signaling lymphocytic activation molecule; CDw150; IPO-3; CD150 (SLAMF1, SLAM)

Function: - high-affinity self-ligand - role in bidirectional T- cell to B-cell stimulation - SLAM-induced signal-transduction events in T-lymphocytes are different from those in B-cells - two modes of SLAM signaling are likely to exist a) one in which the inhibitor SH2D1A acts as a negative regulator b) another in which protein-tyrosine phosphatase 2C (PTPN11)- dependent signal transduction operates - phosphorylated by FYN - interacts (via cytoplasmic domain) with SH2D1A, & with PTPN11 - interacts with INPP5D/SHIP1 - binds to Measles virus H protein & acts as a receptor for this virus Structure: - the most membrane-proximal SH2-binding motif interacts with SH2 domain of SH2D1A & does not need to be phosphorylated on Tyr - contains 1 Ig-like C2-type domain - contains 1 Ig-like V-type domain Compartment: - cell membrane; single-pass type 1 membrane protein - present on the surface of B-cells & T-cells Alternative splicing: named isoforms=3 Expression: - constitutively expressed on - peripheral blood memory T-cells (CD45RO positive subpopulation of T cells) - T-cell clones - immature thymocytes - some B cells - dendritic cells - endothelium - rapidly induced on naive T-cells after activation

General

cluster-of-differentiation antigen; cluster designation antigen; CD antigen glycoprotein immunoglobulin superfamily protein phosphoprotein SLAM family member protein

Properties

SIZE: entity length = 335 aa MW = 37 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-20} N-glycosylation site {N53} N-glycosylation site {N57} N-glycosylation site {N102} N-glycosylation site {N125} immunoglobulin superfamily domain {144-223} MOTIF: N-glycosylation site {N150} immunoglobulin superfamily domain {152} N-glycosylation site {N155} cysteine residue {C158} MODIFICATION: cysteine residue {C228} cysteine residue {C164} MODIFICATION: cysteine residue {C209} N-glycosylation site {N189} cysteine residue {C209} MODIFICATION: cysteine residue {C164} N-glycosylation site {N217} cysteine residue {C228} MODIFICATION: cysteine residue {C158} transmembrane domain {238-258} SH2-binding {281-286} MOTIF: Tyr phosphorylation site {Y281} SH2-binding {307-312} SH2-binding {327-332}

Database Correlations

OMIM 603492 UniProt Q13291 Pfam PF06214 Entrez Gene 6504 Kegg hsa:6504