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very late antigen 5 (VLA-5, integrin alpha-5/beta-1)

Function: - receptor for fibronectin & fibrinogen - the major fibronectin receptor on most cells [3] - recognizes the sequence R-G-D in its ligands Subunits: integrin alpha-5, integrin beta-1 Pathology: - in case of HIV-1 infection, interaction with extracellular viral Tat protein seems to enhance angiogenesis in lesions of Kaposi's sarcoma

Related

fibronectin; FN; cold-insoluble globulin; CIG; contains: anastellin; Ugl-Y1; Ugl-Y2; Ugl-Y3 (FN1, FN)

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-5 MOTIF: signal sequence {1-41} FG-GAP {57-119} MOTIF: N-glycosylation site {N84} cysteine residue {C99} MODIFICATION: cysteine residue {C108} cysteine residue {C108} MODIFICATION: cysteine residue {C99} FG-GAP {131-198} MOTIF: cysteine residue {C156} MODIFICATION: cysteine residue {C176} cysteine residue {C176} MODIFICATION: cysteine residue {C156} N-glycosylation site {N182} cysteine residue {C192} MODIFICATION: cysteine residue {C205} FG-GAP {199-256} MOTIF: cysteine residue {C205} MODIFICATION: cysteine residue {C192} FG-GAP {269-322} MOTIF: N-glycosylation site {N297} N-glycosylation site {N307} N-glycosylation site {N316} FG-GAP {323-389} MOTIF: Ca+2-binding site SITE: 334-342 FG-GAP {390-449} MOTIF: Ca+2-binding site SITE: 401-409 FG-GAP {453-505} MOTIF: Ca+2-binding site SITE: 465-473 cysteine residue {C513} MODIFICATION: cysteine residue {C522} cysteine residue {C522} MODIFICATION: cysteine residue {C513} N-glycosylation site {N524} cysteine residue {C528} MODIFICATION: cysteine residue {C584} N-glycosylation site {N530} cysteine residue {C584} MODIFICATION: cysteine residue {C528} N-glycosylation site {N593} N-glycosylation site {N609} cysteine residue {C645} MODIFICATION: cysteine residue {C651} cysteine residue {C651} MODIFICATION: cysteine residue {C645} N-glycosylation site {N675} N-glycosylation site {N712} cysteine residue {C718} MODIFICATION: cysteine residue {C731} N-glycosylation site {N724} cysteine residue {C731} MODIFICATION: cysteine residue {C718} N-glycosylation site {N773} N-glycosylation site {N868} cysteine residue {C869} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C911} MODIFICATION: cysteine residue {C916} cysteine residue {C916} MODIFICATION: cysteine residue {C911} transmembrane domain {996-1021} HPS5 interaction {1021-1028} MOTIF: GFFKR {1024-1028} 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 = FIBRONECTIN DISTRIBUTION :CELL_TYPE MANY

References

  1. Molecular Cell Biology (2nd ed) Darnell J; Lodish H & Baltimore D (eds), Scientific American Books, WH Freeman, NY 1990, pg 921
  2. UniProt :accession P08648
  3. Akiyama SK, Integrins in cell adhesion and signalling. Hum Cell 1996, 9:161 PMID: 9183647

Components

CD29; integrin-beta 1; fibronectin receptor beta; platelet glycoprotein IIa; VLA-4 beta (ITGB1, FNRB, MDF2, MSK12) CD49e (integrin alpha-5, integrin alpha-F, fibronection receptor alpha subunit, ITGA5)