.52  E-value: 2.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    717 YTVNVNEDRPAGTTVVLISATDEDTGENARITYFM--EDSIPQFRIDADTGAVTTQAELDYEDQVSYTLAITARDNGIPQ 794
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSIlgGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGPP 80
                           90
                   ....*....|.
gi 13325064    795 KSDTTYLEILV 805
Cdd:pfam00028   81 LSSTATVTITV 91
7tmB2_GPR126-like_Adhesion_VIII cd15258
orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family ...
2411-2618 2.89e-21

orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Group VIII adhesion GPCRs include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. GPR126, on the other hand, is required for Schwann cells, but not oligodendrocyte myelination in the peripheral nervous system. Gpr64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also overexpressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320386  Cd Length: 267  Bit Score: 97.87  E-value: 2.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2411 IRRNLTAALGLAQLVFLL--GINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVrdVNTGPMRFYY---ML 2485
Cdd:cd15258   40 IHMNLCAALLLLNLAFLLssWIASFGSDGLCIAVAVALHYFLLACLTWMGLEAFHLYLLLVKV--FNTYIRRYILklcLV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2486 GWGVPAFITGLAVGLDPEGYG-----------NPDFCWlsIYDTLIWSFA----GPVAFAVSMSVFLYILAARASCAAQR 2550
Cdd:cd15258  118 GWGLPALLVTLVLSVRSDNYGpitipngegfqNDSFCW--IRDPVVFYITvvgyFGLTFLFNMVMLATVLVQICRLREKA 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13325064 2551 QGFEKKGPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRK 2618
Cdd:cd15258  196 QATPRKRALHDLLTLLGLTFLLGLTWGLAFFAWGPFNLPFLYLFAIFNSLQGFFIFIWYCSMKENVRK 263
7tmB2_GPR64 cd15444
orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B ...
2402-2621 8.21e-21

orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B secretin-like receptors of seven-transmembrane G protein-coupled receptors; GPR64 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR97, GPR112, GPR114, and GPR126. GPR64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also overexpressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320560  Cd Length: 271  Bit Score: 96.43  E-value: 8.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQA---DLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVrdVNTGP 2478
Cdd:cd15444   31 KIRRDYPSKILIQLCVALLLLNLVFLLDSWIAlykDIVGLCISVAVFLHYFLLVSFTWMGLEAFHMYLALVKV--FNTYI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2479 MRF---YYMLGWGVPAFITGLAVGLDPEGYG-----------NPDFCWLS----IYDTLIWSFAgpVAFAVSMSVFLYIL 2540
Cdd:cd15444  109 RKYilkFCIVGWGVPAVVVAIVLAVSKDNYGlgsygkspngsTDDFCWINnnivFYITVVGYFC--VIFLLNISMFIVVL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2541 AARASCAAQRQ-GFEKKGPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRKA 2619
Cdd:cd15444  187 VQLCRIKKQKQlGAQRKTSLQDLRSVAGITFLLGITWGFAFFAWGPVNLAFMYLFAIFNTLQGFFIFIFYCVAKENVRKQ 266

                 ..
gi 13325064 2620 LK 2621
Cdd:cd15444  267 WR 268
Cadherin pfam00028
Cadherin domain;
820-912 8.40e-21

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 91.98  E-value: 8.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    820 YQGSVYEDVPPFTSVLQISATDRDSGLNGRVFYTFQGGDDGDGdFIVESTSGIVRTLRRLDRENVAQYVLRAYAVDKGMP 899
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGN-FRIDPDTGDISTTKPLDRESIGEYELTVEATDSGGP 79
                           90
                   ....*....|...
gi 13325064    900 PARTPMEVTVTVL 912
Cdd:pfam00028   80 PLSSTATVTITVL 92
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
2402-2621 1.59e-20

brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediate direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320379  Cd Length: 253  Bit Score: 95.40  E-value: 1.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALtevrdvnTGPMRF 2481
Cdd:cd15251   31 RYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTMTAAFLHFFFLSSFCWVLTEAWQSYMAV-------TGRMRT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 ------YYMLGWGVPAFITGLAVGLD-PEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYILAARASCAaqRQGFE 2554
Cdd:cd15251  104 rlirkrFLCLGWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVS--RDGIS 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13325064 2555 KKGPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRKALK 2621
Cdd:cd15251  182 DNAMASLWSSCVVLPLLALTWMSAVLAMTDRRSVLFQILFAVFDSLQGFVIVMVHCILRREVQDAVK 248
Cadherin pfam00028
Cadherin domain;
926-1014 4.52e-20

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 90.05  E-value: 4.52e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    926 FDVFVEENSPIGLAVARVTATDPDEGTNAQIMYQIVEGNIPEVFQLDIFSGELTALVDLDYEDRPEYVLVIQATSA---P 1002
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDLGPNGRIFYSILGGGPGGNFRIDPDTGDISTTKPLDRESIGEYELTVEATDSggpP 80
                           90
                   ....*....|..
gi 13325064   1003 LVSRATVHVRLL 1014
Cdd:pfam00028   81 LSSTATVTITVL 92
7tmB2_BAI2 cd15988
brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 ...
2402-2621 5.59e-20

brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320654  Cd Length: 291  Bit Score: 94.25  E-value: 5.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALteVRDVNTGPMRF 2481
Cdd:cd15988   31 RFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTMTAAFLHFFFLSSFCWVLTEAWQSYLAV--IGRMRTRLVRK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYM-LGWGVPAFITGLAVGLD-PEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYI-----LAARASCA----AQR 2550
Cdd:cd15988  109 RFLcLGWGLPALVVAVSVGFTrTKGYGTASYCWLSLEGGLLYAFVGPAAVIVLVNMLIGIivfnkLMSRDGISdkskKQR 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2551 QGFEK--------KGPVSGLQPSFAVLLLLSATWLLALLS-------------------VNSDTLLFHYLFATCNCIQGP 2603
Cdd:cd15988  189 AGSEAepcsslllKCSKCGVVSSAAMSSATASSAMASLWSscvvlpllaltwmsavlamTDRRSILFQVLFAVFNSVQGF 268
                        250
                 ....*....|....*...
gi 13325064 2604 FIFLSYVVLSKEVRKALK 2621
Cdd:cd15988  269 VIITVHCFLRREVQDVVK 286
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
1618-1767 1.16e-19

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058  Cd Length: 151  Bit Score: 90.56  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 1618 HFLGSSLVAWHGLSLPiSQPWYLSLMFRTRQADGVLLQAITRGRS-TITLQLREGHVMLSVEGTglqASSLRLEPGRA-N 1695
Cdd:cd00110    3 SFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLG---SGSLVLSSKTPlN 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13325064 1696 DGDWHHAQLALGASggpgHAILSFDyGQQRAEGNLGPRLHGLHL-SNITVGGIPG----PAGGVARGFRGCLQGVRV 1767
Cdd:cd00110   79 DGQWHSVSVERNGR----SVTLSVD-GERVVESGSPGGSALLNLdGPLYLGGLPEdlksPGLPVSPGFVGCIRDLKV 150
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
2315-2368 2.97e-19

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 86.29  E-value: 2.97e-19
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 13325064    2315 TKPICVFWNHSilvsgTGGWSARGCEVVFRNESHVSCQCNHMTSFAVLMDVSRR 2368
Cdd:smart00303    1 FNPICVFWDES-----SGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
7tmB2_GPR112 cd15997
Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane ...
2414-2618 3.40e-19

Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR112 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR114, and GPR126. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320663  Cd Length: 269  Bit Score: 91.65  E-value: 3.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2414 NLTAALGLAQLVFLL-----GINQADLpfaCTVIAILLHFLYLCTFSWALLEALHLYRALTEVRDVNtgpMRFYY----M 2484
Cdd:cd15997   43 NLCTALLMLNLVFLLnswlsSFNNYGL---CITVAAFLHYFLLASFTWMGLEAVHMYFALVKVFNIY---IPNYIlkfcI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2485 LGWGVPAFITGLAVGLDPEGYGN----------PDFCWLS----IYDTLIWSFAgpVAFAVSMSVFLYILAARASCAAQR 2550
Cdd:cd15997  117 AGWGIPAVVVALVLAINKDFYGNelssdslhpsTPFCWIQddvvFYISVVAYFC--LIFLCNISMFITVLIQIRSMKAKK 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13325064 2551 Q-GFEKKGPVSGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRK 2618
Cdd:cd15997  195 PsRNWKQGFLHDLKSVASLTFLLGLTWGFAFFAWGPVRIFFLYLFSICNTLQGFFIFVFHCLMKENVRK 263
7tmB2_BAI1 cd15990
brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 ...
2402-2621 8.89e-19

brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320656  Cd Length: 267  Bit Score: 90.05  E-value: 8.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEvRDVNTGPMRF 2481
Cdd:cd15990   34 RYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTG-RLRNRIIRKR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYMLGWGVPAFITGLAVGL-DPEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYILAARASCA----AQRQGFEKK 2556
Cdd:cd15990  113 FLCLGWGLPALVVAISVGFtKAKGYGTVNYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNKLVSkdgiTDKKLKERA 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13325064 2557 GpvSGLQPSFAVLLLLSATWLLALLSV-NSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRKALK 2621
Cdd:cd15990  193 G--ASLWSSCVVLPLLALTWMSAVLAItDRRSALFQILFAVFDSLEGFVIVMVHCILRREVQDAVK 256
LamG smart00282
Laminin G domain;
1639-1767 1.38e-18

Laminin G domain;


Pssm-ID: 214598  Cd Length: 132  Bit Score: 86.62  E-value: 1.38e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    1639 YLSLMFRTRQADGVLLQAITRGRS-TITLQLREGHVMLSVEgTGLQASSLRLEPGRANDGDWHHAQLALGASggpgHAIL 1717
Cdd:smart00282    1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYD-LGSGPARLTSDPTPLNDGQWHRVAVERNGR----SVTL 75
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 13325064    1718 SFDYG-QQRAEGNLGPRLHGLHlSNITVGGIPG----PAGGVARGFRGCLQGVRV 1767
Cdd:smart00282   76 SVDGGnRVSGESPGGLTILNLD-GPLYLGGLPEdlklPPLPVTPGFRGCIRNLKV 129
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
1644-1770 3.22e-17

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 308045  Cd Length: 126  Bit Score: 82.48  E-value: 3.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   1644 FRTRQADGVLLQAITRGRSTITLQLREGHVMLSVEgTGLQASSLRLEPGRANDGDWHHAQLALgasgGPGHAILSFDYGQ 1723
Cdd:pfam02210    1 FRTTQPNGLLLYAGGGGSDFLALELVDGRLVLRYD-LGSGPVSLLSSGKPLNDGQWHRVRVSR----NGRTLTLSVDGQT 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 13325064   1724 QRAEGNLGPRLHGLHLSNITVGGIPGP----AGGVARGFRGCLQGVRVSDT 1770
Cdd:pfam02210   76 VVSALPPGESLLLNLNGPLYLGGLPPLlllpALPVTEGFVGCIRDVRVNGE 126
Cadherin pfam00028
Cadherin domain;
615-703 4.48e-17

Cadherin domain;


Pssm-ID: 278457  Cd Length: 92  Bit Score: 81.19  E-value: 4.48e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    615 YTVRLNEDAAVGTSVVTVSAVDRD--AHSVITYQITSGNTRNRFSITSQSggGLVSLALPLDYKLERQYVLAVTASDG-- 690
Cdd:pfam00028    1 YSASVPENAPVGTEVLTVTATDPDlgPNGRIFYSILGGGPGGNFRIDPDT--GDISTTKPLDRESIGEYELTVEATDSgg 78
                           90
                   ....*....|....
gi 13325064    691 -TRQDTAQIVVNVT 703
Cdd:pfam00028   79 pPLSSTATVTITVL 92
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
2317-2362 1.81e-16

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


Pssm-ID: 307782  Cd Length: 46  Bit Score: 78.18  E-value: 1.81e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 13325064   2317 PICVFWNHSILvSGTGGWSARGCEVVF-RNESHVSCQCNHMTSFAVL 2362
Cdd:pfam01825    1 PQCVFWDFDTG-SGTGGWSTEGCELVTsSNDTHTVCSCNHLTSFAVL 46
HormR smart00008
Domain present in hormone receptors;
1972-2034 1.86e-16

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 78.71  E-value: 1.86e-16
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064    1972 NYDSCPRAIEAGIWWPRTRFGLPAAAPCPKGSFG-----TAVRHCDEHRGWLP--PNLFNCTSITFSELK 2034
Cdd:smart00008    1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGfsyktGASRNCTENGGWSPpfPNYSNCTSNDYEELK 70
7tmB2_GPR126 cd15996
orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G ...
2402-2618 2.14e-16

orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR126 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, and GPR114. GPR126 is required in Schwann cells for proper differentiation and myelination via G-Protein Activation. GPR126 is believed to couple to G(s)-protein, which leads to activation of adenylate cyclase for cAMP production. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320662  Cd Length: 271  Bit Score: 82.63  E-value: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLG--INQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEVrdVNTGPM 2479
Cdd:cd15996   31 KLRRDYPSKILMNLSTALLFLNLVFLLDgwIASFEIDELCITVAVLLHFFLLATFTWMGLEAIHMYIALVKV--FNTYIR 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2480 RF---YYMLGWGVPAFITGLAV------------GLDPEGYGNPDFCWLS----IYDTLIWSFAgpVAFAVSMSVFLYIL 2540
Cdd:cd15996  109 RYilkFCIIGWGLPALIVSIVLastndnygygyyGKDKDGQGGDEFCWIKnpvvFYVTCAAYFG--IMFLMNVAMFIVVM 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13325064 2541 AARASCAAQRQGFEKKGPV-SGLQPSFAVLLLLSATWLLALLSVNSDTLLFHYLFATCNCIQGPFIFLSYVVLSKEVRK 2618
Cdd:cd15996  187 VQICGRNGKRSNRTLREEIlRNLRSVVSLTFLLGMTWGFAFFAWGPVNLAFMYLFTIFNSLQGLFIFVFHCALKENVQK 265
7tmB2_BAI3 cd15989
brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 ...
2402-2621 5.24e-16

brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320655  Cd Length: 293  Bit Score: 81.65  E-value: 5.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2402 RILRSNQHGIRRNLTAALGLAQLVFLLGINQADLPFACTVIAILLHFLYLCTFSWALLEALHLYRALTEvrDVNTGPMRF 2481
Cdd:cd15989   33 RYIRSERSIILINFCLSIISSNILILVGQTQTHNKGICTMTTAFLHFFFLASFCWVLTEAWQSYMAVTG--KIRTRLIRK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2482 YYM-LGWGVPAFITGLAVGLD-PEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMSVFLYILAARAscAAQRQGFEKKG-- 2557
Cdd:cd15989  111 RFLcLGWGLPALVVAISMGFTkAKGYGTPHYCWLSLEGGLLYAFVGPAAAVVLVNMVIGILVFNK--LVSRDGILDKKlk 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2558 --------PVSGLQPSFAVLLLLSATWLLALLSVNS----------------------------DTLLFHYLFATCNCIQ 2601
Cdd:cd15989  189 hragqmsePHSGLTLKCAKCGVVSTTALSATTASNAmaslwsscvvlpllaltwmsavlamtdkRSILFQILFAVFDSLQ 268
                        250       260
                 ....*....|....*....|
gi 13325064 2602 GPFIFLSYVVLSKEVRKALK 2621
Cdd:cd15989  269 GFVIVMVHCILRREVQDAFR 288
Laminin_G_1 pfam00054
Laminin G domain;
1395-1557 7.48e-16

Laminin G domain;


Pssm-ID: 278483  Cd Length: 131  Bit Score: 78.90  E-value: 7.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   1395 FATKERDGLLLYNGRfNEKHDFVALEVIQEQVQLTFSAGESTTTVSPfvPGGVSDGQWHTVQLKYynkpllgqtglpqgp 1474
Cdd:pfam00054    1 FRTTEPSGLLLYNGT-QTERDFLALELRDGRLEVSYDLGSGAAVVRS--GDKLNDGKWHSVELER--------------- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064   1475 sEQKVAVVTVDGCDtgvalrfgSVLGNYScaaqgtqGGSKKSLDLTGPLLLGGVPDLPESFP--VRMRQFVGCMRNLQVD 1552
Cdd:pfam00054   63 -NGRSGTLSVDGEA--------RPTGESP-------LGATTDLDVDGPLYVGGLPSLGVKKRrlAISPSFDGCIRDVIVN 126

                   ....*
gi 13325064   1553 SRHID 1557
Cdd:pfam00054  127 GKPLD 131
7tmB2_GPR128 cd15257
orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G ...
2439-2626 9.74e-16

orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR128 is an orphan receptor of the adhesion family (subclass B2) that belongs to the class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance, as its knockout mice showed a decrease in body weight gain and an increase in intestinal contraction frequency compared to wild-type controls. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320385  Cd Length: 303  Bit Score: 80.69  E-value: 9.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2439 CTVIAILLHFLYLCTFSWALLEALHLYRALteVRDVNTGP---MRFYYMLGWGVPAFITGLAVG----------LDPEGY 2505
Cdd:cd15257   93 CTAVAALLHYFLLVTFMWNAVYSAQLYLLL--IRMMKPLPemfILQASAIGWGIPAVVVAITLGatyrfptslpVFTRTY 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13325064 2506 GNPDFCWLSIYDT-------LIWSFAGPVAFAVSMSVFLYILAARASCAAQRQ-------GFEKK-------GPVSGLQP 2564
Cdd:cd15257  171 RQEEFCWLAALDKnfdikkpLLWGFLLPVGLILITNVILFIMTSQKVLKKNNKklttkkrSYMKKiyitvsvAVVFGITW 250
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13325064 2565 SFAVLLLlsatwllallsVNSDT--LLFHYLFATCNCIQGPFIFLSYVVLSKEVRKALKLACSR 2626
Cdd:cd15257  251 ILGYLML-----------VNNDLskLVFSY