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very late antigen 2 (VLA-2, integrin alpha-2/beta-1)

Function: - integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin & E-cadherin - recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen - responsible for adhesion of platelets & other cells to collagens, modulation of collagen & collagenase gene expression, force generation & organization of newly synthesized extracellular matrix Subunits: integrin alpha-2, integrin beta-1 Compartment: membrane Pathology: - putative receptor for echovirus-1

Related

collagen echovirus fibronectin; FN; cold-insoluble globulin; CIG; contains: anastellin; Ugl-Y1; Ugl-Y2; Ugl-Y3 (FN1, FN) laminin platelet glycoprotein Ia/IIa Ab in blood platelet glycoprotein Ia/IIa Ab in serum platelet glycoprotein Ia/IIa IgG in blood

General

CD49 or Very Late Antigen (VLA)

Properties

COMPARTMENT: plasma membrane CELL: T-cell MOTIF: focal adhesion site glycosylation site membrane region SUBUNITS: integrin alpha-2 MOTIF: signal sequence {1-29} FG-GAP {45-103} MOTIF: cysteine residue {C83} MODIFICATION: cysteine residue {C92} cysteine residue {C92} MODIFICATION: cysteine residue {C83} consensus repeat {104} SEQUENCE-IS: FG-GAP N-glycosylation site {N105} N-glycosylation site {N112} VWFA domain {188-378} MOTIF: N-glycosylation site {N343} FG-GAP {379-433} MOTIF: N-glycosylation site {N432} FG-GAP {434-486} MOTIF: N-glycosylation site {N460} N-glycosylation site {N475} FG-GAP {488-549} MOTIF: Ca+2-binding site SITE: 499-507 FG-GAP {551-610} MOTIF: Ca+2-binding site SITE: 563-571 FG-GAP {615-667} MOTIF: Ca+2-binding site SITE: 627-635 cysteine residue {C680} MODIFICATION: cysteine residue {C737} N-glycosylation site {N699} cysteine residue {C737} MODIFICATION: cysteine residue {C680} cysteine residue {C789} MODIFICATION: cysteine residue {C795} cysteine residue {C795} MODIFICATION: cysteine residue {C789} cysteine residue {C865} MODIFICATION: cysteine residue {C876} cysteine residue {C876} MODIFICATION: cysteine residue {C865} cysteine residue {C1019} MODIFICATION: cysteine residue {C1050} cysteine residue {C1050} MODIFICATION: cysteine residue {C1019} cysteine residue {C1055} MODIFICATION: cysteine residue {C1060} N-glycosylation site {N1057} cysteine residue {C1060} MODIFICATION: cysteine residue {C1055} N-glycosylation site {N1074} N-glycosylation site {N1081} transmembrane domain {1133-1154} HPS5 interaction {1155-1161} MOTIF: GFFKR {1157-1161} integrin-beta 1 MOTIF: signal sequence {1-20} cysteine residue {C27} MODIFICATION: cysteine residue {C464} cysteine residue {C35} MODIFICATION: cysteine residue {C45} cysteine residue {C38} MODIFICATION: cysteine residue {C75} cysteine residue {C45} MODIFICATION: cysteine residue {C35} cysteine residue {C48} MODIFICATION: cysteine residue {C64} N-glycosylation site {N50} cysteine residue {C64} MODIFICATION: cysteine residue {C48} cysteine residue {C75} MODIFICATION: cysteine residue {C38} N-glycosylation site {N94} N-glycosylation site {N97} VWFA domain {140-378} MOTIF: cysteine residue {C207} MODIFICATION: cysteine residue {C213} N-glycosylation site {N212} cysteine residue {C213} MODIFICATION: cysteine residue {C207} cysteine residue {C261} MODIFICATION: cysteine residue {C301} N-glycosylation site {N269} cysteine residue {C301} MODIFICATION: cysteine residue {C261} N-glycosylation site {N363} cysteine residue {C401} MODIFICATION: cysteine residue {C415} N-glycosylation site {N406} cysteine residue {C415} MODIFICATION: cysteine residue {C401} N-glycosylation site {N417} cysteine residue {C435} MODIFICATION: cysteine residue {C691} cysteine residue {C462} MODIFICATION: cysteine residue {C466} cysteine residue {C464} MODIFICATION: cysteine residue {C27} Cysteine-rich tandem repeats {466-635} MOTIF: I {466-515} cysteine residue {C466} MODIFICATION: cysteine residue {C462} cysteine residue {C477} MODIFICATION: cysteine residue {C489} N-glycosylation site {N481} cysteine residue {C486} MODIFICATION: cysteine residue {C525} cysteine residue {C489} MODIFICATION: cysteine residue {C477} cysteine residue {C491} MODIFICATION: cysteine residue {C500} cysteine residue {C500} MODIFICATION: cysteine residue {C491} cysteine residue {C502} MODIFICATION: cysteine residue {C516} II {516-559} cysteine residue {C516} MODIFICATION: cysteine residue {C502} N-glycosylation site {N520} cysteine residue {C525} MODIFICATION: cysteine residue {C486} cysteine residue {C531} MODIFICATION: cysteine residue {C536} cysteine residue {C533} MODIFICATION: cysteine residue {C568} cysteine residue {C536} MODIFICATION: cysteine residue {C531} cysteine residue {C538} MODIFICATION: cysteine residue {C553} cysteine residue {C553} MODIFICATION: cysteine residue {C538} cysteine residue {C555} MODIFICATION: cysteine residue {C560} III {560-598} cysteine residue {C560} MODIFICATION: cysteine residue {C555} cysteine residue {C568} MODIFICATION: cysteine residue {C533} cysteine residue {C574} MODIFICATION: cysteine residue {C579} cysteine residue {C576} MODIFICATION: cysteine residue {C607} cysteine residue {C579} MODIFICATION: cysteine residue {C574} cysteine residue {C581} MODIFICATION: cysteine residue {C590} N-glycosylation site {N584} cysteine residue {C590} MODIFICATION: cysteine residue {C581} cysteine residue {C592} MODIFICATION: cysteine residue {C599} IV {599-635} cysteine residue {C599} MODIFICATION: cysteine residue {C592} cysteine residue {C607} MODIFICATION: cysteine residue {C576} cysteine residue {C613} MODIFICATION: cysteine residue {C618} cysteine residue {C615} MODIFICATION: cysteine residue {C661} cysteine residue {C618} MODIFICATION: cysteine residue {C613} cysteine residue {C620} MODIFICATION: cysteine residue {C630} cysteine residue {C630} MODIFICATION: cysteine residue {C620} cysteine residue {C633} MODIFICATION: cysteine residue {C636} cysteine residue {C636} MODIFICATION: cysteine residue {C633} cysteine residue {C640} MODIFICATION: cysteine residue {C649} cysteine residue {C646} MODIFICATION: cysteine residue {C723} cysteine residue {C649} MODIFICATION: cysteine residue {C640} cysteine residue {C661} MODIFICATION: cysteine residue {C615} cysteine residue {C665} MODIFICATION: cysteine residue {C699} N-glycosylation site {N669} cysteine residue {C691} MODIFICATION: cysteine residue {C435} cysteine residue {C699} MODIFICATION: cysteine residue {C665} cysteine residue {C723} MODIFICATION: cysteine residue {C646} transmembrane domain {729-751} Tyr phosphorylation site {Y783} MISC-INFO: LIGAND = COLLAGEN LIGAND = FIBRONECTIN LIGAND = LAMININ

References

  1. Molecular Cell Biology (2nd ed) Darnell J; Lodish H & Baltimore D (eds), Scientific American Books, WH Freeman, NY 1990, pg 921
  2. Harrison's Principles of Internal Medicine, 13th ed. Isselbacher et al (eds), McGraw-Hill Inc. NY, 1994, pg 769

Components

CD29; integrin-beta 1; fibronectin receptor beta; platelet glycoprotein IIa; VLA-4 beta (ITGB1, FNRB, MDF2, MSK12) CD49b (integrin alpha-2, VLA-2 alpha chain or platelet membrane glycoprotein IA, ITGA2)