Cd244
entrez
18106
canonical
uniprot
Q07763
canonical
ensembl
ENSMUSG00000004709
resolver
ensp
ENSMUSP00000004829
resolver
ensp
ENSMUSP00000216314
resolver
genesymbol
Cd244
resolver
genesymbol_syn
2b4
resolver
genesymbol_syn
Cd244a
resolver
genesymbol_syn
Nmrk
resolver
uniprot
O88654
resolver
uniprot
Q3UV86
resolver
uniprot
Q9JIE0
resolver
uniprot_entry
CD244_MOUSE
resolver
uniprot_sec
O88654
resolver
uniprot_sec
Q3UV86
resolver
uniprot_sec
Q9JIE0
resolver
amino_acid_sequence
MLGQAVLFTTFLLLRAHQGQDCPDSSEEVVGVSGKPVQLRPSNIQTKDVSVQWKKTEQGSHRKIEILNWYNDGPSWSNVSFSDIYGFDYGDFALSIKSAKLQDSGHYLLEITNTGGKVCNKNFQLLILDHVETPNLKAQWKPWTNGTCQLFLSCLVTKDDNVSYALYRGSTLISNQRNSTHWENQIDASSLHTYTCNVSNRASWANHTLNFTHGCQSVPSNFRFLPFGVIIVILVTLFLGAIICFCVWTKKRKQLQFSPKEPLTIYEYVKDSRASRDQQGCSRASGSPSAVQEDGRGQRELDRRVSEVLEQLPQQTFPGDRGTMYSMIQCKPSDSTSQEKCTVYSVVQPSRKSGSKKRNQNSSLSCTVYEEVGNPWLKAHNPARLSRRELENFDVYS
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:12734329, PubMed:19648922, PubMed:20962259, PubMed:8326140). Activating function implicates association with SH2D1A and FYN. 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. Stimulates NK cell cytotoxicity, production of IFN-gamma and granule exocytosis (PubMed:15169881, PubMed:15998796, PubMed:22683124, PubMed:8326140). Optimal expansion and activation of NK cells seems to be dependent on the engagement of CD244 with CD48 expressed on neighboring NK cells (PubMed:15905190). Regulation of NK cell activity by adapters SH2D1B and SH2D1B2 is reported conflictingly (PubMed:16127454, PubMed:16425036). Acts as costimulator in NK activation by enhancing signals by other NK receptors such as NCR3 and NCR1. At early stages of NK cell differentiation may function as an inhibitory receptor possibly ensuring the self-tolerance of developing NK cells (By similarity). 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 (PubMed:11739483). Inhibits inflammatory responses in dendritic cells (DCs) (PubMed:25643613). {ECO:0000250|UniProtKB:Q9BZW8, ECO:0000269|PubMed:11739483, ECO:0000269|PubMed:12734329, ECO:0000269|PubMed:15169881, ECO:0000269|PubMed:15998796, ECO:0000269|PubMed:19648922, ECO:0000269|PubMed:20962259, ECO:0000269|PubMed:22683124, ECO:0000269|PubMed:8326140, ECO:0000305|PubMed:16127454, ECO:0000305|PubMed:16425036}.
uniprot
proteins
mass_dalton
44836
uniprot
proteins
mutagenesis
MUTAGEN 266; /note="Y->F: Decreases downstream phosphorylation of CBL and VAV1. Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-325, F-344 and F-369."; /evidence="ECO:0000269|PubMed:15169881"; MUTAGEN 325; /note="Y->F: Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-266, F-344 and F-369. Weakly decreases downstream phosphorylation of CBL and VAV1; when associated with F-344 and F-369."; /evidence="ECO:0000269|PubMed:15169881"; MUTAGEN 344; /note="Y->F: Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-266, F-325 and F-369. Weakly decreases downstream phosphorylation of CBL and VAV1; when associated with F-325 and F-369."; /evidence="ECO:0000269|PubMed:15169881"; MUTAGEN 369; /note="Y->F: Abolishes downstream phosphorylation of CBL and VAV1; when associated with F-266, F-325 and F-344. Weakly decreases downstream phosphorylation of CBL and VAV1; when associated with F-325 and F-344."; /evidence="ECO:0000269|PubMed:15169881
uniprot
proteins
post_translational_modification
PTM: N-linked glycosylation is essential for the binding to its ligand CD48. Also O-glycosylated, in contrast, O-linked sialylation has a negative impact on ligand binding. {ECO:0000250|UniProtKB:Q9BZW8}.; PTM: Phosphorylated by FYN and CSK on tyrosine residues following activation. Coligation with inhibitory receptors such as KIR2DL1 inhibits phosphorylation upon contact of NK cells with sensitive target cells. {ECO:0000250|UniProtKB:Q9BZW8}.
uniprot
proteins
pubmed
10941850
uniprot
proteins
pubmed
11739483
uniprot
proteins
pubmed
12734329
uniprot
proteins
pubmed
15169881
uniprot
proteins
pubmed
15850375
uniprot
proteins
pubmed
15905190
uniprot
proteins
pubmed
15998796
uniprot
proteins
pubmed
16127454
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16425036
uniprot
proteins
pubmed
17950006
uniprot
proteins
pubmed
19648922
uniprot
proteins
pubmed
20962259
uniprot
proteins
pubmed
22683124
uniprot
proteins
pubmed
25643613
uniprot
proteins
pubmed
8228228
uniprot
proteins
pubmed
8326140
uniprot
proteins
pubmed
9841922
uniprot
proteins
sequence_length
397
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9BZW8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BZW8}. Cell membrane {ECO:0000250|UniProtKB:Q9BZW8}. Membrane raft {ECO:0000250|UniProtKB:Q9BZW8}. Note=Receptor engagement results in a recruitment to lipid drafts essential for the subsequent tyrosine phosphorylation of the ITSMs. {ECO:0000250|UniProtKB:Q9BZW8}.
uniprot
proteins
transmembrane_region
TRANSMEM 227..247; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins