NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|401709956|ref|NP_113706|]
View 

OX-2 membrane glycoprotein precursor [Rattus norvegicus]

Protein Classification

Ig1_MRC-OX-2_like and ig domain-containing protein( domain architecture ID 10861887)

Ig1_MRC-OX-2_like and ig domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 32-139 9.41e-57

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


:

Pssm-ID: 409433  Cd Length: 108  Bit Score: 177.54  E-value: 9.41e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  32 VEVVTQDERKLLHTTASLRCSLKTTQEPLIVTWQKKKAVGPENMVTYSKAHGVVIQPTYRDRINITELGLLNTSITFWNT 111
Cdd:cd05846    1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80

                         90       100
                 ....*....|....*....|....*...
gi 401709956 112 TLDDEGCYMCLFNMFGSGKVSGTACLTL 139
Cdd:cd05846   81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 143-229 1.73e-08

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: 395002  Cd Length: 86  Bit Score: 50.66  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  143 PIVHLHYNYFEDHLNITCSA-TARPAPAISWKGTGSGIENSTEsHSHSNGTTSVTSILRVKDPKTQVGkEVICQVLYLGN 221
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAG-TYTCVVNNPGG 78


                  ....*...
gi 401709956  222 VIDYKQSL 229
Cdd:pfam00047  79 SATLSTSL 86
 
Name Accession Description Interval E-value
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 32-139 9.41e-57

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 177.54  E-value: 9.41e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  32 VEVVTQDERKLLHTTASLRCSLKTTQEPLIVTWQKKKAVGPENMVTYSKAHGVVIQPTYRDRINITELGLLNTSITFWNT 111
Cdd:cd05846    1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80

                         90       100
                 ....*....|....*....|....*...
gi 401709956 112 TLDDEGCYMCLFNMFGSGKVSGTACLTL 139
Cdd:cd05846   81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
IGv smart00406
Immunoglobulin V-Type;
46-123 3.02e-10

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 55.47  E-value: 3.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956    46 TASLRCSLKTTQEP-LIVTWQKKK-AVGPENMVTYSKAHGVVIQPTYRDRINITELGLLNT-SITFWNTTLDDEGCYMCL 122
Cdd:smart00406   1 SVTLSCKFSGSTFSsYYVSWVRQPpGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDvSLTISNLRVEDTGTYYCA 80


                   .
gi 401709956   123 F 123
Cdd:smart00406  81 V 81
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 34-136 3.23e-10

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: 395002  Cd Length: 86  Bit Score: 55.66  E-value: 3.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956   34 VVTQDERKLLHTTASLRCSLKTTQEPLIVTWQKKKAVGPENMVtyskahgvvIQPTYRDRINitelgllnTSITFWNTTL 113
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK---------VKHDNGRTTQ--------SSLLISNVTK 63

                          90       100
                  ....*....|....*....|...
gi 401709956  114 DDEGCYMCLFNMFGSGKVSGTAC 136
Cdd:pfam00047  64 EDAGTYTCVVNNPGGSATLSTSL 86
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 143-229 1.73e-08

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: 395002  Cd Length: 86  Bit Score: 50.66  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  143 PIVHLHYNYFEDHLNITCSA-TARPAPAISWKGTGSGIENSTEsHSHSNGTTSVTSILRVKDPKTQVGkEVICQVLYLGN 221
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAG-TYTCVVNNPGG 78


                  ....*...
gi 401709956  222 VIDYKQSL 229
Cdd:pfam00047  79 SATLSTSL 86
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 159-216 1.37e-06

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409500  Cd Length: 97  Bit Score: 45.86  E-value: 1.37e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956 159 TC-SATARPAPAISWKGTGSGIENSTESHSHSNGTTSVTSILRVKdPKTQV-GKEVICQV 216
Cdd:cd07703   21 RCvSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLV-PTPEAnGKEVTCKV 79
PHA02987 PHA02987
Ig domain OX-2-like protein; Provisional
 43-138 3.98e-04

Ig domain OX-2-like protein; Provisional


Pssm-ID: 165290 [Multi-domain]  Cd Length: 189  Bit Score: 40.62  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  43 LHTTASLRCSLKTTQEPLIVTWQKKKavgpENMVTYSkAHGVVIQPTYRDRINITELGLLNTSITFWNTTLDDEGCYMCL 122
Cdd:PHA02987  29 EHVNVKISCNKTSSFNSILITWKKNN----KTIAGYG-PCGPVIVDKFKNKIEYLSKSFNESTILIKNVSLKDNGCYTCI 103

                         90
                 ....*....|....*..
gi 401709956 123 FNMFGS-GKVSGTACLT 138
Cdd:PHA02987 104 FNTLLSkNNEKGVVCLN 120
PHA02914 PHA02914
Immunoglobulin-like domain protein; Provisional
 103-230 7.02e-03

Immunoglobulin-like domain protein; Provisional


Pssm-ID: 165230  Cd Length: 500  Bit Score: 37.78  E-value: 7.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956 103 NTSITFWNTTLDDEGCYMCLFNMfgSGKVSGTACLTLYVQPIVHLHYNYFED-HLNITCSATA---RPAPAISWKGTGSG 178
Cdd:PHA02914  80 EYSFIEENIGEHEDGDFKCIFYL--GDNESHKHEILVRKAPKIDTTFLEFNDkHTCICCKIDKpmnQDALKVFFVAGGVN 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 401709956 179 IENSTESHSHSNGTTSVTSILRVKDPK-TQVGKEVICQVLYLGNVIDYKQSLD 230
Cdd:PHA02914 158 VDGNFLGKKDFNNDPSNRTVKLCADKShDDTAREALCGVEYFGALKELNISYD 210
 
Name Accession Description Interval E-value
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 32-139 9.41e-57

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 177.54  E-value: 9.41e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  32 VEVVTQDERKLLHTTASLRCSLKTTQEPLIVTWQKKKAVGPENMVTYSKAHGVVIQPTYRDRINITELGLLNTSITFWNT 111
Cdd:cd05846    1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80

                         90       100
                 ....*....|....*....|....*...
gi 401709956 112 TLDDEGCYMCLFNMFGSGKVSGTACLTL 139
Cdd:cd05846   81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 43-138 1.02e-13

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 65.93  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  43 LHTTASLRCSLkTTQEPLI---VTWQKKKAVGPENMVTYSKAHGVVIQPTYRDRINIT--ELGLLNTSITFWNTTLDDEG 117
Cdd:cd05718   13 LGGSVTLPCSL-TSPGTTKitqVTWMKIGAGSSQNVAVFHPQYGPSVPNPYAERVEFLaaRLGLRNATLRIRNLRVEDEG 91

                         90       100
                 ....*....|....*....|.
gi 401709956 118 CYMCLFNMFGSGKVSGTACLT 138
Cdd:cd05718   92 NYICEFATFPQGNRQGTTWLR 112
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 45-140 1.60e-12

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.


Pssm-ID: 409469  Cd Length: 113  Bit Score: 62.67  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  45 TTASLRCS-------LKTTQepliVTWQKKKAVGPENMVTYSKAHGVVIQPTYRDRINITELGLLNTSITFWNTTLDDEG 117
Cdd:cd05886   15 TDVVLHCSfanplpsVKITQ----VTWQKSTNGSKQNVAIYNPSMGVSVLPPYRERVTFLNPSFTDGTIRLSRLELEDEG 90

                         90       100
                 ....*....|....*....|...
gi 401709956 118 CYMCLFNMFGSGKVSGTACLTLY 140
Cdd:cd05886   91 VYICEFATFPTGNRESQLNLTVM 113
IGv smart00406
Immunoglobulin V-Type;
46-123 3.02e-10

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 55.47  E-value: 3.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956    46 TASLRCSLKTTQEP-LIVTWQKKK-AVGPENMVTYSKAHGVVIQPTYRDRINITELGLLNT-SITFWNTTLDDEGCYMCL 122
Cdd:smart00406   1 SVTLSCKFSGSTFSsYYVSWVRQPpGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDvSLTISNLRVEDTGTYYCA 80


                   .
gi 401709956   123 F 123
Cdd:smart00406  81 V 81
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 34-136 3.23e-10

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: 395002  Cd Length: 86  Bit Score: 55.66  E-value: 3.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956   34 VVTQDERKLLHTTASLRCSLKTTQEPLIVTWQKKKAVGPENMVtyskahgvvIQPTYRDRINitelgllnTSITFWNTTL 113
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLK---------VKHDNGRTTQ--------SSLLISNVTK 63

                          90       100
                  ....*....|....*....|...
gi 401709956  114 DDEGCYMCLFNMFGSGKVSGTAC 136
Cdd:pfam00047  64 EDAGTYTCVVNNPGGSATLSTSL 86
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 143-229 1.73e-08

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: 395002  Cd Length: 86  Bit Score: 50.66  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  143 PIVHLHYNYFEDHLNITCSA-TARPAPAISWKGTGSGIENSTEsHSHSNGTTSVTSILRVKDPKTQVGkEVICQVLYLGN 221
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLK-VKHDNGRTTQSSLLISNVTKEDAG-TYTCVVNNPGG 78


                  ....*...
gi 401709956  222 VIDYKQSL 229
Cdd:pfam00047  79 SATLSTSL 86
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 39-129 6.76e-07

First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of DNAX accessory molecule 1 (DNAM-1, also known as CD226). DNAM-1 is a transmembrane protein having two Ig-like domains. It is an adhesion molecule which plays a part in tumor-directed cytotoxicity and adhesion in natural killer (NK) cells and T lymphocytes. It has been shown to regulate the NK cell killing of several tumor types, including myeloma cells and ovarian carcinoma cells. DNAM-1 interacts specifically with poliovirus receptor (PVR; CD155) and nectin -2 (CD211), other members of the Ig superfamily. DNAM-1 is expressed in most peripheral T cells, NK cells, monocytes and a subset of B lymphocytes.


Pssm-ID: 409472  Cd Length: 111  Bit Score: 47.16  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  39 ERKLLHTTA------SLRCSLKTTQEPLIVTWQKKKAVGpENMVTYSKAHGVVIQPTYRDRINI--TELGLLNTSITFWN 110
Cdd:cd05889    3 EEVLWDTSVplsenmSLECVYPSTGILTQVEWTKIGGQK-DNIAVYHPTHGMHIRKPYAGRVYFlnSTMASNNMSLSFRN 81

                         90
                 ....*....|....*....
gi 401709956 111 TTLDDEGCYMCLFNMFGSG 129
Cdd:cd05889   82 ASEDDVGYYSCSLYTYPQG 100
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
 159-216 1.37e-06

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409500  Cd Length: 97  Bit Score: 45.86  E-value: 1.37e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956 159 TC-SATARPAPAISWKGTGSGIENSTESHSHSNGTTSVTSILRVKdPKTQV-GKEVICQV 216
Cdd:cd07703   21 RCvSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLV-PTPEAnGKEVTCKV 79
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 48-139 1.37e-05

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 43.39  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  48 SLRCSLKTTQEPLIVTWQKKKAVGPENMVTYSKAHGVVIQPTYRDRINITELGLLNTSITFWNTTLDDEGCYMCLFNMFG 127
Cdd:cd05887   18 SLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHNVGFSDSGKYICKAVTFP 97

                         90
                 ....*....|..
gi 401709956 128 SGKVSGTACLTL 139
Cdd:cd05887   98 LGNAQSSTTVTV 109
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
 159-229 1.50e-05

Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111.


Pssm-ID: 409384  Cd Length: 96  Bit Score: 42.87  E-value: 1.50e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401709956 159 TC-SATARPAPAISWKGTGSGIENSTEShSHSNGTTSVTSILRVKDPKTQVGKEVICQVLYLGNVIDYKQSL 229
Cdd:cd05719   22 TCiSANGKPPASVTWETDLKGEASTTQV-RGSNGTVTVTSRYRLVPSREADGQPLTCVVEHPSLEKDQRISV 92
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 32-137 3.00e-05

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409581  Cd Length: 112  Bit Score: 42.18  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  32 VEVVTQdERKLLHTTASLRCSLkTTQEPLI----VTWQKKKAVGpeNMVTYSKAHGVVIQPTYRDRINITELG--LLNTS 105
Cdd:cd20989    3 VQVPPE-VRGFLGGSVTLPCHL-LPPNMVThvsqVTWQRHDEHG--SVAVFHPKQGPSFPESERLSFVAARLGaeLRNAS 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 401709956 106 ITFWNTTLDDEGCYMCLFNMFGSGKVSGTACL 137
Cdd:cd20989   79 LAMFGLRVEDEGNYTCEFATFPQGSRSGDTWL 110
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 43-141 1.29e-04

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 40.52  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956   43 LHTTASLRCSLKT--TQEPLIVTWQKKKA-VGPENMVTYSKAHGVviQPTYRDRINITEL-GLLNTSITFWNTTLDDEGC 118
Cdd:pfam07686  10 LGGSVTLPCTYSSsmSEASTSVYWYRQPPgKGPTFLIAYYSNGSE--EGVKKGRFSGRGDpSNGDGSLTIQNLTLSDSGT 87

                          90       100
                  ....*....|....*....|...
gi 401709956  119 YMClfNMFGSGKVSGTACLTLYV 141
Cdd:pfam07686  88 YTC--AVIPSGEGVFGKGTRLTV 108
PHA02987 PHA02987
Ig domain OX-2-like protein; Provisional
 43-138 3.98e-04

Ig domain OX-2-like protein; Provisional


Pssm-ID: 165290 [Multi-domain]  Cd Length: 189  Bit Score: 40.62  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  43 LHTTASLRCSLKTTQEPLIVTWQKKKavgpENMVTYSkAHGVVIQPTYRDRINITELGLLNTSITFWNTTLDDEGCYMCL 122
Cdd:PHA02987  29 EHVNVKISCNKTSSFNSILITWKKNN----KTIAGYG-PCGPVIVDKFKNKIEYLSKSFNESTILIKNVSLKDNGCYTCI 103

                         90
                 ....*....|....*..
gi 401709956 123 FNMFGS-GKVSGTACLT 138
Cdd:PHA02987 104 FNTLLSkNNEKGVVCLN 120
C2-set_2 pfam08205
CD80-like C2-set immunoglobulin domain; These domains belong to the immunoglobulin superfamily.
 159-218 4.74e-04

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


Pssm-ID: 400489  Cd Length: 89  Bit Score: 38.55  E-value: 4.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 401709956  159 TC-SATARPAPAISWKGTGSGIENSTESHSHS--NGTTSVTSILRVKDPKTQVGKEVICQVLY 218
Cdd:pfam08205  20 TCsSAGGKPAPRITWYLDGKPLEAAETSSEQDpeSGLVTVTSELKLVPSRSDHGQSLTCQVSY 82
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 27-142 1.23e-03

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.


Pssm-ID: 409538  Cd Length: 102  Bit Score: 37.52  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956  27 LSTAQVEVVTQDerkllHTTASLRCSLKTTQEPLIVTWQKKkavgpENMVTYSKAHGVVIQPTYRDRINItelglLNTSI 106
Cdd:cd20946    2 VPSSQQVVTVVE-----NQEVILSCKTPKKTSSPRVEWKKL-----QRDVTFVVFQNNKIQGDYKGRAEI-----LGTNI 66

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 401709956 107 TFWNTTLDDEGCYMCLFNMFGSGKVSGTACLTLYVQ 142
Cdd:cd20946   67 TIKNVTRSDSGKYRCEVSARSDGQNLGEVTVTLEVL 102
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 154-202 2.45e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.00  E-value: 2.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 401709956  154 DHLNITCSATARPAPAISWKGTGSGIENSTESHSHSNGTTSVTSILRVK 202
Cdd:pfam13927  17 ETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVT 65
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 46-141 3.58e-03

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 35.94  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956    46 TASLRCSLKTTQEPlIVTWQKKKAvgpenmvtyskahgvvIQPTYRDRINITELGLlNTSITFWNTTLDDEGCYMCLFNm 125
Cdd:smart00410  11 SVTLSCEASGSPPP-EVTWYKQGG----------------KLLAESGRFSVSRSGS-TSTLTISNVTPEDSGTYTCAAT- 71

                           90
                   ....*....|....*.
gi 401709956   126 FGSGKVSGTAclTLYV 141
Cdd:smart00410  72 NSSGSASSGT--TLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 156-216 6.53e-03

Immunoglobulin domain; The members here are composed 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 this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including 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. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 34.61  E-value: 6.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 401709956 156 LNITCSATARPAPAISWKGTGSGIENSTESHSHSNGTTSVtsiLRVKDPKTQVGKEVICQV 216
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGT---LTISNVTLEDSGTYTCVA 58
PHA02914 PHA02914
Immunoglobulin-like domain protein; Provisional
 103-230 7.02e-03

Immunoglobulin-like domain protein; Provisional


Pssm-ID: 165230  Cd Length: 500  Bit Score: 37.78  E-value: 7.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401709956 103 NTSITFWNTTLDDEGCYMCLFNMfgSGKVSGTACLTLYVQPIVHLHYNYFED-HLNITCSATA---RPAPAISWKGTGSG 178
Cdd:PHA02914  80 EYSFIEENIGEHEDGDFKCIFYL--GDNESHKHEILVRKAPKIDTTFLEFNDkHTCICCKIDKpmnQDALKVFFVAGGVN 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 401709956 179 IENSTESHSHSNGTTSVTSILRVKDPK-TQVGKEVICQVLYLGNVIDYKQSLD 230
Cdd:PHA02914 158 VDGNFLGKKDFNNDPSNRTVKLCADKShDDTAREALCGVEYFGALKELNISYD 210
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH