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CD29; integrin-beta 1; fibronectin receptor beta; platelet glycoprotein IIa; VLA-4 beta (ITGB1, FNRB, MDF2, MSK12)
Function:
- Integrin-beta 1 associates with one of 10/16 alpha subunits
- extracellular matrix ligands include fibronectin, laminin, collagen & vitronectin
- integrin-beta 1 is the common subunit of very-late activator proteins (VLA)
Structure:
- belongs to the integrin beta chain family
- contains 1 VWFA domain
Compartment:
- cell membrane
- melanosome, highly enriched in stage 1 melanosomes
- isoform beta-1B does not localize to focal adhesions
Alternative splicing: named isoforms=5
Expression:
- isoform beta-1A is widely expressed
- isoform beta-1B is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells & astrocytoma cells
- isoform beta-1C & isoform beta-1C-2 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblasts, embryonal kidney cells, platelets & several blood cell lines
- isoform beta-C-2, rather than isoform beta-1C, is selectively expressed in primary T-cells
- isoform beta-1C is expressed in nonproliferating & differentiated prostate gland epithelial cells
- isoform beta-1D is expressed specifically in striated muscle (skeletal & cardiac muscle)
General
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
glycoprotein
integrin-beta
Properties
SIZE: entity length = 798 aa
MW = 88 kD
COMPARTMENT: cellular membrane
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}
Database Correlations
OMIM 135630
UniProt P05556
Entrez Gene 3688
References
- Molecular Cell Biology (2nd ed) Darnell J; Lodish H
& Baltimore D (eds), Scientific American Books,
WH Freeman, NY 1990, pg 921
- OMIM :accession 135630
- Clark EA & Brugge JS
Integrins and signal transduction pathways: the road taken.
Science 268:233 1995
PMID: 7716514
- http://www.pathologyoutlines.com/cdmarkers.html
15 October 2002
- Entrez Gene :accession 3688
- Wikipedia; Note: CD29 entry
http://en.wikipedia.org/wiki/CD29
- UniProt :accession P05556
Component-of
CD49 or Very Late Antigen (VLA)