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Conserved domains on  [gi|564394309|ref|XP_006255090|]
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CD226 antigen isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
17-128 1.34e-66

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: 204.71  E-value: 1.34e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309  17 LCEETLWDTTVRLSETMTLECVYPLTDNLTQAEWTKDTGtKKVNIAVYHPNHNMHIDPNYLHRVHFQNATVGFRNMSLSF 96
Cdd:cd05889    1 LVEEVLWDTSVPLSENMSLECVYPSTGILTQVEWTKIGG-QKDNIAVYHPTHGMHIRKPYAGRVYFLNSTMASNNMSLSF 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 564394309  97 YNASEADIGIYTCLFHAFPRGSWEKKIKVVQS 128
Cdd:cd05889   80 RNASEDDVGYYSCSLYTYPQGSWEKVIQVVQS 111
 
Name Accession Description Interval E-value
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
17-128 1.34e-66

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: 204.71  E-value: 1.34e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309  17 LCEETLWDTTVRLSETMTLECVYPLTDNLTQAEWTKDTGtKKVNIAVYHPNHNMHIDPNYLHRVHFQNATVGFRNMSLSF 96
Cdd:cd05889    1 LVEEVLWDTSVPLSENMSLECVYPSTGILTQVEWTKIGG-QKDNIAVYHPTHGMHIRKPYAGRVYFLNSTMASNNMSLSF 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 564394309  97 YNASEADIGIYTCLFHAFPRGSWEKKIKVVQS 128
Cdd:cd05889   80 RNASEDDVGYYSCSLYTYPQGSWEKVIQVVQS 111
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
25-125 1.19e-06

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: 46.68  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309   25 TTVRLSETMTLECVYPL--TDNLTQAEWTKDTGTKKVN--IAVYHPNHNMHIDPNylhRVHFqNATVGFRNMSLSFYNAS 100
Cdd:pfam07686   6 VTVALGGSVTLPCTYSSsmSEASTSVYWYRQPPGKGPTflIAYYSNGSEEGVKKG---RFSG-RGDPSNGDGSLTIQNLT 81
                          90       100
                  ....*....|....*....|....*
gi 564394309  101 EADIGIYTCLFHAFPRGSWEKKIKV 125
Cdd:pfam07686  82 LSDSGTYTCAVIPSGEGVFGKGTRL 106
 
Name Accession Description Interval E-value
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
17-128 1.34e-66

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: 204.71  E-value: 1.34e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309  17 LCEETLWDTTVRLSETMTLECVYPLTDNLTQAEWTKDTGtKKVNIAVYHPNHNMHIDPNYLHRVHFQNATVGFRNMSLSF 96
Cdd:cd05889    1 LVEEVLWDTSVPLSENMSLECVYPSTGILTQVEWTKIGG-QKDNIAVYHPTHGMHIRKPYAGRVYFLNSTMASNNMSLSF 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 564394309  97 YNASEADIGIYTCLFHAFPRGSWEKKIKVVQS 128
Cdd:cd05889   80 RNASEDDVGYYSCSLYTYPQGSWEKVIQVVQS 111
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
19-127 3.99e-28

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: 105.61  E-value: 3.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309  19 EETLWDTTVR--LSETMTLECVY--PLTDNLTQAEWTKDTGTKKVNIAVYHPNHNMHIDPNYLHRVHFQNATVGFRNMSL 94
Cdd:cd05718    1 QRVQVPTEVTgfLGGSVTLPCSLtsPGTTKITQVTWMKIGAGSSQNVAVFHPQYGPSVPNPYAERVEFLAARLGLRNATL 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 564394309  95 SFYNASEADIGIYTCLFHAFPRGSWEKKIKVVQ 127
Cdd:cd05718   81 RIRNLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
24-118 5.71e-14

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: 66.98  E-value: 5.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309  24 DTTVRLSETMTLECVYPLTDNLTQAEWTKDTGTKKVNIAVYHPNHNMHIDPNYLHRVHFQNAtvGFRNMSLSFYNASEAD 103
Cdd:cd05846    7 DTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSS--GLNSTSITIWNVTLED 84
                         90
                 ....*....|....*
gi 564394309 104 IGIYTCLFHAFPRGS 118
Cdd:cd05846   85 EGCYKCLFNTFPDGI 99
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
26-125 1.03e-12

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: 63.80  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309  26 TVRLSETMTLECVYPLTDNLTQAEWTKDTGTKKVNIAVYHPNHNMHIDPNYLHRVHFQNATVgfRNMSLSFYNASEADIG 105
Cdd:cd05887   10 TAVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSL--NDATITLHNVGFSDSG 87
                         90       100
                 ....*....|....*....|
gi 564394309 106 IYTCLFHAFPRGSWEKKIKV 125
Cdd:cd05887   88 KYICKAVTFPLGNAQSSTTV 107
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
45-123 1.09e-09

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: 55.36  E-value: 1.09e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564394309  45 LTQAEWTKDTGTKKVNIAVYHPNHNMHIDPNYLHRVHFQNATvgFRNMSLSFYNASEADIGIYTCLFHAFPRGSWEKKI 123
Cdd:cd05886   32 ITQVTWQKSTNGSKQNVAIYNPSMGVSVLPPYRERVTFLNPS--FTDGTIRLSRLELEDEGVYICEFATFPTGNRESQL 108
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
22-118 1.16e-09

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: 55.28  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309  22 LWDTTVRLSETMTLECvYPLTDN----LTQAEWTK-DTGTkkvNIAVYHPNHNmhidPNYLH--RVHFQNATVG--FRNM 92
Cdd:cd20989    6 PPEVRGFLGGSVTLPC-HLLPPNmvthVSQVTWQRhDEHG---SVAVFHPKQG----PSFPEseRLSFVAARLGaeLRNA 77
                         90       100
                 ....*....|....*....|....*.
gi 564394309  93 SLSFYNASEADIGIYTCLFHAFPRGS 118
Cdd:cd20989   78 SLAMFGLRVEDEGNYTCEFATFPQGS 103
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
25-125 1.19e-06

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: 46.68  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309   25 TTVRLSETMTLECVYPL--TDNLTQAEWTKDTGTKKVN--IAVYHPNHNMHIDPNylhRVHFqNATVGFRNMSLSFYNAS 100
Cdd:pfam07686   6 VTVALGGSVTLPCTYSSsmSEASTSVYWYRQPPGKGPTflIAYYSNGSEEGVKKG---RFSG-RGDPSNGDGSLTIQNLT 81
                          90       100
                  ....*....|....*....|....*
gi 564394309  101 EADIGIYTCLFHAFPRGSWEKKIKV 125
Cdd:pfam07686  82 LSDSGTYTCAVIPSGEGVFGKGTRL 106
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
26-125 5.44e-06

First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is 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 nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain


Pssm-ID: 409471  Cd Length: 108  Bit Score: 44.50  E-value: 5.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394309  26 TVRLSETMTLECVYPLTDNLT--QAEWTK-DTGTKKVNIAVYHPNHNMHIDPNYLHRVHFQnATVGFRNMSLSFYNASEA 102
Cdd:cd05888    4 TVVLGQDAKLPCFYRGDSGEQvgQVAWARvDAGEGAQEIALLHSKYGLHVFPAYEGRVEQP-PPPRPADGSVLLRNAVQA 82
                         90       100
                 ....*....|....*....|...
gi 564394309 103 DIGIYTCLFHAFPRGSWEKKIKV 125
Cdd:cd05888   83 DEGEYECRVSTFPAGNFQAELRL 105
 
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.
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