Contents

Search

very late antigen 4 (VLA-4, integrin alpha-4/beta-1)

Function: - receptor for fibronectin, VCAM1 & laminin ? - recognizes one or more domains within the alternatively spliced CS-1 & CS-5 regions of fibronectin - recognizes the sequence Q-I-D-S in VCAM1 - on activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines - it may also participate in cytolytic T-cell interactions with target cells Subunits: integrin alpha-4, integrin beta-1 Compartment: membrane

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-4 MOTIF: signal sequence {1-39} FG-GAP {55-117} MOTIF: N-glycosylation site {N85} cysteine residue {C97} MODIFICATION: cysteine residue {C107} cysteine residue {C107} MODIFICATION: cysteine residue {C97} FG-GAP {118-193} MOTIF: N-glycosylation site {N144} cysteine residue {C150} MODIFICATION: cysteine residue {C171} cysteine residue {C171} MODIFICATION: cysteine residue {C150} cysteine residue {C189} MODIFICATION: cysteine residue {C204} FG-GAP {194-253} MOTIF: cysteine residue {C204} MODIFICATION: cysteine residue {C189} N-glycosylation site {N235} FG-GAP {254-306} FG-GAP {309-368} MOTIF: Ca+2-binding site SITE: 320-328 FG-GAP {371-430} MOTIF: Ca+2-binding site SITE: 383-391 FG-GAP {433-485} MOTIF: Ca+2-binding site SITE: 445-453 N-glycosylation site {N486} cysteine residue {C492} MODIFICATION: cysteine residue {C501} cysteine residue {C501} MODIFICATION: cysteine residue {C492} cysteine residue {C507} MODIFICATION: cysteine residue {C563} N-glycosylation site {N524} N-glycosylation site {N544} cysteine residue {C563} MODIFICATION: cysteine residue {C507} peptide motif {597-598} cysteine residue {C628} MODIFICATION: cysteine residue {C633} N-glycosylation site {N632} cysteine residue {C633} MODIFICATION: cysteine residue {C628} N-glycosylation site {N651} N-glycosylation site {N666} cysteine residue {C704} MODIFICATION: cysteine residue {C717} cysteine residue {C717} MODIFICATION: cysteine residue {C704} N-glycosylation site {N812} N-glycosylation site {N827} cysteine residue {C858} MODIFICATION: cysteine residue {C896} cysteine residue {C896} MODIFICATION: cysteine residue {C858} cysteine residue {C903} MODIFICATION: cysteine residue {C908} cysteine residue {C908} MODIFICATION: cysteine residue {C903} transmembrane domain {984-1007} GFFKR {1009-1013} Ser phosphorylation site {S1027} 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 P13612

Components

CD29; integrin-beta 1; fibronectin receptor beta; platelet glycoprotein IIa; VLA-4 beta (ITGB1, FNRB, MDF2, MSK12) CD49d (integrin alpha-4, VLA-4 alpha chain, ITGA4)