Contents

Search

very late antigen 1 (VLA-1), a laminin receptor

Function: - receptor for laminin & collagen - receptor for collagen-4 (basement membrane) - recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen Subunits: integrin alpha-1, integrin beta-1 Compartment: membrane Expression: expressed in T-cells Pathology: - role for epidermal T-cell integrin alpha-1/beta-1 & basement membrane collagen-4 in pathophysiology of psoriasis

Related

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

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-1 MOTIF: signal sequence {1-28} FG-GAP {44-103} MOTIF: N-glycosylation site {N74} cysteine residue {C82} MODIFICATION: cysteine residue {C92} cysteine residue {C92} MODIFICATION: cysteine residue {C82} N-glycosylation site {N100} consensus repeat {104} SEQUENCE-IS: FG-GAP N-glycosylation site {N105} N-glycosylation site {N112} VWFA domain {147-360} MOTIF: N-glycosylation site {N217} N-glycosylation site {N317} N-glycosylation site {N341} FG-GAP {349-404} MOTIF: N-glycosylation site {N402} FG-GAP {405-457} MOTIF: N-glycosylation site {N418} FG-GAP {459-520} MOTIF: N-glycosylation site {N460} Ca+2-binding site SITE: 498-506 N-glycosylation site {N532} FG-GAP {540-599} MOTIF: Ca+2-binding site SITE: 580-588 FG-GAP {602-654} MOTIF: Ca+2-binding site SITE: 642-650 cysteine residue {C688} MODIFICATION: cysteine residue {C697} cysteine residue {C697} MODIFICATION: cysteine residue {C688} N-glycosylation site {N699} cysteine residue {C703} MODIFICATION: cysteine residue {C756} N-glycosylation site {N748} cysteine residue {C756} MODIFICATION: cysteine residue {C703} N-glycosylation site {N780} cysteine residue {C808} MODIFICATION: cysteine residue {C814} cysteine residue {C814} MODIFICATION: cysteine residue {C808} N-glycosylation site {N840} cysteine residue {C878} MODIFICATION: cysteine residue {C886} N-glycosylation site {N883} cysteine residue {C886} MODIFICATION: cysteine residue {C878} N-glycosylation site {N908} N-glycosylation site {N915} N-glycosylation site {N939} N-glycosylation site {N966} N-glycosylation site {N974} N-glycosylation site {N1008} cysteine residue {C1030} MODIFICATION: cysteine residue {C1062} cysteine residue {C1062} MODIFICATION: cysteine residue {C1030} cysteine residue {C1065} MODIFICATION: cysteine residue {C1072} cysteine residue {C1072} MODIFICATION: cysteine residue {C1065} N-glycosylation site {N1073} N-glycosylation site {N1083} N-glycosylation site {N1102} N-glycosylation site {N1113} transmembrane domain {1142-1164} GFFKR {1167-1171} 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 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. UniProt :accession P56199
  3. Conrad C, Boyman O, Tonel G, Tun-Kyi A, Laggner U, de Fougerolles A, Kotelianski V, Gardner H, Nestle FO. alpha(1)beta(1) integrin is crucial for accumulation of epidermal T cells and the development of psoriasis. Nat Med. 2007 Jul;13(7):836-42. Epub 2007 Jul 1. PMID: 17603494

Components

CD29; integrin-beta 1; fibronectin receptor beta; platelet glycoprotein IIa; VLA-4 beta (ITGB1, FNRB, MDF2, MSK12) CD49a; integrin alpha-1; CD49 antigen-like family member A; laminin & collagen receptor; VLA-1 (ITGA1)