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Conserved domains on  [gi|26352650|dbj|BAC39955|]
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unnamed protein product [Mus musculus]

Protein Classification

Ig domain-containing protein (domain architecture ID 11669380)

protein containing domain Ig

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
165-238 5.80e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653  Cd Length: 85  Bit Score: 60.98  E-value: 5.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650    165 SLQIQEGESLSLVCMADSNPPAVLSWERPTQKP------FQLS---TPAELQLPRAELEDQGKYICQAQNSQGAQTASVS 235
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaesgrFSVSrsgSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 26352650    236 LSI 238
Cdd:smart00410  83 LTV 85
Ig super family cl11960
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
1-45 8.08e-09

Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


The actual alignment was detected with superfamily member cd05712:

Pssm-ID: 353325  Cd Length: 119  Bit Score: 53.19  E-value: 8.08e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 26352650   1 MGKENSHNCSLDIRDAQKIDTGTYFFRLD--GSVKYSFQKSMLSVLV 45
Cdd:cd05712  72 LGDLGKKNCSLLISDAQPEDSGKYFFRVElgDSNKYNFLKNTLSVVV 118
Ig super family cl11960
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
46-125 1.99e-04

Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


The actual alignment was detected with superfamily member pfam08205:

Pssm-ID: 353325  Cd Length: 89  Bit Score: 39.70  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650    46 IALTEVPNIQVTSTLVSGNStKLLCSVPWacEQGTPPIFSWMSSALTSLGHRT-TLSSELNLTPRPQDNGTNLTCQVNLP 124
Cdd:pfam08205   7 ASLLEGEGPEVVATCSSAGG-KPAPRITW--YLNGKPLEAAETSSEQDPESGLyTVTSTLKLVPSRSDHGQSLTCQVSYP 83

                  .
gi 26352650   125 G 125
Cdd:pfam08205  84 A 84
Ig super family cl11960
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
250-320 7.22e-03

Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


The actual alignment was detected with superfamily member cd05758:

Pssm-ID: 353325  Cd Length: 98  Bit Score: 35.59  E-value: 7.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26352650 250 SFEGQGLHCSCSSRAWPAP-SLRWRLGEGVLEGNSSnGSFTVKSSSAGQWANSSLILSMEFSSNHRLS--CEAW 320
Cdd:cd05758  13 AILGEKARLECLVFSSPPPdRIVWSWDEGFLESGSS-GRFSVETFPTEPGVISVLHISGTQRSDFQTSfnCSAW 85
 
Name Accession Description Interval E-value
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
165-238 5.80e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 60.98  E-value: 5.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650    165 SLQIQEGESLSLVCMADSNPPAVLSWERPTQKP------FQLS---TPAELQLPRAELEDQGKYICQAQNSQGAQTASVS 235
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaesgrFSVSrsgSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 26352650    236 LSI 238
Cdd:smart00410  83 LTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
158-225 3.68e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 339005  Cd Length: 79  Bit Score: 52.92  E-value: 3.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352650   158 KVLQSGASLQIQEGESLSLVCMADSNPPAVLSWERPTQKPFQLSTP---------AELQLPRAELEDQGKYICQAQN 225
Cdd:pfam13927   3 VITVSPSSVVVVEGESVTLTCEATGGPPPTITWYKNGEEISSGSTSarisvsgsnSTLTISNVTREDSGTYTCVASN 79
Ig_Siglec_N cd05712
Immunoglobulin (Ig) domain at the N terminus of Siglec (sialic acid-binding Ig-like lectins); ...
1-45 8.08e-09

Immunoglobulin (Ig) domain at the N terminus of Siglec (sialic acid-binding Ig-like lectins); Ig_Siglec_N: immunoglobulin (Ig) domain at the N terminus of Siglec (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 143189  Cd Length: 119  Bit Score: 53.19  E-value: 8.08e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 26352650   1 MGKENSHNCSLDIRDAQKIDTGTYFFRLD--GSVKYSFQKSMLSVLV 45
Cdd:cd05712  72 LGDLGKKNCSLLISDAQPEDSGKYFFRVElgDSNKYNFLKNTLSVVV 118
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
174-235 1.14e-08

Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 51.47  E-value: 1.14e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 174 LSLVCMADSNPPAVLSWER--------PTQKPFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTASVS 235
Cdd:cd00096   1 VTLTCSASGNPPPTITWLKngkplpssSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
46-125 1.99e-04

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 311910  Cd Length: 89  Bit Score: 39.70  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650    46 IALTEVPNIQVTSTLVSGNStKLLCSVPWacEQGTPPIFSWMSSALTSLGHRT-TLSSELNLTPRPQDNGTNLTCQVNLP 124
Cdd:pfam08205   7 ASLLEGEGPEVVATCSSAGG-KPAPRITW--YLNGKPLEAAETSSEQDPESGLyTVTSTLKLVPSRSDHGQSLTCQVSYP 83

                  .
gi 26352650   125 G 125
Cdd:pfam08205  84 A 84
Ig5_KIRREL3-like cd05758
Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known ...
250-320 7.22e-03

Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2) and similar proteins; Ig5_KIRREL3-like: domain similar to the fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 319310  Cd Length: 98  Bit Score: 35.59  E-value: 7.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26352650 250 SFEGQGLHCSCSSRAWPAP-SLRWRLGEGVLEGNSSnGSFTVKSSSAGQWANSSLILSMEFSSNHRLS--CEAW 320
Cdd:cd05758  13 AILGEKARLECLVFSSPPPdRIVWSWDEGFLESGSS-GRFSVETFPTEPGVISVLHISGTQRSDFQTSfnCSAW 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
5-44 8.04e-03

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 336766  Cd Length: 109  Bit Score: 35.90  E-value: 8.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 26352650     5 NSHNCSLDIRDAQKIDTGTYFFRLDGSVKYSFQKSM-LSVL 44
Cdd:pfam07686  69 SNSDFSLTIQNLTPSDSGTYFCAVGPNGEGVFGKGTrLTVL 109
 
Name Accession Description Interval E-value
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
165-238 5.80e-12

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 60.98  E-value: 5.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650    165 SLQIQEGESLSLVCMADSNPPAVLSWERPTQKP------FQLS---TPAELQLPRAELEDQGKYICQAQNSQGAQTASVS 235
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaesgrFSVSrsgSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 26352650    236 LSI 238
Cdd:smart00410  83 LTV 85
IG smart00409
Immunoglobulin;
165-238 5.80e-12

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 60.98  E-value: 5.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650    165 SLQIQEGESLSLVCMADSNPPAVLSWERPTQKP------FQLS---TPAELQLPRAELEDQGKYICQAQNSQGAQTASVS 235
Cdd:smart00409   3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLlaesgrFSVSrsgSTSTLTISNVTPEDSGTYTCAATNSSGSASSGTT 82

                   ...
gi 26352650    236 LSI 238
Cdd:smart00409  83 LTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
158-225 3.68e-09

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 339005  Cd Length: 79  Bit Score: 52.92  E-value: 3.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26352650   158 KVLQSGASLQIQEGESLSLVCMADSNPPAVLSWERPTQKPFQLSTP---------AELQLPRAELEDQGKYICQAQN 225
Cdd:pfam13927   3 VITVSPSSVVVVEGESVTLTCEATGGPPPTITWYKNGEEISSGSTSarisvsgsnSTLTISNVTREDSGTYTCVASN 79
I-set pfam07679
Immunoglobulin I-set domain;
165-238 4.28e-09

Immunoglobulin I-set domain;


Pssm-ID: 336764  Cd Length: 90  Bit Score: 53.02  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650   165 SLQIQEGESLSLVCMADSNPPAVLSWERPTQKP-----FQLSTP---AELQLPRAELEDQGKYICQAQNSQGAQTASVSL 236
Cdd:pfam07679   9 DVEVSEGESARFTCTVTGDPDPEVSWFKDGSPLrsssrFRVTYEggtYTLTISNVQIDDSGKYTCVATNSAGEAEASAEL 88

                  ..
gi 26352650   237 SI 238
Cdd:pfam07679  89 TV 90
Ig_Siglec_N cd05712
Immunoglobulin (Ig) domain at the N terminus of Siglec (sialic acid-binding Ig-like lectins); ...
1-45 8.08e-09

Immunoglobulin (Ig) domain at the N terminus of Siglec (sialic acid-binding Ig-like lectins); Ig_Siglec_N: immunoglobulin (Ig) domain at the N terminus of Siglec (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains (an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains), followed by transmembrane and short cytoplasmic domains. Human siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 143189  Cd Length: 119  Bit Score: 53.19  E-value: 8.08e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 26352650   1 MGKENSHNCSLDIRDAQKIDTGTYFFRLD--GSVKYSFQKSMLSVLV 45
Cdd:cd05712  72 LGDLGKKNCSLLISDAQPEDSGKYFFRVElgDSNKYNFLKNTLSVVV 118
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
174-235 1.14e-08

Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319273  Cd Length: 70  Bit Score: 51.47  E-value: 1.14e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 174 LSLVCMADSNPPAVLSWER--------PTQKPFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTASVS 235
Cdd:cd00096   1 VTLTCSASGNPPPTITWLKngkplpssSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSASASVT 70
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
170-238 1.43e-08

Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death, and protection of the organism against non-self.


Pssm-ID: 143222  Cd Length: 74  Bit Score: 51.09  E-value: 1.43e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26352650 170 EGESLSLVCMADSNPPAVLSWER-----PTQKPFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTASVSLSI 238
Cdd:cd05745   1 EGQTVDFLCEAQGYPQPVIAWTKggsqlSVDRRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
IGc2 smart00408
Immunoglobulin C-2 Type;
170-228 3.72e-08

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 49.71  E-value: 3.72e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26352650    170 EGESLSLVCMADSNPPAVLSWER---PTQKPFQLS-TPAELQLPRAELEDQGKYICQAQNSQG 228
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKdgkPLPESNRFVaSGSTLTIKSVSLEDSGLYTCVAENSAG 63
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
158-237 1.42e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: domain similar to the M5, fifth immunoglobulin (Ig)-like domain from the human titin C terminus. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone, and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching.


Pssm-ID: 143224  Cd Length: 92  Bit Score: 46.19  E-value: 1.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 158 KVLQSGASLQIQEGESLSLVCMADSNPPAVLSWERPTQ-----KPFQLST---PAELQLPRAELEDQGKYICQAQNSQGA 229
Cdd:cd05747   5 TILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQiivssQRHQITSteyKSTFEISKVQMSDEGNYTVVVENSEGK 84

                ....*...
gi 26352650 230 QTASVSLS 237
Cdd:cd05747  85 QEAQFTLT 92
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
171-232 1.48e-06

Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III(FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal act ivity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 319277  Cd Length: 88  Bit Score: 46.00  E-value: 1.48e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352650 171 GESLSLVCMADSNPPAVLSWERPTQKPF----QLSTPAELQLPRAELEDQGKYICQAQNSQGAQTA 232
Cdd:cd04968  16 GQTVTLECFALGNPVPQIKWRKVDGSPSsqwtTSTSEPVLEIPNVQFEDEGTYECEAENSRGKDTV 81
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
171-238 2.60e-06

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig3_NCAM-1_like: domain similar to the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1,and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207  Cd Length: 95  Bit Score: 45.31  E-value: 2.60e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352650 171 GESLSLVCMADSNPPAVLSW-------ERPTQKPFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTASVSLSI 238
Cdd:cd05730  18 GQSVTLACDADGFPEPTMTWtkdgepiESGEEKYSFNEDGSEMTILDVDKLDEAEYTCIAENKAGEQEAEIHLKV 92
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
178-238 2.29e-05

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar to the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 143202  Cd Length: 69  Bit Score: 42.01  E-value: 2.29e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26352650 178 CMADSNPPAVLSWER-----PTQKpFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTASVSLSI 238
Cdd:cd05725   5 CEVGGDPVPTVLWRKedgelPKGR-AEILDDKSLKIRNVTAGDEGSYTCEAENMVGKIEASASLTV 69
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
170-238 2.36e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 41.97  E-value: 2.36e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352650   170 EGESLSLVCMADSNPPAVLSWER-----PTQKPFqlstpaelqLPRAELEDQGKYICQAQNSQGA-QTASVSLSI 238
Cdd:pfam13895  13 EGEPVTLTCSAPGNPPANYTWYKggealNSSPNF---------ISSVSAEDSGTYTCVARNGRGGkVSNPVELTV 78
Ig_Myomesin_like_C cd05737
C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: ...
168-238 5.21e-05

C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: domain similar to the C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein. Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 41.42  E-value: 5.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 168 IQEGESLSLVCMADSNPPAVLSW---ERPTQK------PFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTASVSLSI 238
Cdd:cd05737  13 IMEGKTLNLTCNVWGDPPPEVSWlknDQALAFldhcnlKVEAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVTVSV 92
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
171-231 6.39e-05

Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 143259  Cd Length: 88  Bit Score: 41.16  E-value: 6.39e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352650 171 GESLSLVCMADSNPPAVLSWER---PTQKPFQLSTP-AELQLPRAELEDQGKYICQAQNSQGAQT 231
Cdd:cd05851  16 GQNVTLECFALGNPVPVIRWRKilePMPATAEISMSgAVLKIFNIQPEDEGTYECEAENIKGKDK 80
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
46-125 1.99e-04

CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.


Pssm-ID: 311910  Cd Length: 89  Bit Score: 39.70  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650    46 IALTEVPNIQVTSTLVSGNStKLLCSVPWacEQGTPPIFSWMSSALTSLGHRT-TLSSELNLTPRPQDNGTNLTCQVNLP 124
Cdd:pfam08205   7 ASLLEGEGPEVVATCSSAGG-KPAPRITW--YLNGKPLEAAETSSEQDPESGLyTVTSTLKLVPSRSDHGQSLTCQVSYP 83

                  .
gi 26352650   125 G 125
Cdd:pfam08205  84 A 84
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
171-233 3.07e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); Ig2_FGFRL1-like: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 143264  Cd Length: 82  Bit Score: 39.05  E-value: 3.07e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 171 GESLSLVCMADSNPPAVLSWERpTQKPFQLSTPAE-------LQLPRAELEDQGKYICQAQNSQGAQTAS 233
Cdd:cd05856   9 GSSVRLKCVASGNPRPDITWLK-DNKPLTPTEIGEsrkkkwtLSLKNLKPEDSGKYTCHVSNRAGEINAT 77
Ig4_Robo cd05726
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar ...
171-242 3.52e-04

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar to the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.


Pssm-ID: 143203  Cd Length: 90  Bit Score: 39.17  E-value: 3.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 171 GESLSLVCMADSNPPAVLSWER--------PTQKP-----FQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTASVSLS 237
Cdd:cd05726   1 GRTVTFQCEATGNPQPAIFWQKegsqnllfSYQPPqsssrFSVSQTGDLTITNVQRSDVGYYICQTLNVAGSILTKAYLE 80

                ....*
gi 26352650 238 IRSLV 242
Cdd:cd05726  81 VTDVI 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
164-236 3.75e-04

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 333796  Cd Length: 86  Bit Score: 39.09  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650   164 ASLQIQEGESLSLVCMA-DSNPPAVLSWERPTQKPFQLSTP---------AELQLPRAELEDQGKYICQAQNSQGAQTAS 233
Cdd:pfam00047   4 PSVTVLEGESATLTCSAsTGSPLPDVTWSKEGGTLIESLRVghdngrttqSSLLISNVTLEDAGTYTCVVNNPGGPATLS 83

                  ...
gi 26352650   234 VSL 236
Cdd:pfam00047  84 TSL 86
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
171-238 4.75e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; Ig4_Contactin-2-like: fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (aliases TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205  Cd Length: 85  Bit Score: 38.74  E-value: 4.75e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26352650 171 GESLSLVCMADSNPPAVLSWER-----PTQKPFQLSTpAELQLPRAELEDQGKYICQAQNSQGAQTASVSLSI 238
Cdd:cd05728  14 GSSLRWECKASGNPRPAYRWLKngqplASENRIEVEA-GDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
Ig_3 cd05765
Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) ...
171-238 5.39e-04

Subgroup of the immunoglobulin (Ig) superfamily; Ig_3: subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 143242  Cd Length: 81  Bit Score: 38.29  E-value: 5.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 171 GESLSLVCMADSNPPAVLSWERPTQ-------KPFQL------STPAELQLPRAELEDQGKYICQAQNSQGAQTASVSLS 237
Cdd:cd05765   1 GETASFHCDVTGRPPPEITWEKQVHgkenlimRPNHVrgnvvvTNIGQLVIYNAQPQDAGLYTCTARNSGGLLRANFPLS 80

                .
gi 26352650 238 I 238
Cdd:cd05765  81 V 81
Ig_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2); ...
168-238 5.72e-04

C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2); Ig_M-protein_C: the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains, and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 38.74  E-value: 5.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 168 IQEGESLSLVCMADSNPPAVLSWERPTQKpFQLSTP----------AELQLPRAELEDQGKYICQAQNSQGAQTASVSLS 237
Cdd:cd05891  13 IMEGKTLNLTCTVFGNPDPEVIWFKNDQD-IELSEHysvkleqgkyASLTIKGVTSEDSGKYSINVKNKYGGETVDVTVS 91

                .
gi 26352650 238 I 238
Cdd:cd05891  92 V 92
IgC_CRIg cd16082
Immunoglobulin (Ig) constant domain in complement receptor of the immunoglobulin superfamily ...
162-233 6.96e-04

Immunoglobulin (Ig) constant domain in complement receptor of the immunoglobulin superfamily (CRIg); The N-terminal domain of CRIg (also referred to as Z39Ig and V-set and Ig domain-containing 4 (VSIG4), belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. CRIg plays a role in the complement system, an inhibitor of the alternative pathway convertases, and a negative regulator of T cell activation. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins such as butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 319331  Cd Length: 86  Bit Score: 38.20  E-value: 6.96e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26352650 162 SGASLQIQEGESLSLVCMADSNPPAVLSW--ERP-TQKPFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQTAS 233
Cdd:cd16082   4 SGYGFTVPQGMRISLQCQAWGSPPISYVWykEQTnNQEPIKVAALSTLLFKPAVVADSGSYFCTAKGRVGSEQRS 78
Ig1_NCAM-2 cd05866
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: ...
160-238 7.63e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2; Ig1_NCAM-2: first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-2 (OCAM/mamFas II, RNCAM). NCAM-2 is organized similarly to NCAM-1, including five N-terminal Ig-like domains and two fibronectin type III domains. NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE), and may function like NCAM, as an adhesion molecule.


Pssm-ID: 143274  Cd Length: 92  Bit Score: 38.47  E-value: 7.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 160 LQSGASLQIQE---GESLSLVCMADSNPPAvLSWERPtQKPFQLSTP----------AELQLPRAELEDQGKYICQAQNS 226
Cdd:cd05866   1 LQVSISLSKVElsvGESKFFTCTAIGEPES-IDWYNP-QGEKIVSSQrvvvqkegvrSRLTIYNANIEDAGIYRCQATDA 78
                        90
                ....*....|...
gi 26352650 227 QG-AQTASVSLSI 238
Cdd:cd05866  79 KGqTQEATVVLEI 91
Ig_PDGFR-alphabeta cd05861
Immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha ...
171-238 1.59e-03

Immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha (CD140a), and beta (CD140b); Ig_PDGFR-alphabeta: immunoglobulin (Ig)-like domain of platelet-derived growth factor (PDGF) receptors (R), alpha (CD140a), and beta (CD140b). PDGF is a potent mitogen for connective tissue cells. PDGF-stimulated processes are mediated by three different PDGFs (PDGF-A,-B, and C). PDGFRalpha binds to all three PDGFs, whereas the PDGFRbeta binds only to PDGF-B. PDGFRs alpha and beta have similar organization: an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFRalpha and PDGFRbeta are essential for normal development.


Pssm-ID: 143269  Cd Length: 84  Bit Score: 37.15  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 171 GESLSLVCMADSNPPAVLSWERPTQKPFQLSTPAE------------LQLPRAELEDQGKYICQAQNSQGAQTASVSLSI 238
Cdd:cd05861   1 GETITVNCIVQGNEVVDFSWTYPGKDIGKGIPEVEevkvpattlrstLTFPHATVEDSGTYECAAHESTQDQKAFKKVNI 80
Ig2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, ...
175-239 1.60e-03

Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR; Ig2_RPTP_IIa_LAR_like: domain similar to the second immunoglobulin (Ig)-like domain found in the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR. LAR belongs to the RPTP type IIa subfamily. Members of this subfamily are cell adhesion molecule-like proteins involved in central nervous system (CNS) development. They have large extracellular portions, comprised of multiple Ig-like domains and two to nine fibronectin type III (FNIII) domains, and a cytoplasmic portion having two tandem phosphatase domains.


Pssm-ID: 319301  Cd Length: 74  Bit Score: 36.95  E-value: 1.60e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26352650 175 SLVCMADSNPPAVLSW-------ERPTQKPFQLSTPAELQLPRAELEDQGKYICQAQNSQGAQ-TASVSLSIR 239
Cdd:cd05738   2 TMLCAASGNPDPEITWfkdflpvDTTSNGRIKQLRSGALQIENSEESDQGKYECVATNSAGTRySAPANLYVR 74
Ig_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
171-238 2.34e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and similar proteins; Ig_VEGFR_like: immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and related proteins. The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members, VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGF-A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF, VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-2 and -1 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group also contains alpha-type platelet-derived growth factor receptor precursor (PDGFR)-alpha (CD140a), and PDGFR-beta (CD140b). PDGFRs alpha and beta have an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion that has protein tyrosine kinase activity.


Pssm-ID: 319303  Cd Length: 85  Bit Score: 36.89  E-value: 2.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26352650 171 GESLSLVCMA--DSNPPAVLSWERPTQKPFQLSTPAE--------------LQLPRAELEDQGKYICQAQNSQGAQTASV 234
Cdd:cd05742   1 GENLVLNCTAigNLNTRVNFEWSYPDKKNGRLSEPRRidflldhanhirsiLHIDKAELEDSGLYTCNVREGPNDHFDEK 80

                ....
gi 26352650 235 SLSI 238
Cdd:cd05742  81 AINV 84
Ig5_KIRREL3-like cd05758
Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known ...
250-320 7.22e-03

Fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2) and similar proteins; Ig5_KIRREL3-like: domain similar to the fifth immunoglobulin (Ig)-like domain of Kirrel (kin of irregular chiasm-like) 3 (also known as Neph2). This protein has five Ig-like domains, one transmembrane domain, and a cytoplasmic tail. Included in this group is mammalian Kirrel (Neph1), Kirrel2 (Neph3), and Drosophila RST (irregular chiasm C-roughest) protein. These proteins contain multiple Ig domains, have properties of cell adhesion molecules, and are important in organ development.


Pssm-ID: 319310  Cd Length: 98  Bit Score: 35.59  E-value: 7.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26352650 250 SFEGQGLHCSCSSRAWPAP-SLRWRLGEGVLEGNSSnGSFTVKSSSAGQWANSSLILSMEFSSNHRLS--CEAW 320
Cdd:cd05758  13 AILGEKARLECLVFSSPPPdRIVWSWDEGFLESGSS-GRFSVETFPTEPGVISVLHISGTQRSDFQTSfnCSAW 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
5-44 8.04e-03

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 336766  Cd Length: 109  Bit Score: 35.90  E-value: 8.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 26352650     5 NSHNCSLDIRDAQKIDTGTYFFRLDGSVKYSFQKSM-LSVL 44
Cdd:pfam07686  69 SNSDFSLTIQNLTPSDSGTYFCAVGPNGEGVFGKGTrLTVL 109
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig) ...
204-236 8.83e-03

Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules, which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG1, -2, -3, and -4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions; for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors; in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms, which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and -3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 143227  Cd Length: 75  Bit Score: 34.81  E-value: 8.83e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 26352650 204 AELQLPRAELEDQGKYICQAQNSQGAQTASVSL 236
Cdd:cd05750  43 SELQINKAKLADSGEYTCVVENILGNDTVTANV 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
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