ID:ITB1_HUMAN DESCRIPTION: RecName: Full=Integrin beta-1; AltName: Full=Fibronectin receptor subunit beta; AltName: Full=VLA-4 subunit beta; AltName: CD_antigen=CD29; Flags: Precursor; FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta- 1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha- 1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha- 3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha- 10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. Isoform beta-1B interferes with isoform beta-1A resulting in a dominant negative effect on cell adhesion and migration (in vitro). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. May be involved in up- regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and GNB2L1/RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha- 5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or alpha-V. Binds LGALS3BP and NMRK2, when associated with alpha-7, but not with alpha-5. Interacts with FLNA, FLNB and RANBP9. Isoform Beta-1D interacts with ACE2. Isoform Beta-1A interacts with the C-terminal region of FLNC. Interacts with KRT1 in the presence of GNB2L1 and SRC. Interacts with HIV-1 Tat. Binds to human echoviruses 1 and 8 capsid proteins and acts as a receptor for these viruses. Interacts with RAB21. Interacts (via the cytoplasmic region) with RAB25 (via the hypervariable C-terminal region). Interacts with FGR and HCK (By similarity). Interacts with MYO10. Interacts with DAB2. Interacts with human cytomegalovirus/HHV-5 envelop glycoprotein B/gB. INTERACTION: Q9BY76:ANGPTL4; NbExp=2; IntAct=EBI-703066, EBI-2968146; P32927:CSF2RB; NbExp=5; IntAct=EBI-703066, EBI-1809771; P05413:FABP3; NbExp=2; IntAct=EBI-703066, EBI-704216; P17301:ITGA2; NbExp=3; IntAct=EBI-703066, EBI-702960; P13612:ITGA4; NbExp=3; IntAct=EBI-703066, EBI-703044; P07948:LYN; NbExp=4; IntAct=EBI-703066, EBI-79452; P49023:PXN; NbExp=2; IntAct=EBI-6082935, EBI-702209; P35282:Rab21 (xeno); NbExp=3; IntAct=EBI-703066, EBI-1993555; SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Melanosome. Cleavage furrow. Note=Isoform beta-1B does not localize to focal adhesions. Highly enriched in stage I melanosomes. Located on plasma membrane of neuroblastoma NMB7 cells. In a lung cancer cell line, in prometaphase and metaphase, localizes diffusely at the membrane and in afew intracellular vesicles. In early telophase, detected mainly on the matrix-facing side of the cells. By mid-telophase, concentrated to the ingressing cleavage furrow, mainly to the basal side of the furrow. In late telophase, concentrated to the extending protrusions formed at the opposite ends of the spreading daughter cells, in vesicles at the base of the lamellipodia formed by the separating daughter cells. TISSUE SPECIFICITY: Isoform beta-1A is widely expressed, other isoforms are generally coexpressed with a more restricted distribution. Isoform beta-1B is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform beta-1C and isoform beta-1C-2 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform beta-C-2, rather than isoform beta-1C, is selectively expressed in peripheral T-cells. Isoform beta-1C is expressed in non-proliferating and differentiated prostate gland epithelial cells and in platelets, on the surface of erythroleukemia cells and in various hematopoietic cell lines. Isoform beta-1D is expressed specifically in striated muscle (skeletal and cardiac muscle). PTM: The cysteine residues are involved in intrachain disulfide bonds (By similarity). SIMILARITY: Belongs to the integrin beta chain family. SIMILARITY: Contains 1 VWFA domain. SEQUENCE CAUTION: Sequence=CAD97649.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; WEB RESOURCE: Name=Wikipedia; Note=CD29 entry; URL="http://en.wikipedia.org/wiki/CD29";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P05556
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.