signal-regulatory protein gamma; SIRP-gamma; CD172 antigen-like family member B; signal-regulatory protein beta-2; SIRP-b2; SIRP-beta-2; CD172g (SIRPG, SIRPB2)

Function: - probable immunoglobulin-like cell surface receptor - on binding with CD47, mediates cell-cell adhesion - engagement on T-cells by CD47 on antigen-presenting cells results in enhanced antigen-specific T-cell proliferation & costimulates T-cell activation - interacts with CD47 Structure: - contains 2 Ig-like C1-type domains (immunoglobulin-like) - contains 1 Ig-like V-type domain (immunoglobulin-like) Compartment: membrane Alternative splicing: named isoforms=4 Expression: - detected in liver, & at very low levels in brain, heart, lung, pancreas, kidney, placenta & skeletal muscle - expressed on CD4+ T-cells, CD8+ T-cells, CD56-bright natural killer cells (NK cells), CD20+ cells, & all activated NK cells - mainly present in the paracortical T-cell area of lymph nodes, with only sparse positive cells in the mantle & in the germinal center of B-cell follicles - in the thymus, primarily expressed in the medulla on mature T lymphocytes that have undergone thymic selection

General

cluster-of-differentiation antigen; cluster designation antigen; CD antigen glycoprotein signal-regulatory protein (SIRP)

Properties

SIZE: MW = 42 kD entity length = 387 aa COMPARTMENT: cellular membrane MOTIF: signal sequence {1-28} immunoglobulin superfamily domain {29-137} MOTIF: cysteine residue {C53} MODIFICATION: cysteine residue {C119} cysteine residue {C119} MODIFICATION: cysteine residue {C53} immunoglobulin superfamily domain {146-245} MOTIF: cysteine residue {C168} MODIFICATION: cysteine residue {C226} cysteine residue {C226} MODIFICATION: cysteine residue {C168} N-glycosylation site {N243} immunoglobulin superfamily domain {252-340} MOTIF: N-glycosylation site {N268} cysteine residue {C271} MODIFICATION: cysteine residue {C329} N-glycosylation site {N309} N-glycosylation site {N317} cysteine residue {C329} MODIFICATION: cysteine residue {C271} transmembrane domain {361-383}

Database Correlations

OMIM 605466 UniProt Q9P1W8 Pfam PF00047

References

UniProt :accession Q9P1W8