| IED ID | IndEnz0002002805 |
| Enzyme Type ID | protease002805 |
| Protein Name |
Integrin beta-1 Fibronectin receptor subunit beta VLA-4 subunit beta CD antigen CD29 |
| Gene Name | Itgb1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MNLQLVSWIGLISLICSVFGQTDKNRCLKANAKSCGECIQAGPNCGWCTNTTFLQEGMPTSARCDDLEALKKKGCQPSDIENPRGSQTIKKNKNVTNRSKGMAEKLRPEDITQIQPQQLLLKLRSGEPQKFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTDRGEFFNELVGQQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNVYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSGNSSNVIQLIIDAYNSLSSEVILENSKLPDGVTINYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITANKCPNKESETIKIKPLGFTEEVEVVLQFICKCNCQSHGIPASPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCRCRVCECYPNYTGSACDCSLDTGPCLASNGQICNGRGICECGACKCTDPKFQGPTCETCQTCLGVCAEHKECVQCRAFNKGEKKDTCAQECSHFNLTKVESREKLPQPVQVDPVTHCKEKDIDDCWFYFTYSVNGNNEAIVHVVETPDCPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK |
| Enzyme Length | 798 |
| Uniprot Accession Number | P09055 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | 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-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (PubMed:10634791). Integrin alpha-4/beta-1 is a receptor for VCAM1 and 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. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. 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. When associated with alpha-7/beta-1 integrin, regulates cell adhesion and laminin matrix deposition (PubMed:12941630). Involved in promoting endothelial cell motility and angiogenesis (PubMed:15181153). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules (PubMed:21768292). May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis (PubMed:18804435). ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (By similarity). ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (By similarity). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (By similarity). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (By similarity). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). {ECO:0000250|UniProtKB:P05556, ECO:0000250|UniProtKB:P07228, ECO:0000269|PubMed:10634791, ECO:0000269|PubMed:12941630, ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:18804435, ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:21768292}.; FUNCTION: [Isoform 2]: Isoform 2 displaces isoform 1 in striated muscles. {ECO:0000269|PubMed:8567725}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (1); Chain (1); Compositional bias (1); Cross-link (1); Disulfide bond (28); Domain (1); Erroneous initiation (1); Glycosylation (12); Metal binding (10); Modified residue (5); Mutagenesis (2); Region (7); Repeat (4); Sequence conflict (7); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Cell adhesion;Cell junction;Cell membrane;Cell projection;Disulfide bond;Endosome;Glycoprotein;Integrin;Isopeptide bond;Magnesium;Membrane;Metal-binding;Myogenesis;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix;Ubl conjugation |
| Interact With | P26955; Q01768; Q6F5E0; Q91YD9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome {ECO:0000269|PubMed:21768292, ECO:0000269|PubMed:8567725}. Melanosome {ECO:0000250|UniProtKB:P05556}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle {ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P05556}. Cell surface {ECO:0000250|UniProtKB:P05556}. Note=Colocalizes with ITGB1BP1 and metastatic suppressor protein NME2 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen. Translocates from peripheral focal adhesions to fibrillar adhesions in an ITGB1BP1-dependent manner. Enriched preferentially at invadopodia, cell membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. {ECO:0000250|UniProtKB:P05556}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane, sarcolemma. Cell junction. Note=In cardiac muscle, isoform 2 is found in costameres and intercalated disks. |
| Modified Residue | MOD_RES 777; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:19144319; MOD_RES 783; /note=Phosphotyrosine; /evidence=ECO:0007744|PubMed:17947660; MOD_RES 785; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05556; MOD_RES 789; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P05556; MOD_RES 794; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P05556 |
| Post Translational Modification | PTM: The cysteine residues are involved in intrachain disulfide bonds. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..20 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5XQ0; |
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| Motif | |
| Gene Encoded By | |
| Mass | 88,231 |
| Kinetics | |
| Metal Binding | METAL 152; /note=Magnesium; /evidence=ECO:0000250; METAL 154; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 156; /note=Calcium 1; /evidence=ECO:0000250; METAL 157; /note=Calcium 1; /evidence=ECO:0000250; METAL 189; /note=Calcium 2; /evidence=ECO:0000250; METAL 244; /note=Calcium 2; /evidence=ECO:0000250; METAL 246; /note=Calcium 2; /evidence=ECO:0000250; METAL 248; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 249; /note=Calcium 2; /evidence=ECO:0000250; METAL 249; /note=Magnesium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |