ITB1_RAT
ID ITB1_RAT Reviewed; 799 AA.
AC P49134; A2RRT8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Integrin beta-1;
DE AltName: Full=Beta oligodendroglia;
DE Short=Beta OL;
DE AltName: Full=Fibronectin receptor subunit beta;
DE AltName: Full=VLA-4 subunit beta;
DE AltName: CD_antigen=CD29;
DE Flags: Precursor;
GN Name=Itgb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oligodendrocyte;
RX PubMed=7541764; DOI=10.1016/0378-1119(94)00911-b;
RA Malek-Hedayat S., Rome L.H.;
RT "Cloning and sequence of the cDNA encoding the rat oligodendrocyte integrin
RT beta 1 subunit.";
RL Gene 158:287-290(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and
CC alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1
CC and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-
CC E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-
CC 4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-
CC 11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-
CC 4/beta-1 recognizes one or more domains within the alternatively
CC spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1
CC is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1,
CC alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin
CC alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in
CC sperm-egg fusion. Integrin alpha-4/beta-1 is a receptor for VCAM1 and
CC recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a
CC receptor for VCAM1, cytotactin and osteopontin. It recognizes the
CC sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a
CC receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-
CC 3/beta-1 provides a docking site for FAP (seprase) at invadopodia
CC plasma membranes in a collagen-dependent manner and hence may
CC participate in the adhesion, formation of invadopodia and matrix
CC degradation processes, promoting cell invasion. Alpha-3/beta-1 may
CC mediate with LGALS3 the stimulation by CSPG4 of endothelial cells
CC migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-
CC 1 integrins recognize the sequence R-G-D in a wide array of ligands.
CC When associated with alpha-7/beta-1 integrin, regulates cell adhesion
CC and laminin matrix deposition. Involved in promoting endothelial cell
CC motility and angiogenesis. Involved in osteoblast compaction through
CC the fibronectin fibrillogenesis cell-mediated matrix assembly process
CC and the formation of mineralized bone nodules. May be involved in up-
CC regulation of the activity of kinases such as PKC via binding to KRT1.
CC Together with KRT1 and RACK1, serves as a platform for SRC activation
CC or inactivation. Plays a mechanistic adhesive role during telophase,
CC required for the successful completion of cytokinesis (By similarity).
CC ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor
CC in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1
CC bind to PLA2G2A via a site (site 2) which is distinct from the
CC classical ligand-binding site (site 1) and this induces integrin
CC conformational changes and enhanced ligand binding to site 1.
CC ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-
CC D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B
CC and binding is essential for IL1B signaling (By similarity).
CC ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for
CC CD40/CD40LG signaling (By similarity). Plays an important role in
CC myoblast differentiation and fusion during skeletal myogenesis (By
CC similarity). {ECO:0000250|UniProtKB:P05556,
CC ECO:0000250|UniProtKB:P07228, ECO:0000250|UniProtKB:P09055}.
CC -!- SUBUNIT: Interacts with seprase FAP (seprase); the interaction occurs
CC at the cell surface of invadopodia membrane in a collagen-dependent
CC manner (By similarity). Heterodimer of an alpha and a beta subunit.
CC Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4,
CC alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or
CC alpha-V. ITGA6:ITGB1 is found in a complex with CD9; interaction takes
CC place in oocytes and is involved in sperm-egg fusion. Binds LGALS3BP
CC and NMRK2, when associated with alpha-7, but not with alpha-5.
CC Interacts with FLNA, FLNB, FLNC and RANBP9. Interacts with KRT1 in the
CC presence of RACK1 and SRC. Interacts with JAML; integrin alpha-4/beta-1
CC may regulate leukocyte to endothelial cells adhesion by controlling
CC JAML homodimerization. Interacts with RAB21. Interacts (via the
CC cytoplasmic region) with RAB25 (via the hypervariable C-terminal
CC region). Interacts with MYO10. Interacts with ITGB1BP1 (via C-terminal
CC region); the interaction is a prerequisite for focal adhesion
CC disassembly. Interacts with TLN1; the interaction is prevented by
CC competitive binding of ITGB1BP1. Interacts with ACAP1; required for
CC ITGB1 recycling. Interacts with ASAP3. Interacts with FERMT2; the
CC interaction is inhibited in presence of ITGB1BP1. Interacts with DAB2.
CC Interacts with FGR and HCK. Isoform 2 interacts with alpha-7A and
CC alpha-7B in adult skeletal muscle. Isoform 2 interacts with alpha-7B in
CC cardiomyocytes of adult heart. Interacts with EMP2; the interaction may
CC be direct or indirect and ITGB1 has a heterodimer form (By similarity).
CC ITGA5:ITGB1 interacts with CCN3 (By similarity). ITGA4:ITGB1 is found
CC in a ternary complex with CX3CR1 and CX3CL1 (By similarity).
CC ITGA5:ITGB1 interacts with FBN1 (By similarity). ITGA5:ITGB1 interacts
CC with IL1B. Interacts with MDK. ITGA4:ITGB1 interacts with MDK; this
CC interaction mediates MDK-induced osteoblast cells migration through PXN
CC phosphorylation. ITGA6:ITGB1 interacts with MDK; this interaction
CC mediates MDK-induced neurite-outgrowth (By similarity). ITGA5:ITGB1
CC interacts with ACE2 (By similarity). Interacts with TMEM182 and LAMB1
CC (By similarity). {ECO:0000250|UniProtKB:P05556,
CC ECO:0000250|UniProtKB:P07228, ECO:0000250|UniProtKB:P09055}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type
CC I membrane protein {ECO:0000255}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein
CC {ECO:0000255}. Recycling endosome {ECO:0000250|UniProtKB:P05556}.
CC Melanosome {ECO:0000250|UniProtKB:P05556}. Cell projection,
CC lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P05556}. Cell surface
CC {ECO:0000250|UniProtKB:P05556}. Note=Enriched preferentially at
CC invadopodia, cell membrane protrusions that correspond to sites of cell
CC invasion, in a collagen-dependent manner. Localized at plasma and
CC ruffle membranes in a collagen-independent manner. Colocalizes with
CC ITGB1BP1 and metastatic suppressor protein NME2 at the edge or
CC peripheral ruffles and lamellipodia during the early stages of cell
CC spreading on fibronectin or collagen. Translocates from peripheral
CC focal adhesions to fibrillar adhesions in an ITGB1BP1-dependent manner.
CC {ECO:0000250|UniProtKB:P05556}.
CC -!- PTM: The cysteine residues are involved in intrachain disulfide bonds.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI31846.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U12309; AAA86669.1; -; mRNA.
DR EMBL; BC131845; AAI31846.1; ALT_FRAME; mRNA.
DR PIR; JC4126; JC4126.
DR RefSeq; NP_058718.2; NM_017022.2.
DR AlphaFoldDB; P49134; -.
DR SMR; P49134; -.
DR BioGRID; 246668; 9.
DR CORUM; P49134; -.
DR IntAct; P49134; 4.
DR MINT; P49134; -.
DR STRING; 10116.ENSRNOP00000014785; -.
DR GlyGen; P49134; 12 sites.
DR iPTMnet; P49134; -.
DR PhosphoSitePlus; P49134; -.
DR jPOST; P49134; -.
DR PaxDb; P49134; -.
DR PRIDE; P49134; -.
DR GeneID; 24511; -.
DR KEGG; rno:24511; -.
DR UCSC; RGD:2927; rat.
DR CTD; 3688; -.
DR RGD; 2927; Itgb1.
DR eggNOG; KOG1226; Eukaryota.
DR InParanoid; P49134; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P49134; -.
DR TreeFam; TF105392; -.
DR Reactome; R-RNO-1566948; Elastic fibre formation.
DR Reactome; R-RNO-1566977; Fibronectin matrix formation.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-210991; Basigin interactions.
DR Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-RNO-3000157; Laminin interactions.
DR Reactome; R-RNO-3000170; Syndecan interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-445144; Signal transduction by L1.
DR Reactome; R-RNO-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8875513; MET interacts with TNS proteins.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9634597; GPER1 signaling.
DR PRO; PR:P49134; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0005912; C:adherens junction; IDA:RGD.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:SynGO.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; IDA:RGD.
DR GO; GO:0097386; C:glial cell projection; IDA:ARUK-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030056; C:hemidesmosome; IDA:RGD.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099699; C:integral component of synaptic membrane; ISO:RGD.
DR GO; GO:0034665; C:integrin alpha1-beta1 complex; ISO:RGD.
DR GO; GO:0034680; C:integrin alpha10-beta1 complex; ISO:RGD.
DR GO; GO:0034681; C:integrin alpha11-beta1 complex; ISO:RGD.
DR GO; GO:0034666; C:integrin alpha2-beta1 complex; ISO:RGD.
DR GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:RGD.
DR GO; GO:0034674; C:integrin alpha5-beta1 complex; ISO:RGD.
DR GO; GO:0034677; C:integrin alpha7-beta1 complex; ISO:RGD.
DR GO; GO:0034679; C:integrin alpha9-beta1 complex; IDA:RGD.
DR GO; GO:0008305; C:integrin complex; IDA:RGD.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0035748; C:myelin sheath abaxonal region; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0051393; F:alpha-actinin binding; IDA:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; IDA:RGD.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; ISO:RGD.
DR GO; GO:0001968; F:fibronectin binding; IDA:RGD.
DR GO; GO:0005178; F:integrin binding; IMP:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0043236; F:laminin binding; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0048675; P:axon extension; ISO:RGD.
DR GO; GO:0071711; P:basement membrane organization; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:RGD.
DR GO; GO:0007161; P:calcium-independent cell-matrix adhesion; ISO:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0023035; P:CD40 signaling pathway; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IGI:ARUK-UCL.
DR GO; GO:0001708; P:cell fate specification; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0030030; P:cell projection organization; IMP:ARUK-UCL.
DR GO; GO:0033631; P:cell-cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0031589; P:cell-substrate adhesion; ISO:RGD.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEP:RGD.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:RGD.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; IEP:RGD.
DR GO; GO:0021943; P:formation of radial glial scaffolds; ISO:RGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0008354; P:germ cell migration; ISO:RGD.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:SynGO.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:ARUK-UCL.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0048333; P:mesodermal cell differentiation; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0031345; P:negative regulation of cell projection organization; IMP:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0006909; P:phagocytosis; IMP:ARUK-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:RGD.
DR GO; GO:0051951; P:positive regulation of glutamate uptake involved in transmission of nerve impulse; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; ISO:RGD.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:RGD.
DR GO; GO:0032594; P:protein transport within lipid bilayer; IMP:RGD.
DR GO; GO:0150103; P:reactive gliosis; ISO:RGD.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0010710; P:regulation of collagen catabolic process; ISS:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:1901979; P:regulation of inward rectifier potassium channel activity; ISO:RGD.
DR GO; GO:0150003; P:regulation of spontaneous synaptic transmission; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0071559; P:response to transforming growth factor beta; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR GO; GO:0099561; P:synaptic membrane adhesion to extracellular matrix; IC:UniProtKB.
DR GO; GO:0001894; P:tissue homeostasis; IMP:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR027071; Integrin_beta-1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF28; PTHR10082:SF28; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Disulfide bond; Endosome; Glycoprotein; Integrin; Isopeptide bond;
KW Magnesium; Membrane; Metal-binding; Myogenesis; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..798
FT /note="Integrin beta-1"
FT /id="PRO_0000016336"
FT TOPO_DOM 21..729
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 730..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 753..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 140..378
FT /note="VWFA"
FT REPEAT 467..516
FT /note="I"
FT REPEAT 517..560
FT /note="II"
FT REPEAT 561..599
FT /note="III"
FT REPEAT 600..636
FT /note="IV"
FT REGION 207..213
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT REGION 295..314
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT REGION 383..466
FT /note="Interaction with TMEM182"
FT /evidence="ECO:0000250|UniProtKB:P07228"
FT REGION 467..636
FT /note="Cysteine-rich tandem repeats"
FT REGION 763..768
FT /note="Signal for sorting from recycling endosomes;
FT interaction with ACAP1"
FT /evidence="ECO:0000250"
FT REGION 786..793
FT /note="Interaction with ITGB1BP1"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 778
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 784
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 790
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 795
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..45
FT /evidence="ECO:0000250"
FT DISULFID 35..465
FT /evidence="ECO:0000250"
FT DISULFID 38..75
FT /evidence="ECO:0000250"
FT DISULFID 48..64
FT /evidence="ECO:0000250"
FT DISULFID 207..213
FT /evidence="ECO:0000250"
FT DISULFID 261..301
FT /evidence="ECO:0000250"
FT DISULFID 401..415
FT /evidence="ECO:0000250"
FT DISULFID 435..463
FT /evidence="ECO:0000250"
FT DISULFID 467..692
FT /evidence="ECO:0000250"
FT DISULFID 478..490
FT /evidence="ECO:0000250"
FT DISULFID 487..526
FT /evidence="ECO:0000250"
FT DISULFID 492..501
FT /evidence="ECO:0000250"
FT DISULFID 503..517
FT /evidence="ECO:0000250"
FT DISULFID 532..537
FT /evidence="ECO:0000250"
FT DISULFID 534..569
FT /evidence="ECO:0000250"
FT DISULFID 539..554
FT /evidence="ECO:0000250"
FT DISULFID 556..561
FT /evidence="ECO:0000250"
FT DISULFID 575..580
FT /evidence="ECO:0000250"
FT DISULFID 577..608
FT /evidence="ECO:0000250"
FT DISULFID 582..591
FT /evidence="ECO:0000250"
FT DISULFID 593..600
FT /evidence="ECO:0000250"
FT DISULFID 614..619
FT /evidence="ECO:0000250"
FT DISULFID 616..662
FT /evidence="ECO:0000250"
FT DISULFID 621..631
FT /evidence="ECO:0000250"
FT DISULFID 634..637
FT /evidence="ECO:0000250"
FT DISULFID 641..650
FT /evidence="ECO:0000250"
FT DISULFID 647..724
FT /evidence="ECO:0000250"
FT DISULFID 666..700
FT /evidence="ECO:0000250"
FT CROSSLNK 795
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT CONFLICT 76
FT /note="H -> Q (in Ref. 2; AAI31846)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="K -> N (in Ref. 2; AAI31846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 88495 MW; F4475202EB8A3EA6 CRC64;
MNLQLVFWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN TTFLQEGMPT
SARCDDLEAL KKKGCHPSDI ENPRGSQTIK KNKNVTNRSK GMAEKLRPED ITQIQPQQLL
LKLRSGEPQK FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY CKNGVNGTGE NGRKCSNISI
GDEVQFEISI TANKCPNKES ENQLKLNPLG FTEEVEVVLQ FICKCNCQSH GIPASPKCHE
GNGTFECGAC RCNEGRVGRH CECSTDEVNS EDMDAYCRKE NSSEICSNNG ECVCGQCVCR
KRENTNEIYS GKFCECDNFN CDRSNGLICG GNGVCRCRVC ECYPNYTGSA CDCSLDTVPC
VATNGQICNG RGICECGACK CTDPKFQGPT CETCQTCLGV CAEHKECVQC RAFNKGEKKD
TCAQECSHFN LTKVESREKL PQPVQVDPVT HCKEKDIDDC WFYFTYSVNS KGEAHVHVVE
TPDCPTGPDI IPIVAGVVAG IVLIGLALLL IWKLLMIIHD RREFAKFEKE KMNAKWDTGE
NPIYKSAVTT VVNPKYEGK
