ID ITB1_CHICK Reviewed; 803 AA. AC P07228; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 24-JAN-2024, entry version 173. DE RecName: Full=Integrin beta-1; DE AltName: Full=CSAT antigen; DE AltName: Full=JG22 antigen; DE AltName: Full=RGD-receptor; DE Flags: Precursor; GN Name=ITGB1; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Embryonic fibroblast; RX PubMed=3487386; DOI=10.1016/0092-8674(86)90744-0; RA Tamkun J.W., Desimone D.W., Fonda D., Patel R.S., Buck C., Horwitz A.F., RA Hynes R.O.; RT "Structure of integrin, a glycoprotein involved in the transmembrane RT linkage between fibronectin and actin."; RL Cell 46:271-282(1986). RN [2] RP FUNCTION, AND INTERACTION WITH TMEM182 AND LAMB1. RX PubMed=34427057; DOI=10.1002/jcsm.12767; RA Luo W., Lin Z., Chen J., Chen G., Zhang S., Liu M., Li H., He D., Liang S., RA Luo Q., Zhang D., Nie Q., Zhang X.; RT "TMEM182 interacts with integrin beta 1 and regulates myoblast RT differentiation and muscle regeneration."; RL J. Cachexia Sarcopenia Muscle 12:1704-1723(2021). 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-1 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 (By similarity). Integrin alpha-4/beta-1 is a receptor CC for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha- CC 9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It CC recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha- CC 3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. CC Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at CC invadopodia plasma membranes in a collagen-dependent manner and hence CC may 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. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act CC as its coreceptor in CX3CR1-dependent fractalkine signaling. CC ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which CC is distinct from the classical ligand-binding site (site 1) and this CC induces integrin conformational changes and enhanced ligand binding to CC site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and CC mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 acts as a CC receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion CC to FN1 (By similarity). ITGA5:ITGB1 is a receptor for IL1B and binding CC is essential for IL1B signaling. ITGA5:ITGB3 is a receptor for soluble CC CD40LG and is required for CD40/CD40LG signaling (By similarity). Plays CC an important role in myoblast differentiation and fusion during CC skeletal myogenesis (PubMed:34427057). {ECO:0000250|UniProtKB:P05556, CC ECO:0000250|UniProtKB:P09055}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-1 associates CC with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-5, alpha-6, CC alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or alpha-V (By CC similarity). Interacts with TMEM182 and LAMB1 (PubMed:34427057). CC {ECO:0000250|UniProtKB:P05556, ECO:0000269|PubMed:34427057}. CC -!- INTERACTION: CC P07228; P05094: ACTN1; NbExp=4; IntAct=EBI-5606437, EBI-5847257; CC P07228; P21333: FLNA; Xeno; NbExp=2; IntAct=EBI-5606437, EBI-350432; 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}. Melanosome {ECO:0000250|UniProtKB:P05556}. Cell CC projection, lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell CC projection, ruffle {ECO:0000250|UniProtKB:P05556}. Cell junction, focal CC adhesion {ECO:0000250|UniProtKB:P05556}. CC -!- TISSUE SPECIFICITY: Expressed on surface of embryonic fibroblasts (at CC protein level). {ECO:0000269|PubMed:3487386}. CC -!- DOMAIN: The VWFA domain (or beta I domain) contains three cation- CC binding sites: the ligand-associated metal ion-binding site (LIMBS or CC SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent CC MIDAS site (ADMIDAS). This domain is also part of the ligand-binding CC site. {ECO:0000250|UniProtKB:P05556}. CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M14049; AAA48926.1; -; mRNA. DR PIR; A23947; IJCH3. DR AlphaFoldDB; P07228; -. DR BMRB; P07228; -. DR SMR; P07228; -. DR IntAct; P07228; 4. DR MINT; P07228; -. DR STRING; 9031.ENSGALP00000054354; -. DR GlyCosmos; P07228; 12 sites, No reported glycans. DR iPTMnet; P07228; -. DR PaxDb; 9031-ENSGALP00000011559; -. DR VEuPathDB; HostDB:geneid_374058; -. DR eggNOG; KOG1226; Eukaryota. DR InParanoid; P07228; -. DR PhylomeDB; P07228; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:AgBase. DR GO; GO:0008305; C:integrin complex; IBA:GO_Central. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IBA:GO_Central. DR GO; GO:0001968; F:fibronectin binding; IBA:GO_Central. DR GO; GO:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:AgBase. DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW. DR GO; GO:0045445; P:myoblast differentiation; IMP:UniProtKB. DR GO; GO:0007520; P:myoblast fusion; IMP:UniProtKB. DR Gene3D; 4.10.1240.30; -; 1. DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1. DR Gene3D; 2.10.25.10; Laminin; 4. DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1. DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR040622; I-EGF_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; INTEGRIN BETA SUBUNIT; 1. DR PANTHER; PTHR10082:SF28; INTEGRIN BETA-1; 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; SSF57196; EGF/Laminin; 2. DR SUPFAM; SSF69687; Integrin beta tail domain; 1. DR SUPFAM; SSF69179; Integrin domains; 1. DR SUPFAM; SSF103575; Plexin repeat; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS00243; INTEGRIN_BETA; 3. PE 1: Evidence at protein level; KW Calcium; Cell adhesion; Cell junction; Cell membrane; Cell projection; KW Disulfide bond; EGF-like domain; Glycoprotein; Integrin; Magnesium; KW Membrane; Metal-binding; Myogenesis; Phosphoprotein; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..24 FT /evidence="ECO:0000250" FT CHAIN 25..803 FT /note="Integrin beta-1" FT /id="PRO_0000016337" FT TOPO_DOM 25..733 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 734..756 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 757..803 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 30..80 FT /note="PSI" FT /evidence="ECO:0000255" FT DOMAIN 144..382 FT /note="VWFA" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 444..506 FT /note="EGF-like 1" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 507..559 FT /note="EGF-like 2" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 560..596 FT /note="EGF-like 3" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 597..640 FT /note="EGF-like 4" FT /evidence="ECO:0000250|UniProtKB:P05106" FT REGION 211..217 FT /note="CX3CL1-binding" FT /evidence="ECO:0000250|UniProtKB:P05556" FT REGION 299..318 FT /note="CX3CL1-binding" FT /evidence="ECO:0000250|UniProtKB:P05556" FT REGION 387..470 FT /note="Interaction with TMEM182" FT /evidence="ECO:0000269|PubMed:34427057" FT BINDING 156 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="in MIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 158 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="in ADMIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 158 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="in MIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 161 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="in ADMIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 162 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="in ADMIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 193 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 248 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 250 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 252 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 253 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT BINDING 253 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="in MIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05556" FT MOD_RES 25 FT /note="Blocked amino end (Gln)" FT MOD_RES 788 FT /note="Phosphotyrosine; by Tyr-kinases" FT /evidence="ECO:0000255" FT CARBOHYD 216 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 273 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 367 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 410 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 421 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 433 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 445 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 486 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 525 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 589 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 624 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 674 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 31..49 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 39..469 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 42..68 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 52..79 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 211..217 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 265..305 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 405..419 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 439..467 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 471..491 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 482..494 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 496..505 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 507..538 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 521..536 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 530..541 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 543..558 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 560..581 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 565..579 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 573..584 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 586..595 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 597..620 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 604..618 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 612..623 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 625..635 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 638..641 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 645..696 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 651..670 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 654..666 FT /evidence="ECO:0000250|UniProtKB:P05556" FT DISULFID 704..728 FT /evidence="ECO:0000250|UniProtKB:P05556" SQ SEQUENCE 803 AA; 88554 MW; 2F6FEFCDF2C80457 CRC64; MAETNLTLLT WAGILCCLIW SGSAQQGGSD CIKANAKSCG ECIQAGPNCG WCKKTDFLQE GEPTSARCDD LAALKSKGCP EQDIENPRGS KRVLEDREVT NRKIGAAEKL KPEAITQIQP QKLVLQLRVG EPQTFSLKFK RAEDYPIDLY YLMDLSYSMK DDLENVKSLG TALMREMEKI TSDFRIGFGS FVEKTVMPYI STTPAKLRNP CTGDQNCTSP FSYKNVLSLT SEGNKFNELV GKQHISGNLD SPEGGFDAIM QVAVCGDQIG WRNVTRLLVF STDAGFHFAG DGKLGGIVLP NDGKCHLENN MYTMSHYYDY PSIAHLVQKL SENNIQTIFA VTEEFQAVYK ELKNLIPKSA VGTLSSNSSN VIQLIIDAYN SLSSEVILEN SKLPKEVTIS YKSYCKNGVN DTQEDGRKCS NISIGDEVRF EINVTANECP KKGQNETIKI KPLGFTEEVE IHLQFICDCL CQSEGEPNSP ACHDGNGTFE CGACRCNEGR IGRLCECSTD EVNSEDMDAY CRRENSTEIC SNNGECICGQ CVCKKRENTN EVYSGKYCEC DNFNCDRSNG LICGGNGICK CRVCECFPNF TGSACDCSLD TTPCMAGNGQ ICNGRGTCEC GTCNCTDPKF QGPTCEMCQT CLGVCAEHKD CVQCRAFEKG EKKETCSQEC MHFNMTRVES RGKLPQPVHP DPLSHCKEKD VGDCWFYFTY SVNSNGEASV HVVETPECPS GPDIIPIVAG VVAGIVLIGL ALLLIWKLLM IIHDRREFAK FEKEKMNAKW DTGENPIYKS AVTTVVNPKY EGK //