CD226_MOUSE
ID CD226_MOUSE Reviewed; 333 AA.
AC Q8K4F0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=CD226 antigen;
DE AltName: Full=Platelet and T-cell activation antigen 1;
DE AltName: CD_antigen=CD226;
DE Flags: Precursor;
GN Name=Cd226; Synonyms=Pta1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Jin B., Zhang X., Li D., Ouyang W., Jia W., Chen L., Xie X., Ning S.,
RA Zhang Y.;
RT "Gene cloning and characterization of mouse platelet and T cell activation
RT antigen 1 (PTA1/CD226).";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in intercellular adhesion, lymphocyte signaling,
CC cytotoxicity and lymphokine secretion mediated by cytotoxic T-
CC lymphocyte (CTL) and NK cell. Cell surface receptor for NECTIN2. Upon
CC ligand binding, stimulates T-cell proliferation and cytokine
CC production, including that of IL2, IL5, IL10, IL13, and IFNG. Competes
CC with PVRIG for NECTIN2-binding. {ECO:0000250|UniProtKB:Q15762}.
CC -!- SUBUNIT: Interacts with PVR and NECTIN2. Competes with PVRIG for
CC NECTIN2-binding. {ECO:0000250|UniProtKB:Q15762}.
CC -!- INTERACTION:
CC Q8K4F0; P15151: PVR; Xeno; NbExp=3; IntAct=EBI-27124659, EBI-3919694;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; AF416980; AAN04295.1; -; mRNA.
DR CCDS; CCDS29392.1; -.
DR RefSeq; NP_848802.2; NM_178687.2.
DR RefSeq; XP_006526525.1; XM_006526462.3.
DR PDB; 6ISA; X-ray; 2.00 A; A=21-243.
DR PDB; 6ISC; X-ray; 2.20 A; A=21-243.
DR PDBsum; 6ISA; -.
DR PDBsum; 6ISC; -.
DR AlphaFoldDB; Q8K4F0; -.
DR SMR; Q8K4F0; -.
DR IntAct; Q8K4F0; 1.
DR STRING; 10090.ENSMUSP00000043551; -.
DR GlyGen; Q8K4F0; 7 sites.
DR iPTMnet; Q8K4F0; -.
DR PhosphoSitePlus; Q8K4F0; -.
DR EPD; Q8K4F0; -.
DR MaxQB; Q8K4F0; -.
DR PaxDb; Q8K4F0; -.
DR PRIDE; Q8K4F0; -.
DR ProteomicsDB; 283739; -.
DR ABCD; Q8K4F0; 27 sequenced antibodies.
DR Antibodypedia; 2514; 815 antibodies from 38 providers.
DR DNASU; 225825; -.
DR Ensembl; ENSMUST00000037142; ENSMUSP00000043551; ENSMUSG00000034028.
DR Ensembl; ENSMUST00000236828; ENSMUSP00000158324; ENSMUSG00000034028.
DR GeneID; 225825; -.
DR KEGG; mmu:225825; -.
DR UCSC; uc008fvo.1; mouse.
DR CTD; 10666; -.
DR MGI; MGI:3039602; Cd226.
DR VEuPathDB; HostDB:ENSMUSG00000034028; -.
DR eggNOG; ENOG502RY5X; Eukaryota.
DR GeneTree; ENSGT00500000044993; -.
DR HOGENOM; CLU_069157_0_0_1; -.
DR InParanoid; Q8K4F0; -.
DR OMA; DAREDIY; -.
DR OrthoDB; 843835at2759; -.
DR PhylomeDB; Q8K4F0; -.
DR TreeFam; TF336260; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 225825; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Cd226; mouse.
DR PRO; PR:Q8K4F0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8K4F0; protein.
DR Bgee; ENSMUSG00000034028; Expressed in blood and 55 other tissues.
DR ExpressionAtlas; Q8K4F0; baseline and differential.
DR Genevisible; Q8K4F0; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060369; P:positive regulation of Fc receptor mediated stimulatory signaling pathway; ISO:MGI.
DR GO; GO:0002891; P:positive regulation of immunoglobulin mediated immune response; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0033005; P:positive regulation of mast cell activation; ISO:MGI.
DR GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; IMP:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; ISO:MGI.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042842; CD226.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR47011; PTHR47011; 1.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..333
FT /note="CD226 antigen"
FT /id="PRO_0000014667"
FT TOPO_DOM 19..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..127
FT /note="Ig-like C2-type 1"
FT DOMAIN 136..237
FT /note="Ig-like C2-type 2"
FT REGION 287..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 319
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15762"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 153..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6ISA"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6ISA"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:6ISA"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:6ISA"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:6ISC"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:6ISA"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:6ISA"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:6ISA"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:6ISA"
SQ SEQUENCE 333 AA; 38063 MW; ACDE524D0F475C97 CRC64;
MAYVTWLLAI LHVHKALCEE TLWDTTVRLS ETMTLECVYP LTHNLTQVEW TKNTGTKTVS
IAVYNPNHNM HIESNYLHRV HFLNSTVGFR NMSLSFYNAS EADIGIYSCL FHAFPNGPWE
KKIKVVWSDS FEIAAPSDSY LSAEPGQDVT LTCQLPRTWP VQQVIWEKVQ PHQVDILASC
NLSQETRYTS KYLRQTRSNC SQGSMKSILI IPNAMAADSG LYRCRSEAIT GKNKSFVIRL
IITDGGTNKH FILPIVGGLV SLLLVILIII IFILYNRKRR RQVRIPLKEP RDKQSKVATN
CRSPTSPIQS TDDEKEDIYV NYPTFSRRPK PRL
