CD244
entrez
51744
canonical
uniprot
Q9BZW8
canonical
ensembl
ENSG00000122223
resolver
ensp
ENSP00000313619
resolver
ensp
ENSP00000357012
resolver
ensp
ENSP00000357013
resolver
ensp
ENSP00000432636
resolver
ensp
ENSP00000554408
resolver
genesymbol
CD244
resolver
genesymbol_syn
2B4
resolver
hgnc
HGNC:18171
resolver
uniprot
Q5VYI2
resolver
uniprot
Q5VYI6
resolver
uniprot
Q5VYI7
resolver
uniprot
Q96T47
resolver
uniprot
Q9NQD2
resolver
uniprot
Q9NQD3
resolver
uniprot
Q9Y288
resolver
uniprot_entry
CD244_HUMAN
resolver
uniprot_sec
Q5VYI2
resolver
uniprot_sec
Q5VYI6
resolver
uniprot_sec
Q5VYI7
resolver
uniprot_sec
Q96T47
resolver
uniprot_sec
Q9NQD2
resolver
uniprot_sec
Q9NQD3
resolver
uniprot_sec
Q9Y288
resolver
amino_acid_sequence
MLGQVVTLILLLLLKVYQGKGCQGSADHVVSISGVPLQLQPNSIQTKVDSIAWKKLLPSQNGFHHILKWENGSLPSNTSNDRFSFIVKNLSLLIKAAQQQDSGLYCLEVTSISGKVQTATFQVFVFESLLPDKVEKPRLQGQGKILDRGRCQVALSCLVSRDGNVSYAWYRGSKLIQTAGNLTYLDEEVDINGTHTYTCNVSNPVSWESHTLNLTQDCQNAHQEFRFWPFLVIIVILSALFLGTLACFCVWRRKRKEKQSETSPKEFLTIYEDVKDLKTRRNHEQEQTFPGGGSTIYSMIQSQSSAPTSQEPAYTLYSLIQPSRKSGSRKRNHSPSFNSTIYEVIGKSQPKAQNPARLSRKELENFDVYS
uniprot
proteins
function
FUNCTION: Heterophilic receptor of the signaling lymphocytic activation molecule (SLAM) family; its ligand is CD48. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Acts as activating natural killer (NK) cell receptor (PubMed:10359122, PubMed:11714776, PubMed:8376943). Activating function implicates association with SH2D1A and FYN (PubMed:15713798). Downstreaming signaling involves predominantly VAV1, and, to a lesser degree, INPP5D/SHIP1 and CBL. Signal attenuation in the absence of SH2D1A is proposed to be dependent on INPP5D and to a lesser extent PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:10934222, PubMed:15713798). Stimulates NK cell cytotoxicity, production of IFN-gamma and granule exocytosis (PubMed:11714776, PubMed:8376943). Optimal expansion and activation of NK cells seems to be dependent on the engagement of CD244 with CD48 expressed on neighboring NK cells (By similarity). Acts as costimulator in NK activation by enhancing signals by other NK receptors such as NCR3 and NCR1 (PubMed:10741393). At early stages of NK cell differentiation may function as an inhibitory receptor possibly ensuring the self-tolerance of developing NK cells (PubMed:11917118). Involved in the regulation of CD8(+) T-cell proliferation; expression on activated T-cells and binding to CD48 provides costimulatory-like function for neighboring T-cells (By similarity). Inhibits inflammatory responses in dendritic cells (DCs) (By similarity). {ECO:0000250|UniProtKB:Q07763, ECO:0000269|PubMed:10359122, ECO:0000269|PubMed:10741393, ECO:0000269|PubMed:10934222, ECO:0000269|PubMed:11714776, ECO:0000269|PubMed:11917118, ECO:0000269|PubMed:8376943, ECO:0000305|PubMed:15713798}.
uniprot
proteins
mass_dalton
41616
uniprot
proteins
mutagenesis
MUTAGEN 68; /note="K->A: Disrupts interaction with CD48; when associated with A-70."; /evidence="ECO:0000269|PubMed:16002700"; MUTAGEN 70; /note="E->A: Disrupts interaction with CD48; when associated with A-68."; /evidence="ECO:0000269|PubMed:16002700
uniprot
proteins
post_translational_modification
PTM: N-linked glycosylation is essential for the binding to its ligand CD48 (PubMed:21606496). Also O-glycosylated, in contrast, O-linked sialylation has a negative impact on ligand binding (PubMed:21606496). {ECO:0000269|PubMed:21606496}.; PTM: Phosphorylated by FYN and CSK on tyrosine residues following activation (PubMed:11034353). Coligation with inhibitory receptors such as KIR2DL1 inhibits phosphorylation upon contact of NK cells with sensitive target cells (PubMed:10358138). {ECO:0000269|PubMed:10358138, ECO:0000269|PubMed:11034353}.
uniprot
proteins
pubmed
10358138
uniprot
proteins
pubmed
10359122
uniprot
proteins
pubmed
10458320
uniprot
proteins
pubmed
10556801
uniprot
proteins
pubmed
10741393
uniprot
proteins
pubmed
10934222
uniprot
proteins
pubmed
11003394
uniprot
proteins
pubmed
11034353
uniprot
proteins
pubmed
11714776
uniprot
proteins
pubmed
11815622
uniprot
proteins
pubmed
11917118
uniprot
proteins
pubmed
12458214
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15713798
uniprot
proteins
pubmed
16002700
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
19499526
uniprot
proteins
pubmed
20164429
uniprot
proteins
pubmed
21606496
uniprot
proteins
pubmed
24642916
uniprot
proteins
pubmed
26221972
uniprot
proteins
pubmed
27249817
uniprot
proteins
pubmed
8376943
uniprot
proteins
pubmed
9841922
uniprot
proteins
sequence_length
370
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:10359122}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}. Membrane raft {ECO:0000269|PubMed:11034353}. Note=Receptor engagement results in a recruitment to lipid drafts essential for the subsequent tyrosine phosphorylation of the ITSMs. {ECO:0000269|PubMed:11034353}.
uniprot
proteins
transmembrane_region
TRANSMEM 230..250; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins