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integrin alpha-4/beta-7
Function:
- role in adhesive interactions of leukocytes
- receptor for fibronectin, VCAM1 & MADCAM1
- recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin
- recognizes the sequence L-D-T in MADCAM1
Structure:
- subunits: integrin alpha-V, integrin beta-7
Compartment: membrane
General
integrin
Properties
COMPARTMENT: plasma membrane
MOTIF: focal adhesion site
transmembrane domain
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 7
MOTIF: signal sequence {1-19}
cysteine residue {C45}
MODIFICATION: cysteine residue {C476}
cysteine residue {C51}
MODIFICATION: cysteine residue {C61}
cysteine residue {C54}
MODIFICATION: cysteine residue {C91}
cysteine residue {C61}
MODIFICATION: cysteine residue {C51}
cysteine residue {C64}
MODIFICATION: cysteine residue {C80}
N-glycosylation site {N68}
cysteine residue {C80}
MODIFICATION: cysteine residue {C64}
cysteine residue {C91}
MODIFICATION: cysteine residue {C54}
VWFA domain {150-389}
MOTIF: cysteine residue {C216}
MODIFICATION: cysteine residue {C223}
cysteine residue {C223}
MODIFICATION: cysteine residue {C216}
cysteine residue {C271}
MODIFICATION: cysteine residue {C311}
N-glycosylation site {N279}
cysteine residue {C311}
MODIFICATION: cysteine residue {C271}
binding site
FOR-BINDING-OF: RGD cell-attachment sequence
cysteine residue {C412}
MODIFICATION: cysteine residue {C428}
cysteine residue {C428}
MODIFICATION: cysteine residue {C412}
N-glycosylation site {N434}
cysteine residue {C448}
MODIFICATION: cysteine residue {C688}
cysteine residue {C474}
MODIFICATION: cysteine residue {C478}
cysteine residue {C476}
MODIFICATION: cysteine residue {C45}
N-glycosylation site {N477}
Cysteine-rich tandem repeats {478-640}
MOTIF: consensus repeat {478-526}
cysteine residue {C478}
MODIFICATION: cysteine residue {C474}
cysteine residue {C488}
MODIFICATION: cysteine residue {C500}
cysteine residue {C497}
MODIFICATION: cysteine residue {C537}
cysteine residue {C500}
MODIFICATION: cysteine residue {C488}
cysteine residue {C502}
MODIFICATION: cysteine residue {C511}
cysteine residue {C511}
MODIFICATION: cysteine residue {C502}
cysteine residue {C513}
MODIFICATION: cysteine residue {C527}
consensus repeat {527-565}
cysteine residue {C527}
MODIFICATION: cysteine residue {C513}
N-glycosylation site {N531}
cysteine residue {C537}
MODIFICATION: cysteine residue {C497}
cysteine residue {C543}
MODIFICATION: cysteine residue {C548}
cysteine residue {C545}
MODIFICATION: cysteine residue {C574}
cysteine residue {C548}
MODIFICATION: cysteine residue {C543}
cysteine residue {C550}
MODIFICATION: cysteine residue {C559}
cysteine residue {C559}
MODIFICATION: cysteine residue {C550}
cysteine residue {C561}
MODIFICATION: cysteine residue {C566}
consensus repeat {566-604}
cysteine residue {C566}
MODIFICATION: cysteine residue {C561}
cysteine residue {C574}
MODIFICATION: cysteine residue {C545}
cysteine residue {C580}
MODIFICATION: cysteine residue {C585}
cysteine residue {C582}
MODIFICATION: cysteine residue {C613}
cysteine residue {C585}
MODIFICATION: cysteine residue {C580}
cysteine residue {C587}
MODIFICATION: cysteine residue {C596}
N-glycosylation site {N590}
cysteine residue {C596}
MODIFICATION: cysteine residue {C587}
cysteine residue {C598}
MODIFICATION: cysteine residue {C605}
consensus repeat {605-640}
cysteine residue {C605}
MODIFICATION: cysteine residue {C598}
cysteine residue {C613}
MODIFICATION: cysteine residue {C582}
cysteine residue {C619}
MODIFICATION: cysteine residue {C624}
cysteine residue {C621}
MODIFICATION: cysteine residue {C666}
cysteine residue {C624}
MODIFICATION: cysteine residue {C619}
cysteine residue {C626}
MODIFICATION: cysteine residue {C635}
cysteine residue {C635}
MODIFICATION: cysteine residue {C626}
cysteine residue {C638}
MODIFICATION: cysteine residue {C641}
binding site
SITE: C-TERMINAL
FOR-BINDING-OF: cytoskeletal protein
cysteine residue {C641}
MODIFICATION: cysteine residue {C638}
cysteine residue {C645}
MODIFICATION: cysteine residue {C654}
cysteine residue {C654}
MODIFICATION: cysteine residue {C645}
N-glycosylation site {N665}
cysteine residue {C666}
MODIFICATION: cysteine residue {C621}
N-glycosylation site {N674}
cysteine residue {C688}
MODIFICATION: cysteine residue {C448}
transmembrane domain {724-746}
Tyr phosphorylation site {Y778}
References
- UniProt :accession P26010
- UniProt :accession P13612
Components
CD49d (integrin alpha-4, VLA-4 alpha chain, ITGA4)
integrin-beta 7 (ITGB7)