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CD49 or Very Late Antigen (VLA)
The CD49 antigen subtypes are determined by the integrin-alpha subunits.
Interactions
molecular events
Related
fibronectin; FN; cold-insoluble globulin; CIG; contains: anastellin; Ugl-Y1; Ugl-Y2; Ugl-Y3 (FN1, FN)
laminin
Specific
very late antigen 1 (VLA-1), a laminin receptor
very late antigen 2 (VLA-2, integrin alpha-2/beta-1)
very late antigen 3 (VLA-3, integrin alpha-3/beta-1)
very late antigen 4 (VLA-4, integrin alpha-4/beta-1)
very late antigen 5 (VLA-5, integrin alpha-5/beta-1)
very late antigen 6 (VLA-6, integrin alpha-6/beta-1)
General
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
integrin
Properties
COMPARTMENT: plasma membrane
CELL: T-cell
MOTIF: focal adhesion site
glycosylation site
membrane region
SUBUNITS: integrin-alpha
MOTIF: cysteine residue {CYS1}
MODIFICATION: cysteine residue {CYS2}
cysteine residue {CYS2}
MODIFICATION: cysteine residue {CYS1}
transmembrane domain
kxgffkr
NAME: kxgffkr
SITE: cytoplasmic domain
FOR-BINDING-OF: calreticulin
FORM: kxgffkr
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
Molecular Cell Biology (2nd ed) Darnell J; Lodish H
& Baltimore D (eds), Scientific American Books,
WH Freeman, NY 1990, pg 921
Component-of
molecular complex
Components
CD29; integrin-beta 1; fibronectin receptor beta; platelet glycoprotein IIa; VLA-4 beta (ITGB1, FNRB, MDF2, MSK12)
integrin-alpha