ITB1_CHICK
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 03-AUG-2022, entry version 166.
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 is a
CC receptor for IL1B and binding is essential for IL1B signaling.
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
CC (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}. Cell surface
CC {ECO:0000250|UniProtKB:P05556}.
CC -!- TISSUE SPECIFICITY: Expressed on surface of embryonic fibroblasts (at
CC protein level). {ECO:0000269|PubMed:3487386}.
CC -!- PTM: The cysteine residues are involved in intrachain disulfide bonds.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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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.ENSGALP00000011559; -.
DR iPTMnet; P07228; -.
DR PaxDb; P07228; -.
DR VEuPathDB; HostDB:geneid_374058; -.
DR eggNOG; KOG1226; Eukaryota.
DR InParanoid; P07228; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P07228; -.
DR Proteomes; UP000000539; Unplaced.
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; IEA:InterPro.
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:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
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; 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 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Integrin; Magnesium; Membrane; Metal-binding;
KW Myogenesis; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW 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 144..382
FT /note="VWFA"
FT REPEAT 471..520
FT /note="I"
FT REPEAT 521..564
FT /note="II"
FT REPEAT 565..603
FT /note="III"
FT REPEAT 604..640
FT /note="IV"
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 REGION 471..640
FT /note="Cysteine-rich tandem repeats"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 193
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 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
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"
FT DISULFID 39..469
FT /evidence="ECO:0000250"
FT DISULFID 42..79
FT /evidence="ECO:0000250"
FT DISULFID 52..68
FT /evidence="ECO:0000250"
FT DISULFID 211..217
FT /evidence="ECO:0000250"
FT DISULFID 265..305
FT /evidence="ECO:0000250"
FT DISULFID 405..419
FT /evidence="ECO:0000250"
FT DISULFID 439..467
FT /evidence="ECO:0000250"
FT DISULFID 471..696
FT /evidence="ECO:0000250"
FT DISULFID 482..494
FT /evidence="ECO:0000250"
FT DISULFID 491..530
FT /evidence="ECO:0000250"
FT DISULFID 496..505
FT /evidence="ECO:0000250"
FT DISULFID 507..521
FT /evidence="ECO:0000250"
FT DISULFID 536..541
FT /evidence="ECO:0000250"
FT DISULFID 538..573
FT /evidence="ECO:0000250"
FT DISULFID 543..558
FT /evidence="ECO:0000250"
FT DISULFID 560..565
FT /evidence="ECO:0000250"
FT DISULFID 579..584
FT /evidence="ECO:0000250"
FT DISULFID 581..612
FT /evidence="ECO:0000250"
FT DISULFID 586..595
FT /evidence="ECO:0000250"
FT DISULFID 597..604
FT /evidence="ECO:0000250"
FT DISULFID 618..623
FT /evidence="ECO:0000250"
FT DISULFID 620..666
FT /evidence="ECO:0000250"
FT DISULFID 625..635
FT /evidence="ECO:0000250"
FT DISULFID 638..641
FT /evidence="ECO:0000250"
FT DISULFID 645..654
FT /evidence="ECO:0000250"
FT DISULFID 651..728
FT /evidence="ECO:0000250"
FT DISULFID 670..704
FT /evidence="ECO:0000250"
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
