CD51 (integrin alpha-V, vitronectin receptor alpha chain, ITGAV, MSK8, VNRA)

Function: 1) integrin alpha-V associates with either a) integrin beta-1 b) integrin beta-3 c) integrin beta-5 d) integrin beta-6 e) integrin beta-8 2) the alpha-V integrins are receptors for a) vitronectin b) cytotactin c) fibronectin d) fibrinogen e) laminin f) matrix metalloproteinase-2 g) osteopontin h) osteomodulin i) prothrombin j) thrombospondin k) von Willebrand factor 3) the alpha-V integrins recognize the sequence R-G-D in a wide array of ligands Structure: - composed of an heavy & a light chain linked by a disulfide bond - belongs to the integrin alpha chain family - contains 7 FG-GAP repeats Compartment: membrane; Single-pass type 1 membrane protein Alternative splicing: named isoforms=2 Expression: - platelets - endothelial cells - megakaryocytes Pathology: - interacts with extracellular HIV-1 viral Tat protein - seems to enhance angiogenesis in Kaposi's sarcoma lesions

General

cluster-of-differentiation antigen; cluster designation antigen; CD antigen integrin-alpha

Properties

SIZE: entity length = 1048 aa MW = 116 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-30} FG-GAP {46-108} MOTIF: N-glycosylation site {N74} cysteine residue {C89} MODIFICATION: cysteine residue {C97} cysteine residue {C97} MODIFICATION: cysteine residue {C89} FG-GAP {113-178} MOTIF: cysteine residue {C138} MODIFICATION: cysteine residue {C158} cysteine residue {C158} MODIFICATION: cysteine residue {C138} cysteine residue {C172} MODIFICATION: cysteine residue {C185} FG-GAP {179-236} MOTIF: cysteine residue {C185} MODIFICATION: cysteine residue {C172} FG-GAP {249-302} MOTIF: Ca+2-binding site SITE: 260-268 N-glycosylation site {N290} N-glycosylation site {N296} FG-GAP {303-362} MOTIF: Ca+2-binding site SITE: 314-322 FG-GAP {367-427} MOTIF: Ca+2-binding site SITE: 379-387 FG-GAP {432-483} MOTIF: Ca+2-binding site SITE: 443-451 N-glycosylation site {N488} cysteine residue {C491} MODIFICATION: cysteine residue {C502} cysteine residue {C502} MODIFICATION: cysteine residue {C491} cysteine residue {C508} MODIFICATION: cysteine residue {C565} N-glycosylation site {N554} cysteine residue {C565} MODIFICATION: cysteine residue {C508} N-glycosylation site {N615} cysteine residue {C626} MODIFICATION: cysteine residue {C632} cysteine residue {C632} MODIFICATION: cysteine residue {C626} cysteine residue {C698} MODIFICATION: cysteine residue {C711} N-glycosylation site {N704} cysteine residue {C711} MODIFICATION: cysteine residue {C698} N-glycosylation site {N835} N-glycosylation site {N851} cysteine residue {C852} MODIFICATION: cysteine residue {C-INTERCHAIN} N-glycosylation site {N874} cysteine residue {C904} MODIFICATION: cysteine residue {C909} cysteine residue {C909} MODIFICATION: cysteine residue {C904} N-glycosylation site {N945} N-glycosylation site {N973} N-glycosylation site {N980} transmembrane domain {993-1016} GFFKR {1019-1023}

Database Correlations

OMIM 193210 UniProt P06756 PFAM correlations Entrez Gene 3685 Kegg hsa:3685