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   24-JAN-2024, entry version 148.
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.ENSMUSP00000158324; -.
DR   GlyCosmos; Q8K4F0; 7 sites, No reported glycans.
DR   GlyGen; Q8K4F0; 7 sites.
DR   iPTMnet; Q8K4F0; -.
DR   PhosphoSitePlus; Q8K4F0; -.
DR   EPD; Q8K4F0; -.
DR   MaxQB; Q8K4F0; -.
DR   PaxDb; 10090-ENSMUSP00000043551; -.
DR   ProteomicsDB; 283739; -.
DR   ABCD; Q8K4F0; 19 sequenced antibodies.
DR   Antibodypedia; 2514; 922 antibodies from 39 providers.
DR   DNASU; 225825; -.
DR   Ensembl; ENSMUST00000037142.13; ENSMUSP00000043551.6; ENSMUSG00000034028.17.
DR   Ensembl; ENSMUST00000236828.2; ENSMUSP00000158324.2; ENSMUSG00000034028.17.
DR   GeneID; 225825; -.
DR   KEGG; mmu:225825; -.
DR   UCSC; uc008fvo.1; mouse.
DR   AGR; MGI:3039602; -.
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; IREPYAD; -.
DR   OrthoDB; 5354047at2759; -.
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 77 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 57 other cell types or tissues.
DR   ExpressionAtlas; Q8K4F0; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
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: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   GO; GO:0032729; P:positive regulation of type II interferon production; IMP:MGI.
DR   CDD; cd05889; IgV_1_DNAM-1_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; CD226 ANTIGEN; 1.
DR   PANTHER; PTHR47011:SF1; CD226 ANTIGEN; 1.
DR   Pfam; PF07686; V-set; 2.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   Genevisible; Q8K4F0; MM.
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
//