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Database: UniProt
Entry: P07228
LinkDB: P07228
Original site: P07228 
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   13-FEB-2019, entry version 154.
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;
OC   Phasianidae; 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.,
RA   Horwitz A.F., 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).
CC   -!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-
CC       1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-
CC       1/beta-1 and alpha-2/beta-1 recognize the proline-hydroxylated
CC       sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-
CC       3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-
CC       10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for
CC       fibronectin. Alpha-4/beta-1 recognizes one or more domains within
CC       the alternatively spliced CS-1 and CS-5 regions of fibronectin.
CC       Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin
CC       alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1
CC       are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1)
CC       is present in oocytes and is involved in sperm-egg fusion (By
CC       similarity). 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
CC       is a receptor for VCAM1, cytotactin and osteopontin. It recognizes
CC       the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-
CC       1 is a receptor for epiligrin, thrombospondin and CSPG4. Integrin
CC       alpha-3/beta-1 provides a docking site for FAP (seprase) at
CC       invadopodia plasma membranes in a collagen-dependent manner and
CC       hence may participate in the adhesion, formation of invadopodia
CC       and matrix degradation processes, promoting cell invasion. Alpha-
CC       3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of
CC       endothelial cells migration. Integrin alpha-V/beta-1 is a receptor
CC       for vitronectin. Beta-1 integrins recognize the sequence R-G-D in
CC       a wide array of ligands. When associated with alpha-7/beta-1
CC       integrin, regulates cell adhesion and laminin matrix deposition.
CC       Involved in promoting endothelial cell motility and angiogenesis.
CC       Involved in osteoblast compaction through the fibronectin
CC       fibrillogenesis cell-mediated matrix assembly process and the
CC       formation of mineralized bone nodules. May be involved in up-
CC       regulation of the activity of kinases such as PKC via binding to
CC       KRT1. Together with KRT1 and RACK1, serves as a platform for SRC
CC       activation or inactivation. ITGA4:ITGB1 binds to fractalkine
CC       (CX3CL1) and may act as its coreceptor in CX3CR1-dependent
CC       fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A
CC       via a site (site 2) which is distinct from the classical ligand-
CC       binding site (site 1) and this induces integrin conformational
CC       changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as
CC       a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent
CC       cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and
CC       binding is essential for IL1B signaling.
CC       {ECO:0000250|UniProtKB:P05556, ECO:0000250|UniProtKB:P09055}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-1
CC       associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-
CC       5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or
CC       alpha-V (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P05094:ACTN1; NbExp=4; IntAct=EBI-5606437, EBI-5847257;
CC       P21333:FLNA (xeno); NbExp=2; IntAct=EBI-5606437, EBI-350432;
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Cell projection, invadopodium membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Cell projection, ruffle membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P05556}.
CC       Cell projection, lamellipodium {ECO:0000250|UniProtKB:P05556}.
CC       Cell projection, ruffle {ECO:0000250|UniProtKB:P05556}. Cell
CC       junction, focal adhesion {ECO:0000250|UniProtKB:P05556}. Cell
CC       surface {ECO:0000250|UniProtKB:P05556}.
CC   -!- TISSUE SPECIFICITY: Expressed on surface of embryonic fibroblasts
CC       (at protein level). {ECO:0000269|PubMed:3487386}.
CC   -!- PTM: The cysteine residues are involved in intrachain disulfide
CC       bonds.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; M14049; AAA48926.1; -; mRNA.
DR   PIR; A23947; IJCH3.
DR   UniGene; Gga.111; -.
DR   ProteinModelPortal; P07228; -.
DR   SMR; P07228; -.
DR   IntAct; P07228; 3.
DR   MINT; P07228; -.
DR   STRING; 9031.ENSGALP00000011559; -.
DR   iPTMnet; P07228; -.
DR   PaxDb; P07228; -.
DR   PRIDE; P07228; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P07228; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P07228; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005623; C:cell; IDA:AgBase.
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:0071438; C:invadopodium membrane; ISS:UniProtKB.
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   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   Complete proteome; Disulfide bond; Glycoprotein; Integrin; Magnesium;
KW   Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       {ECO:0000250}.
FT   CHAIN        25    803       Integrin beta-1.
FT                                /FTId=PRO_0000016337.
FT   TOPO_DOM     25    733       Extracellular. {ECO:0000255}.
FT   TRANSMEM    734    756       Helical. {ECO:0000255}.
FT   TOPO_DOM    757    803       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      144    382       VWFA.
FT   REPEAT      471    520       I.
FT   REPEAT      521    564       II.
FT   REPEAT      565    603       III.
FT   REPEAT      604    640       IV.
FT   REGION      211    217       CX3CL1-binding.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   REGION      299    318       CX3CL1-binding.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   REGION      471    640       Cysteine-rich tandem repeats.
FT   METAL       156    156       Magnesium. {ECO:0000250}.
FT   METAL       158    158       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       160    160       Calcium 1. {ECO:0000250}.
FT   METAL       161    161       Calcium 1. {ECO:0000250}.
FT   METAL       193    193       Calcium 2. {ECO:0000250}.
FT   METAL       248    248       Calcium 2. {ECO:0000250}.
FT   METAL       250    250       Calcium 2. {ECO:0000250}.
FT   METAL       252    252       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       253    253       Calcium 2. {ECO:0000250}.
FT   METAL       253    253       Magnesium. {ECO:0000250}.
FT   MOD_RES      25     25       Blocked amino end (Gln).
FT   MOD_RES     788    788       Phosphotyrosine; by Tyr-kinases.
FT                                {ECO:0000255}.
FT   CARBOHYD    216    216       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    273    273       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    367    367       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    410    410       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    421    421       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    433    433       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    445    445       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    486    486       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    525    525       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    589    589       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    624    624       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    674    674       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     31     49       {ECO:0000250}.
FT   DISULFID     39    469       {ECO:0000250}.
FT   DISULFID     42     79       {ECO:0000250}.
FT   DISULFID     52     68       {ECO:0000250}.
FT   DISULFID    211    217       {ECO:0000250}.
FT   DISULFID    265    305       {ECO:0000250}.
FT   DISULFID    405    419       {ECO:0000250}.
FT   DISULFID    439    467       {ECO:0000250}.
FT   DISULFID    471    696       {ECO:0000250}.
FT   DISULFID    482    494       {ECO:0000250}.
FT   DISULFID    491    530       {ECO:0000250}.
FT   DISULFID    496    505       {ECO:0000250}.
FT   DISULFID    507    521       {ECO:0000250}.
FT   DISULFID    536    541       {ECO:0000250}.
FT   DISULFID    538    573       {ECO:0000250}.
FT   DISULFID    543    558       {ECO:0000250}.
FT   DISULFID    560    565       {ECO:0000250}.
FT   DISULFID    579    584       {ECO:0000250}.
FT   DISULFID    581    612       {ECO:0000250}.
FT   DISULFID    586    595       {ECO:0000250}.
FT   DISULFID    597    604       {ECO:0000250}.
FT   DISULFID    618    623       {ECO:0000250}.
FT   DISULFID    620    666       {ECO:0000250}.
FT   DISULFID    625    635       {ECO:0000250}.
FT   DISULFID    638    641       {ECO:0000250}.
FT   DISULFID    645    654       {ECO:0000250}.
FT   DISULFID    651    728       {ECO:0000250}.
FT   DISULFID    670    704       {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
//
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