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Conserved domains on  [gi|26338003|dbj|BAC32687|]
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unnamed protein product [Mus musculus]

Protein Classification

Ig2_Follistatin_like domain-containing protein (domain architecture ID 10146175)

Ig2_Follistatin_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
43-118 4.43e-45

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; Ig2_Follistatin_like: domain similar to the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


:

Pssm-ID: 143213  Cd Length: 76  Bit Score: 152.77  E-value: 4.43e-45
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338003  43 ASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVGVDEDISSLFIEDS 118
Cdd:cd05736   1 ASLRCHAEGIPLPRLTWLKNGMDITPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEAGVDEDISSLFVEDS 76
 
Name Accession Description Interval E-value
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
43-118 4.43e-45

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; Ig2_Follistatin_like: domain similar to the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 143213  Cd Length: 76  Bit Score: 152.77  E-value: 4.43e-45
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338003  43 ASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVGVDEDISSLFIEDS 118
Cdd:cd05736   1 ASLRCHAEGIPLPRLTWLKNGMDITPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEAGVDEDISSLFVEDS 76
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
25-102 1.06e-18

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 339005  Cd Length: 79  Bit Score: 80.27  E-value: 1.06e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26338003    25 PPVIRVYPETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMDVSTQ-MSKQLSLLANGSELHIGSVRYEDTGAYTCIAKN 102
Cdd:pfam13927   1 KPVITVSPSSVVVVEGESVTLTCEATGGPPPTITWYKNGEEISSGsTSARISVSGSNSTLTISNVTREDSGTYTCVASN 79
IGc2 smart00408
Immunoglobulin C-2 Type;
39-105 3.67e-14

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 67.05  E-value: 3.67e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26338003     39 PGVAASLRCHAEGIPLPRIIWLKNGmdvsTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKDG----KPLPESNRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
 
Name Accession Description Interval E-value
Ig2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; ...
43-118 4.43e-45

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5 and similar proteins; Ig2_Follistatin_like: domain similar to the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 143213  Cd Length: 76  Bit Score: 152.77  E-value: 4.43e-45
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338003  43 ASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVGVDEDISSLFIEDS 118
Cdd:cd05736   1 ASLRCHAEGIPLPRLTWLKNGMDITPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNEAGVDEDISSLFVEDS 76
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
25-102 1.06e-18

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 339005  Cd Length: 79  Bit Score: 80.27  E-value: 1.06e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26338003    25 PPVIRVYPETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMDVSTQ-MSKQLSLLANGSELHIGSVRYEDTGAYTCIAKN 102
Cdd:pfam13927   1 KPVITVSPSSVVVVEGESVTLTCEATGGPPPTITWYKNGEEISSGsTSARISVSGSNSTLTISNVTREDSGTYTCVASN 79
Ig cd00096
Immunoglobulin domain; Immunoglobulin (Ig) domain found in the Ig superfamily. The Ig ...
43-108 9.65e-16

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: 71.50  E-value: 9.65e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338003  43 ASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVGVDE 108
Cdd:cd00096   1 VTLTCSASGNPPPTITWLKNGKPLPSSSRFRRRSSGGNGTLTISNVTPEDSGTYTCVASNSAGSAS 66
IGc2 smart00408
Immunoglobulin C-2 Type;
39-105 3.67e-14

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 67.05  E-value: 3.67e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26338003     39 PGVAASLRCHAEGIPLPRIIWLKNGmdvsTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:smart00408   1 EGQSVTLTCPAEGNPVPNITWLKDG----KPLPESNRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
I-set pfam07679
Immunoglobulin I-set domain;
26-115 2.19e-13

Immunoglobulin I-set domain;


Pssm-ID: 336764  Cd Length: 90  Bit Score: 65.73  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003    26 PVIRVYPETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:pfam07679   1 PKFTQKPKDVEVSEGESARFTCTVTGDPDPEVSWFKDGSPLRSSSRFRVTYEGGTYTLTISNVQIDDSGKYTCVATNSAG 80
                          90
                  ....*....|
gi 26338003   106 VDEDISSLFI 115
Cdd:pfam07679  81 EAEASAELTV 90
Ig3_NCAM-1_like cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); ...
25-113 7.93e-11

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: 58.40  E-value: 7.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  25 PPVIRV-YPETQAQ-EPGVAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKqLSLLANGSELHIGSVRYEDTGAYTCIAKN 102
Cdd:cd05730   1 PPTIRArQSEVNATaNLGQSVTLACDADGFPEPTMTWTKDGEPIESGEEK-YSFNEDGSEMTILDVDKLDEAEYTCIAEN 79
                        90
                ....*....|.
gi 26338003 103 EVGVDEDISSL 113
Cdd:cd05730  80 KAGEQEAEIHL 90
IG smart00409
Immunoglobulin;
32-108 1.51e-10

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 57.52  E-value: 1.51e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26338003     32 PETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMD-VSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVGVDE 108
Cdd:smart00409   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
32-108 1.51e-10

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


Pssm-ID: 214653  Cd Length: 85  Bit Score: 57.52  E-value: 1.51e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26338003     32 PETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMD-VSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVGVDE 108
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKlLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSAS 78
Ig3_Contactin cd04968
Third immunoglobulin (Ig) domain of contactin; Ig3_Contactin_like: Third Ig domain of ...
25-107 1.04e-09

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: 55.24  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  25 PPVIRVYPETQAQEPGVAASLRCHAEGIPLPRIIWLK-NGMdvstQMSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNE 103
Cdd:cd04968   1 PSIKVRFPADTYALKGQTVTLECFALGNPVPQIKWRKvDGS----PSSQWTTSTSEPV-LEIPNVQFEDEGTYECEAENS 75

                ....
gi 26338003 104 VGVD 107
Cdd:cd04968  76 RGKD 79
Ig1_Robo cd07693
First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; ...
25-106 2.17e-09

First immunoglobulin (Ig)-like domain in Robo (roundabout) receptors and similar proteins; Ig1_Robo: domain similar to the first 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: 143317  Cd Length: 100  Bit Score: 54.47  E-value: 2.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  25 PPVIRVYPETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLS---LLANGSELHI----GSVRYEDTGAYT 97
Cdd:cd07693   1 PPRIVEHPSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDPRShriVLPSGSLFFLrvvhGRKGRSDEGVYV 80

                ....*....
gi 26338003  98 CIAKNEVGV 106
Cdd:cd07693  81 CVAHNSLGE 89
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins (NRGs); Ig_Pro_neuregulin: immunoglobulin (Ig) ...
44-107 4.42e-09

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: 52.92  E-value: 4.42e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26338003  44 SLRCHAEGI-PLPRIIWLKNGMDVSTQMSKQLSLLANG---SELHIGSVRYEDTGAYTCIAKNEVGVD 107
Cdd:cd05750   2 VLKCEATSEyPSLRFKWFKDGKELNRKNKPRNIKIRNKkknSELQINKAKLADSGEYTCVVENILGND 69
Ig_1 cd05763
Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: subgroup of the immunoglobulin (Ig) ...
43-105 6.92e-09

Subgroup of the immunoglobulin (Ig) superfamily; Ig_1: 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: 143240  Cd Length: 75  Bit Score: 52.24  E-value: 6.92e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26338003  43 ASLRCHAEGIPLPRIIWLKNG-MDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05763   1 ARLECAATGHPTPQIAWQKDGgTDFPAARERRMHVMPEDDVFFIVDVKIEDTGVYSCTAQNTAG 64
Ig_NCAM-1_like cd05732
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar ...
24-116 2.46e-08

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM) and similar proteins; Ig_NCAM-1 like: domain similar to the fourth 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. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE).


Pssm-ID: 143209  Cd Length: 96  Bit Score: 51.37  E-value: 2.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  24 VPPVIrVYPETQAQEPGVAASLRCHAEGIPLPRIIWlKNGMDVSTQMSKQLS--LLANG----SELHIGSVRYEDTGAYT 97
Cdd:cd05732   1 VQPKI-TYLENQTAVELEQITLTCEAEGDPIPEITW-RRATRNFSEGDKSLDgrIVVRGharvSSLTLKDVQLTDAGRYD 78
                        90
                ....*....|....*....
gi 26338003  98 CIAKNEVGVdeDISSLFIE 116
Cdd:cd05732  79 CEASNRIGG--DQQSMYLE 95
Ig3_Contactin-1 cd05851
Third immunoglobulin (Ig) domain of contactin-1; Ig3_Contactin-1: Third Ig domain of the ...
25-116 4.98e-08

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: 50.41  E-value: 4.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  25 PPVIRV-YPETQAQEpGVAASLRCHAEGIPLPRIIWLKngmdVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNE 103
Cdd:cd05851   1 PADINVkFKDTYALK-GQNVTLECFALGNPVPVIRWRK----ILEPMPATAEISMSGAVLKIFNIQPEDEGTYECEAENI 75
                        90
                ....*....|...
gi 26338003 104 VGVDEDISSLFIE 116
Cdd:cd05851  76 KGKDKHQARVYVQ 88
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: ...
45-105 1.15e-07

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM_like: domain similar to the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 319298  Cd Length: 71  Bit Score: 48.58  E-value: 1.15e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26338003  45 LRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLlanGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05731   3 LECIAEGLPTPDIRWIKLGGELPKGRTKFENF---NKTLKIENVSEADSGEYQCTASNTMG 60
Ig2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar ...
45-105 1.31e-07

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor and similar proteins; Ig2_FGFR_like: domain similar to the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor_like-1(FGFRL1). 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: 319297  Cd Length: 85  Bit Score: 49.14  E-value: 1.31e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26338003  45 LRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLAN-GSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05729  14 LECGARGNPTPNITWLKDGKQKWKINVIRPTRVEEkGWVLIIRRAIPRDTGKYTCIVSNQYG 75
Ig_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar domains; Ig_Titin_like: ...
24-108 2.10e-07

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: 48.89  E-value: 2.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  24 VPPVIRVYPETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNE 103
Cdd:cd05747   2 LPATILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVENS 81

                ....*
gi 26338003 104 VGVDE 108
Cdd:cd05747  82 EGKQE 86
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2 and similar proteins; ...
38-105 2.12e-07

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: 48.37  E-value: 2.12e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  38 EPGVAASLR--CHAEGIPLPRIIWLKNGMDVSTQMSKQLSllanGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05728  10 EADIGSSLRweCKASGNPRPAYRWLKNGQPLASENRIEVE----AGDLRITKLSLSDSGMYQCVAENKHG 75
Ig1_Neogenin cd05722
First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first ...
40-103 2.18e-07

First immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig1_Neogenin: first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 143199  Cd Length: 95  Bit Score: 48.63  E-value: 2.18e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSEL--HIGSVRYE--DTGAYTCIAKNE 103
Cdd:cd05722  14 GGPVVLNCSAEGEPPPKIEWKKDGVLLNLVSDERRQQLPNGSLLitSVVHSKHNkpDEGFYQCVAQND 81
Ig_NCAM-1 cd05869
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: ...
31-116 4.24e-07

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-1 (NCAM); Ig_NCAM-1: immunoglobulin (Ig)-like domain similar to the fourth Ig 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: 143277  Cd Length: 97  Bit Score: 48.05  E-value: 4.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  31 YPETQ-AQEPGVAASLRCHAEGIPLPRIIWlKNGMDVSTQMSKQLS------LLANGSELHIGSVRYEDTGAYTCIAKNE 103
Cdd:cd05869   7 YVENQtAMELEEQITLTCEASGDPIPSITW-RTSTRNISSEEKTLDghivvrSHARVSSLTLKYIQYTDAGEYLCTASNT 85
                        90
                ....*....|...
gi 26338003 104 VGVdeDISSLFIE 116
Cdd:cd05869  86 IGQ--DSQSMYLE 96
Ig2_RPTP_IIa_LAR_like cd05738
Second immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, ...
43-105 6.51e-07

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: 46.58  E-value: 6.51e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26338003  43 ASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05738   1 ATMLCAASGNPDPEITWFKDFLPVDTTSNGRIKQLRSGA-LQIENSEESDQGKYECVATNSAG 62
Ig2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain ...
40-108 8.76e-07

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig2_Robo: domain similar to the second 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: 143201  Cd Length: 86  Bit Score: 46.62  E-value: 8.76e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  40 GVAASLRCHA-EGIPLPRIIWLKNGMDVSTQmSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVGVDE 108
Cdd:cd05724  11 GEMAVLECSPpRGHPEPTVSWRKDGQPLNLD-NERVRIVDDGN-LLIAEARKSDEGTYKCVATNMVGERE 78
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
39-108 1.04e-06

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: 46.41  E-value: 1.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26338003    39 PGVAASLRCHA-EGIPLPRIIWLKNGMdvstqmSKQLSLLAN-------GSELHIGSVRYEDTGAYTCIAKNEVGVDE 108
Cdd:pfam00047  10 EGESATLTCSAsTGSPLPDVTWSKEGG------TLIESLRVGhdngrttQSSLLISNVTLEDAGTYTCVVNNPGGPAT 81
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
40-105 1.42e-06

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); Ig4_L1-NrCAM_like: fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 319284  Cd Length: 76  Bit Score: 45.91  E-value: 1.42e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLKNGMDVSTQmSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd04978   1 GETGELICEAEGNPQPTITWRLNGVPIEPA-PEDMRRTVDGRTLIFSNLQPNDTAVYQCNASNVHG 65
Ig1_Contactin cd04967
First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First Ig domain of contactins. ...
26-105 1.51e-06

First immunoglobulin (Ig) domain of contactin; Ig1_Contactin: First 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 activity 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: 319276  Cd Length: 91  Bit Score: 46.05  E-value: 1.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  26 PVIRVYPETQAQEpgvAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLAnGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd04967   8 PDDTIFPEESDEE---KVALNCRARANPPPTYRWKMNGTEIKLEPDSRYSLVG-GNLVISNPSKAKDAGHYQCLATNTVG 83
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth Ig domain of ...
47-113 2.78e-06

Fifth immunoglobulin (Ig) domain of contactin; Ig5_Contactin_like: Fifth 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: 319278  Cd Length: 73  Bit Score: 44.75  E-value: 2.78e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26338003  47 CHAEGIPLPRIIWLKNGMDVSTqmSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVGVDEDISSL 113
Cdd:cd04969   8 CKPKASPKPTISWSKGTELLTN--SSRICILPDGS-LKIKNVSKSDEGKYTCFAVNFFGKANSTGSL 71
Ig_TrkABC_d4 cd04972
Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the ...
32-108 3.10e-06

Fourth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB and TrkC; TrkABC_d4: the fourth domain of Trk receptors TrkA, TrkB and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains. The fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, B, and C mediate the trophic effects of the neurotrophin Nerve growth factor (NGF) family. TrkA is recognized by NGF. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system.


Pssm-ID: 143173  Cd Length: 90  Bit Score: 45.20  E-value: 3.10e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26338003  32 PETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVGVDE 108
Cdd:cd04972   7 PNATVVYEGGTATIRCTAEGSPLPKVEWIIAGLIVIQTRTDTLETTVDIYNLQLSNITSETQTTVTCTAENPVGQAN 83
Ig1_Contactin-5 cd05848
First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the ...
44-106 3.63e-06

First immunoglobulin (Ig) domain of contactin-5; Ig1_Contactin-5: First Ig domain of the neural cell adhesion molecule contactin-5. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains, anchored to the membrane by glycosylphosphatidylinositol. The different contactins show different expression patterns in the central nervous system. In rats, a lack of contactin-5 (NB-2) results in an impairment of the neuronal activity in the auditory system. Contactin-5 is expressed specifically in the postnatal nervous system, peaking at about 3 weeks postnatal. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala; lower levels of expression have been detected in the corpus callosum, caudate nucleus, and spinal cord.


Pssm-ID: 143256  Cd Length: 94  Bit Score: 45.31  E-value: 3.63e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26338003  44 SLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLaNGSELHIGSVRYEDTGAYTCIAKNEVGV 106
Cdd:cd05848  23 ILNCEARGNPVPTYRWLRNGTEIDTESDYRYSLI-DGNLIISNPSEVKDSGRYQCLATNSIGS 84
Ig_2 cd05764
Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: subgroup of the immunoglobulin (Ig) ...
40-105 4.11e-06

Subgroup of the immunoglobulin (Ig) superfamily; Ig_2: 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: 143241  Cd Length: 74  Bit Score: 44.40  E-value: 4.11e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLK-NGMDVSTqmSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05764   1 GQRATLRCKARGDPEPAIHWISpDGKLISN--SSRTLVYDNGT-LDILITTVKDTGSFTCIASNAAG 64
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
26-106 4.97e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 316418  Cd Length: 78  Bit Score: 44.28  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003    26 PVIRVYPETQAQepGVAASLRCHAEGIPLPRIIWLKNGMDVSTQMSkqlsllangselHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:pfam13895   2 PVLTPSPTVVTE--GEPVTLTCSAPGNPPANYTWYKGGEALNSSPN------------FISSVSAEDSGTYTCVARNGRG 67

                  .
gi 26338003   106 V 106
Cdd:pfam13895  68 G 68
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: ...
45-107 5.31e-06

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); Ig_DSCAM: immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the mental retardation phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 143211  Cd Length: 79  Bit Score: 44.15  E-value: 5.31e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26338003  45 LRCHAEGIPLPRIIW-LKNGMDVSTQ-----MSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVGVD 107
Cdd:cd05734   3 LNCSAEGYPPPTIVWkHSKGRGHPQHthtccLAGRIQLLSNGS-LLIKHVLEEDSGYYLCKVSNDVGAD 70
Ig4_Peroxidasin cd05746
Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth ...
45-105 6.55e-06

Fourth immunoglobulin (Ig)-like domain of peroxidasin; Ig4_Peroxidasin: the fourth 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: 143223  Cd Length: 69  Bit Score: 43.71  E-value: 6.55e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26338003  45 LRCHAEGIPLPRIIWLKNGMDVSTqmSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05746   3 IPCSAQGDPEPTITWNKDGVQVTE--SGKFHISPEGY-LAIRDVGVADQGRYECVARNTIG 60
Ig1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; Ig1_Contactin-1: First Ig domain of the ...
26-105 9.89e-06

First immunoglobulin (Ig) domain of contactin-1; Ig1_Contactin-1: First 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: 143257  Cd Length: 93  Bit Score: 43.79  E-value: 9.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  26 PVIRVYPEtQAQEPGVaaSLRCHAEGIPLPRIIWLKNGMDVSTqMSKQLSLLanGSELHIGSV-RYEDTGAYTCIAKNEV 104
Cdd:cd05849   8 PIDTIYPE-ESTEGKV--SVNCRARANPFPIYKWRKNNLDIDL-TNDRYSMV--GGNLVINNPdKYKDAGRYVCIVSNIY 81

                .
gi 26338003 105 G 105
Cdd:cd05849  82 G 82
Ig2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
36-105 1.53e-05

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: 42.90  E-value: 1.53e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26338003  36 AQEPGVAASLRCHAEGIPLPRIIWLKNG---MDVSTQMSKQLSLlangsELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05856   5 ARPVGSSVRLKCVASGNPRPDITWLKDNkplTPTEIGESRKKKW-----TLSLKNLKPEDSGKYTCHVSNRAG 72
Ig3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig3_Robo: domain similar ...
43-113 1.80e-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: 42.39  E-value: 1.80e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26338003  43 ASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLsllaNGSELHIGSVRYEDTGAYTCIAKNEVGVDEDISSL 113
Cdd:cd05725   1 VEFQCEVGGDPVPTVLWRKEDGELPKGRAEIL----DDKSLKIRNVTAGDEGSYTCEAENMVGKIEASASL 67
Ig_CEACAM cd05740
Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion ...
26-115 2.88e-05

Immunoglobulin (Ig)-like domain of carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM); Ig_CEACAM: Immunoglobulin (Ig)-like domain 4 in carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins, expressed by epithelial cells, leukocytes, endothelial cells and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions, it is a cell adhesion molecule, and a signaling molecule that regulates the growth of tumor cells, it is an angiogenic factor, and is a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 143217  Cd Length: 91  Bit Score: 42.65  E-value: 2.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  26 PVIRVYPETQAQEP--GVAASLRCHAEGiPLPRIIWLKNGMDVstqMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNE 103
Cdd:cd05740   2 PVINSNNSVGNQPPedNQPVTLTCEAEG-QATYIWWVNNGSLL---VPPRLQLSNDNRTLTFNNVTRSDTGHYQCEASNE 77
                        90
                ....*....|..
gi 26338003 104 VGVdeDISSLFI 115
Cdd:cd05740  78 VSN--MTSDPYI 87
Ig_Myomesin_like_C cd05737
C-temrinal immunoglobulin (Ig)-like domain of myomesin and M-protein; Ig_Myomesin_like_C: ...
27-105 4.71e-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: 42.19  E-value: 4.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  27 VIRVYPETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMDVstQMSKQLSL-LANGSELH--IGSVRYEDTGAYTCIAKNE 103
Cdd:cd05737   3 VLGGLPDVVTIMEGKTLNLTCNVWGDPPPEVSWLKNDQAL--AFLDHCNLkVEAGRTVYftINGVSSEDSGKYGLVVKNK 80

                ..
gi 26338003 104 VG 105
Cdd:cd05737  81 YG 82
Ig_NCAM-2 cd05870
Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM ...
25-105 8.09e-05

Immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM); Ig_NCAM-2: immunoglobulin (Ig)-like domain similar to the fourth Ig domain of Neural Cell Adhesion Molecule NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is organized similarly to NCAM , 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: 143278  Cd Length: 98  Bit Score: 41.50  E-value: 8.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  25 PPVIRVYPETQAQepGVAASLRCHAEGIPLPRIIWLK--NGM-----DVSTQMSKQLSLLANGSELHIGSVRYEDTGAYT 97
Cdd:cd05870   3 PHIIQLKNETTVE--NGAATLSCKAEGEPIPEITWKRasDGHtfsegDKSPDGRIEVKGQHGESSLHIKDVKLSDSGRYD 80

                ....*...
gi 26338003  98 CIAKNEVG 105
Cdd:cd05870  81 CEAASRIG 88
Ig4_NrCAM cd05868
Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); Ig4_ ...
40-105 8.22e-05

Fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule); Ig4_ NrCAM: fourth immunoglobulin (Ig)-like domain of NrCAM (NgCAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six IG-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 143276  Cd Length: 76  Bit Score: 40.75  E-value: 8.22e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLKNGMDVS---TQMSKQLsllaNGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05868   1 GEDGTLICRANGNPKPSISWLTNGVPIEiapTDPSRKV----DGDTIIFSKVQERSSAVYQCNASNEYG 65
Ig_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; Ig_Myotilin_like_C: ...
44-106 9.75e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; Ig_Myotilin_like_C: immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners: all three bind to alpha-actinin; in addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP).


Pssm-ID: 319304  Cd Length: 75  Bit Score: 40.67  E-value: 9.75e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338003  44 SLRCHAEGIPLPRIIWLKNGMDVSTQMSKqLSLLANGSELH---IGSVRYEDTGAYTCIAKNEVGV 106
Cdd:cd05744   2 KLECQVLAIPPPQIFWKKENEMLQFNTDR-ISLYQDNHGRIcllIKDVTKEDAGWYTVSAKNEAGI 66
Ig4_L1-CAM_like cd05867
Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: ...
40-105 1.07e-04

Fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig4_L1-CAM_like: fourth immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 143275  Cd Length: 76  Bit Score: 40.64  E-value: 1.07e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05867   1 GETARLDCQVEGIPTPNITWSINGAPIEGTDPDPRRHVSSGA-LILTDVQPSDTAVYQCEARNRHG 65
Ig2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: ...
45-105 1.92e-04

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; Ig2_FGFR: second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, -2, -3, -4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 143265  Cd Length: 85  Bit Score: 40.23  E-value: 1.92e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26338003  45 LRCHAEGIPLPRIIWLKNGMDVSTQ--MSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05857  14 FRCPAAGNPTPTMRWLKNGKEFKQEhrIGGYKVRNQHWS-LIMESVVPSDKGNYTCVVENEYG 75
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin ...
51-108 2.81e-04

Immunoglobulin (Ig)-like domain of titin and similar domains; Ig_Titin_like: immunoglobulin (Ig)-like domain found in titin-like proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; 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. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin, and similar to titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle, which also have repeated Ig-like and FN-III domains.


Pssm-ID: 319305  Cd Length: 74  Bit Score: 39.12  E-value: 2.81e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 26338003  51 GIPLPRIIWLKNGMDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVGVDE 108
Cdd:cd05748  10 GRPTPTVTWSKDGQPLKLSGRVQIETTATSTSLVIKNAKRSDSGKYTLTLKNSAGEKS 67
Ig_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2); ...
44-105 3.82e-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: 39.51  E-value: 3.82e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26338003  44 SLRCHAEGIPLPRIIWLKNGMDVstQMSKQLSL-LANG--SELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05891  20 NLTCTVFGNPDPEVIWFKNDQDI--ELSEHYSVkLEQGkyASLTIKGVTSEDSGKYSINVKNKYG 82
Ig2_Axl_Tyro3_like cd05749
Second immunoglobulin (Ig)-like domain of Axl/Tyro3 family receptor tyrosine kinases (RTKs); ...
30-106 4.56e-04

Second immunoglobulin (Ig)-like domain of Axl/Tyro3 family receptor tyrosine kinases (RTKs); Ig2_Tyro3_like: the second immunoglobulin (Ig)-like domain in the Axl/Tyro3 family of receptor tyrosine kinases (RTKs). This family includes Axl (also known as Ark, Ufo, and Tyro7), Tyro3 (also known as Sky, Rse, Brt, Dtk, and Tif), and Mer (also known as Nyk, c-Eyk, and Tyro12). Axl/Tyro3 family receptors have an extracellular portion with two Ig-like domains followed by two fibronectin-types III (FNIII) domains, a membrane-spanning single helix, and a cytoplasmic tyrosine kinase domain. Axl, Tyro3 and Mer are widely expressed in adult tissues, though they show higher expression in the brain, in the lymphatic and vascular systems, and in the testis. Axl, Tyro3, and Mer bind the vitamin K dependent protein Gas6 with high affinity, and in doing so activate their tyrosine kinase activity. Axl/Gas6 signaling may play a part in cell adhesion processes, prevention of apoptosis, and cell proliferation.


Pssm-ID: 143226  Cd Length: 81  Bit Score: 38.99  E-value: 4.56e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26338003  30 VYPETQAQEPGVAASLRCHAEGIPLP-RIIWLKNGMDVSTQMSKQLSLLaNGSELHigsvryeDTGAYTCIAKNEVGV 106
Cdd:cd05749   3 VEPEDLSVTANTPFNLTCQAVGPPEPvEILWWQGGSPLGDPPAPSPSVL-NVPGLN-------ETSKFSCEAHNAKGV 72
Ig_Palladin_C cd05893
C-terminal immunoglobulin (Ig)-like domain of palladin; Ig_Palladin_C: C-terminal ...
45-106 4.78e-04

C-terminal immunoglobulin (Ig)-like domain of palladin; Ig_Palladin_C: C-terminal immunoglobulin (Ig)-like domain of palladin. Palladin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to this family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Palladin binds to alpha-actinin ezrin, vasodilator-stimulated phosphoprotein VASP, SPIN90 (DIP, mDia interacting protein), and Src. Palladin also binds F-actin directly, via its Ig3 domain. Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions.


Pssm-ID: 143301  Cd Length: 75  Bit Score: 38.50  E-value: 4.78e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26338003  45 LRCHAEGIPLPRIIWLKNGMDVsTQMSKQLSLLANGSE---LHIGSVRYEDTGAYTCIAKNEVGV 106
Cdd:cd05893   3 LECRVSGVPHPQIFWKKENESL-THNTDRVSMHQDNCGyicLLIQGATKEDAGWYTVSAKNEAGI 66
Ig3_FGFR-2 cd05858
Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); ...
40-106 5.36e-04

Third immunoglobulin (Ig)-like domain of fibroblast growth factor receptor 2 (FGFR2); Ig3_FGFR-2-like; domain similar to the third immunoglobulin (Ig)-like domain of human fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factors (FGFs) participate in morphogenesis, development, angiogenesis, and wound healing. These FGF-stimulated processes are mediated by four FGFR tyrosine kinases (FGRF1-4). FGFRs are comprised of an extracellular portion consisting of three Ig-like domains, a transmembrane helix, and a cytoplasmic portion having protein tyrosine kinase activity. The highly conserved Ig-like domains 2 and 3, and the linker region between D2 and D3 define a general binding site for FGFs. FGFR2 is required for male sex determination.


Pssm-ID: 143266  Cd Length: 90  Bit Score: 39.15  E-value: 5.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLK----NGMDVSTQMSKQLSLL----ANGSE-----LHIGSVRYEDTGAYTCIAKNEVGV 106
Cdd:cd05858   1 GSTVEFVCKVYSDAQPHIQWLKhvekNGSKYGPDGLPYVTVLktagVNTTDkemevLYLRNVTFEDAGEYTCLAGNSIGI 80
Ig_Myotilin_C cd05892
C-terminal immunoglobulin (Ig)-like domain of myotilin; Ig_Myotilin_C: C-terminal ...
43-106 6.21e-04

C-terminal immunoglobulin (Ig)-like domain of myotilin; Ig_Myotilin_C: C-terminal immunoglobulin (Ig)-like domain of myotilin. Mytolin belongs to the palladin-myotilin-myopalladin family. Proteins belonging to the latter family contain multiple Ig-like domains and function as scaffolds, modulating actin cytoskeleton. Myotilin is most abundant in skeletal and cardiac muscle, and is involved in maintaining sarcomere integrity. It binds to alpha-actinin, filamin and actin. Mutations in myotilin lead to muscle disorders.


Pssm-ID: 143300  Cd Length: 75  Bit Score: 38.39  E-value: 6.21e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26338003  43 ASLRCHAEGIPLPRIIWLKNGMDVSTQmSKQLSLLANGS---ELHIGSVRYEDTGAYTCIAKNEVGV 106
Cdd:cd05892   1 VKLECQISAIPPPKIFWKRNNEMVQYN-TDRISLYQDNSgrvTLLIKNVNKKDAGWYTVSAVNEAGV 66
Ig4_Robo cd05726
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; Ig4_Robo: domain similar ...
40-105 6.67e-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: 38.78  E-value: 6.67e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLKNGMDV------STQMSKQLSLLANGsELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05726   1 GRTVTFQCEATGNPQPAIFWQKEGSQNllfsyqPPQSSSRFSVSQTG-DLTITNVQRSDVGYYICQTLNVAG 71
Ig4_Neogenin cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth ...
45-115 6.67e-04

Fourth immunoglobulin (Ig)-like domain in neogenin and similar proteins; Ig4_Neogenin: fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC, which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain.


Pssm-ID: 212460  Cd Length: 71  Bit Score: 38.02  E-value: 6.67e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26338003  45 LRCHAEGIPLPRIIWLKNGMDVSTqmSKQLSLLANGSELHIGSVRyEDTGAYTCIAKNEVGVDEDISSLFI 115
Cdd:cd05723   4 FECEVTGKPTPTVKWVKNGDMVIP--SDYFKIVKEHNLQVLGLVK-SDEGFYQCIAENDVGNVQAGAQLII 71
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; Ig3_Peroxidasin: the third ...
40-115 7.73e-04

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: 38.00  E-value: 7.73e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLKNGMDVStqMSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVGVDEDISSLFI 115
Cdd:cd05745   2 GQTVDFLCEAQGYPQPVIAWTKGGSQLS--VDRRHLVLSSGT-LRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
Ig3_L1-CAM cd05876
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: ...
45-105 1.35e-03

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM); Ig3_L1-CAM: third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains, five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM.


Pssm-ID: 143284  Cd Length: 71  Bit Score: 37.21  E-value: 1.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26338003  45 LRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSllaNGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05876   3 LECIAEGLPTPEVHWDRIDGPLSPNRTKKLN---NNKTLQLDNVLESDDGEYVCTAENSEG 60
Ig_Perlecan_like cd05743
Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan ...
40-105 1.59e-03

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar domains; Ig_Perlecan_like: the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar domains. Perlecan consists of five domains. Domain I has three putative heparan sulfate attachment sites; domain II has four LDL receptor-like repeats, and one Ig-like repeat; domain III resembles the short arm of laminin chains; domain IV has multiple Ig-like repeats (21 repeats in human perlecan); and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.


Pssm-ID: 143220  Cd Length: 78  Bit Score: 37.08  E-value: 1.59e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLKN-GMDVSTQMSKQLSLLANGSeLHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05743   1 GETVEFTCVATGVPTPIINWRLNwGHVPDSARVSITSEGGYGT-LTIRDVKESDQGAYTCEAINTRG 66
Ig3_RPTP_IIa_LAR_like cd05739
Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, ...
40-122 1.72e-03

Third immunoglobulin (Ig)-like domain of the receptor protein tyrosine phosphatase (RPTP)-F, also known as LAR; Ig3_RPTP_IIa_LAR_like: domain similar to the third 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. Included in this group is Drosophila LAR (DLAR).


Pssm-ID: 143216  Cd Length: 69  Bit Score: 36.79  E-value: 1.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  40 GVAASLRCHAEGIPLPRIIWLKNGMDVSTQmsKQLSLLANGSELhigsVRYEDTGAYTCIAknevgvdedISSL-FIEDS 118
Cdd:cd05739   1 GGSVNLTCVAVGAPMPYVKWMKGGEELTKE--DEMPVGRNVLEL----TNIYESANYTCVA---------ISSLgMIEAT 65

                ....
gi 26338003 119 ARKT 122
Cdd:cd05739  66 AQVT 69
Ig_VEGFR-1 cd07702
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); ...
53-97 1.73e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1); Ig_VEGFR-1: immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor 1 (VEGFR-1). 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. VEGFRs bind VEGFs with high affinity at the Ig-like domains. VEGFR-1 binds VEGF-A strongly; 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-1 may play an inhibitory rolet in the function of VEGFR-2 by binding VEGF-A and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis and may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells.


Pssm-ID: 143326  Cd Length: 72  Bit Score: 37.17  E-value: 1.73e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 26338003  53 PLPRIIWLKNGMDVSTQMSKQLSllaNGSELHIGSVRYEDTGAYT 97
Cdd:cd07702  11 PAPEVIWLKDGLPAAEKCSRYHV---DGYSLVIKDVTEEDAGIYT 52
Ig2_PTK7 cd05760
Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7, also known as CCK4; ...
44-105 1.82e-03

Second immunoglobulin (Ig)-like domain of protein tyrosine kinase (PTK) 7, also known as CCK4; Ig2_PTK7: domain similar to the second immunoglobulin (Ig)-like domain in protein tyrosine kinase (PTK) 7, also known as CCK4. PTK7 is a subfamily of the receptor protein tyrosine kinase family, and is referred to as an RPTK-like molecule. RPTKs transduce extracellular signals across the cell membrane, and play important roles in regulating cell proliferation, migration, and differentiation. PTK7 is organized as an extracellular portion having seven Ig-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase-like domain. PTK7 is considered a pseudokinase as it has several unusual residues in some of the highly conserved tyrosine kinase (TK) motifs; it is predicted to lack TK activity. PTK7 may function as a cell-adhesion molecule. PTK7 mRNA is expressed at high levels in placenta, melanocytes, liver, lung, pancreas, and kidney. PTK7 is overexpressed in several cancers, including melanoma and colon cancer lines.


Pssm-ID: 143237  Cd Length: 77  Bit Score: 37.20  E-value: 1.82e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26338003  44 SLRCHAEGIPLPRIIWLKNGMDVSTQMSKQlSLLANGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05760   2 TLRCHIDGHPRPTYQWFRDGTPLSDGQGNY-SVSSKERTLTLRSAGPDDSGLYYCCAHNAFG 62
Ig4_PDGFR cd05859
Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); ...
44-115 1.95e-03

Fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR); IG4_PDGFR: The fourth immunoglobulin (Ig)-like domain of platelet-derived growth factor receptor (PDGFR) alpha and beta. PDGF is a potent mitogen for connective tissue cells. PDGF-stimulated processes are mediated by three different PDGFs (PDGF-A,-B, and C). PDGFR alpha binds to all three PDGFs, whereas the PDGFR beta binds only to PDGF-B. PDGF alpha is organized as an extracellular component having five Ig-like domains, a transmembrane segment, and a cytoplasmic portion having protein tyrosine kinase activity. In mice, PDGFR alpha and PDGFR beta are essential for normal development.


Pssm-ID: 143267  Cd Length: 101  Bit Score: 37.54  E-value: 1.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26338003  44 SLRCHAEGIPLPRIIWLKNGMDVS------TQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEvgvDEDISSLFI 115
Cdd:cd05859  22 EFVVEVEAYPPPQIRWLKDNRTLIenlteiTTSEHNVQETRYVSKLKLIRAKEEDSGLYTALAQNE---DAVKSYTFA 96
Ig1_Contactin-2 cd05850
First immunoglobulin (Ig) domain of contactin-2; Ig1_Contactin-2: First Ig domain of the ...
26-105 2.04e-03

First immunoglobulin (Ig) domain of contactin-2; Ig1_Contactin-2: First Ig domain of the neural cell adhesion molecule contactin-2-like. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. It may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. 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. 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-2 is also expressed in retinal amacrine cells in the developing chick retina, corresponding to the period of formation and maturation of AC processes.


Pssm-ID: 143258  Cd Length: 94  Bit Score: 37.61  E-value: 2.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  26 PVIRVYPETQAQEpgvAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLAnGSELHIGSVRYEDTGAYTCIAKNEVG 105
Cdd:cd05850   8 PSSLLFPEGSPEE---KVTLGCRARASPPATYRWKMNGTEIKFAPESRYTLVA-GNLVINNPQKARDAGSYQCLAINRCG 83
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; Ig_Pro_neuregulin-1: ...
45-107 2.40e-03

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; Ig_Pro_neuregulin-1: immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family, which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules, which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. 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.


Pssm-ID: 143303  Cd Length: 76  Bit Score: 36.90  E-value: 2.40e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26338003  45 LRCHAEG-IPLPRIIWLKNGMDVSTQMSKQLSLLANG----SELHIGSVRYEDTGAYTCIAKNEVGVD 107
Cdd:cd05895   3 LRCETVSeYPSLRFKWFKNGKEIGAKNKPDNKIKIRKkkksSELQISKASLADNGEYKCMVSSKLGND 70
Ig_VEGFR cd04976
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); ...
51-102 3.86e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR); Ig_VEGFR: immunoglobulin (Ig)-like domain of vascular endothelial growth factor receptor (VEGFR). 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). VEGFRs bind VEGFs with high affinity at 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.


Pssm-ID: 319282  Cd Length: 70  Bit Score: 35.99  E-value: 3.86e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 26338003  51 GIPLPRIIWLKNGMDVSTQMSKQLsllanGSELHIGSVRYEDTGAYTCIAKN 102
Cdd:cd04976   9 AYPPPEFKWYKNGKPITENHTKKS-----GYSLQIKDVTEHDAGNYTVVLTN 55
Ig8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
26-117 6.71e-03

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar domains; Ig8_hMLCK_like: the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar domains. MLCK is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+, which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 143239  Cd Length: 98  Bit Score: 36.09  E-value: 6.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338003  26 PVIRVYPETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMDVstQMSKQLSLLA--NGSELHIGSVRYEDTGAYTCIAKNE 103
Cdd:cd05762   1 PQIIQFPEDMKVRAGESVELFCKVTGTQPITCTWMKFRKQI--QEGEGIKIENteNSSKLTITEGQQEHCGCYTLEVENK 78
                        90
                ....*....|....
gi 26338003 104 VGVDEDISSLFIED 117
Cdd:cd05762  79 LGSRQAQVNLTVVD 92
 
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.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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