CD226_MACMU
ID CD226_MACMU Reviewed; 336 AA.
AC O18906;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 107.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10647817; DOI=10.3109/10425179909033941;
RA Tian F., Li D., Xia H., Liu X., Jia W., Sun C., Sun K., Jin B.;
RT "Isolation of cDNAs encoding gibbon and monkey platelet and T cell
RT activation antigen 1 (PTA1).";
RL DNA Seq. 10:155-161(1999).
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 -!- 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; AF030432; AAB84281.1; -; mRNA.
DR RefSeq; NP_001036108.1; NM_001042643.1.
DR AlphaFoldDB; O18906; -.
DR SMR; O18906; -.
DR STRING; 9544.ENSMMUP00000012105; -.
DR GeneID; 703878; -.
DR KEGG; mcc:703878; -.
DR CTD; 10666; -.
DR eggNOG; ENOG502RY5X; Eukaryota.
DR InParanoid; O18906; -.
DR OrthoDB; 843835at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060369; P:positive regulation of Fc receptor mediated stimulatory signaling pathway; IBA:GO_Central.
DR GO; GO:0002891; P:positive regulation of immunoglobulin mediated immune response; IBA:GO_Central.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IBA:GO_Central.
DR GO; GO:0033005; P:positive regulation of mast cell activation; IBA:GO_Central.
DR GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; IBA:GO_Central.
DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IBA:GO_Central.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IBA:GO_Central.
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; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR47011; PTHR47011; 1.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW 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..336
FT /note="CD226 antigen"
FT /id="PRO_0000014666"
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..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..126
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..239
FT /note="Ig-like C2-type 2"
FT REGION 298..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15762"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 336 AA; 38532 MW; A802BC7E56237CF3 CRC64;
MDYPTLLLAL LHVYRALCEE VLWHTSVPFA ENMSLECVYP SVGILTQVEW FKIGTEKDSI
AIFSPTHGMV IRKPYAERVY FLNSTMASNN MTLFFRNASE DDVGYYSCSL YTYPQGTWQK
VIQVVQSDGF EAAVPPNSHI VSEPGKNITL TCQPQMTWPV QEVRWEKIQP HQIDLLTYCD
LVHGRNFTSK FPRQIVSNCS HGSWSFIVVP DVTASDSGLY RCHLQASAGE NETFVMRLTV
AEGQTDNQYT RFVTGGTVLL LLFVISITTI IVIFLNRRRR RERSDLYTES WDTQKAPKNY
RSPISASQPT NQSMDDTRED IYVNYPTFSR RPKTRV
