ITB6_BOVIN
ID ITB6_BOVIN Reviewed; 788 AA.
AC Q8SQB8; Q0PE61;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Integrin beta-6;
DE Flags: Precursor;
GN Name=ITGB6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION AS A FMDV RECEPTOR.
RX PubMed=12551988; DOI=10.1128/jvi.77.4.2500-2511.2003;
RA Duque H., Baxt B.;
RT "Foot-and-mouth disease virus receptors: comparison of bovine alpha(V)
RT integrin utilization by type A and O viruses.";
RL J. Virol. 77:2500-2511(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tongue;
RA Du J.-Z., Chang H.-Y., Cong G., Shao J.-J., Lin T., Cai X., Xie Q.;
RT "Molecular cloning and characterization of cDNA encoding bovine beta6
RT subunit.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Integrin alpha-V:beta-6 (ITGAV:ITGB6) is a receptor for
CC fibronectin and cytotactin (By similarity). It recognizes the sequence
CC R-G-D in its ligands (By similarity). ITGAV:ITGB6 acts as a receptor
CC for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to
CC FBN1 (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-
CC G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1)
CC from regulatory Latency-associated peptide (LAP), thereby playing a key
CC role in TGF-beta-1 activation (By similarity).
CC {ECO:0000250|UniProtKB:P18564, ECO:0000250|UniProtKB:Q9Z0T9}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By similarity).
CC Interacts with FLNB. Interacts with HAX1. ITGAV:ITGB6 interacts with
CC FBN1 (By similarity). ITGAV:ITGB6 interacts with TGFB1 (By similarity).
CC {ECO:0000250|UniProtKB:P18564, ECO:0000250|UniProtKB:Q9Z0T9}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P18564}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; AF468060; AAL78039.1; -; mRNA.
DR EMBL; DQ867017; ABH04286.1; -; mRNA.
DR RefSeq; NP_777123.1; NM_174698.2.
DR RefSeq; XP_005202466.1; XM_005202409.3.
DR AlphaFoldDB; Q8SQB8; -.
DR SMR; Q8SQB8; -.
DR STRING; 9913.ENSBTAP00000011972; -.
DR PaxDb; Q8SQB8; -.
DR PRIDE; Q8SQB8; -.
DR Ensembl; ENSBTAT00000079094; ENSBTAP00000064115; ENSBTAG00000009080.
DR GeneID; 282644; -.
DR KEGG; bta:282644; -.
DR CTD; 3694; -.
DR VEuPathDB; HostDB:ENSBTAG00000009080; -.
DR VGNC; VGNC:30331; ITGB6.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_011772_0_1_1; -.
DR InParanoid; Q8SQB8; -.
DR OMA; LSGPHCA; -.
DR OrthoDB; 473040at2759; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000009080; Expressed in gluteus medius and 70 other tissues.
DR ExpressionAtlas; Q8SQB8; baseline.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0034685; C:integrin alphav-beta6 complex; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
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:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015436; Integrin_bsu-6.
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:SF11; PTHR10082:SF11; 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; 2.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Integrin;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..788
FT /note="Integrin beta-6"
FT /id="PRO_0000244819"
FT TOPO_DOM 22..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 131..371
FT /note="VWFA"
FT REPEAT 456..501
FT /note="I"
FT REPEAT 502..543
FT /note="II"
FT REPEAT 544..582
FT /note="III"
FT REPEAT 583..619
FT /note="IV"
FT REGION 456..619
FT /note="Cysteine-rich tandem repeats"
FT REGION 731..758
FT /note="Interaction with HAX1"
FT /evidence="ECO:0000250"
FT CARBOHYD 48
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 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..454
FT /evidence="ECO:0000250"
FT DISULFID 31..41
FT /evidence="ECO:0000250"
FT DISULFID 34..70
FT /evidence="ECO:0000250"
FT DISULFID 44..59
FT /evidence="ECO:0000250"
FT DISULFID 197..204
FT /evidence="ECO:0000250|UniProtKB:P18564"
FT DISULFID 252..293
FT /evidence="ECO:0000250|UniProtKB:P18564"
FT DISULFID 394..406
FT /evidence="ECO:0000250"
FT DISULFID 426..670
FT /evidence="ECO:0000250"
FT DISULFID 452..456
FT /evidence="ECO:0000250"
FT DISULFID 467..479
FT /evidence="ECO:0000250"
FT DISULFID 476..511
FT /evidence="ECO:0000250"
FT DISULFID 481..490
FT /evidence="ECO:0000250"
FT DISULFID 492..502
FT /evidence="ECO:0000250"
FT DISULFID 517..522
FT /evidence="ECO:0000250"
FT DISULFID 519..552
FT /evidence="ECO:0000250"
FT DISULFID 524..537
FT /evidence="ECO:0000250"
FT DISULFID 539..544
FT /evidence="ECO:0000250"
FT DISULFID 558..563
FT /evidence="ECO:0000250"
FT DISULFID 560..591
FT /evidence="ECO:0000250"
FT DISULFID 565..574
FT /evidence="ECO:0000250"
FT DISULFID 576..583
FT /evidence="ECO:0000250"
FT DISULFID 597..602
FT /evidence="ECO:0000250"
FT DISULFID 599..645
FT /evidence="ECO:0000250"
FT DISULFID 604..614
FT /evidence="ECO:0000250"
FT DISULFID 617..620
FT /evidence="ECO:0000250"
FT DISULFID 624..633
FT /evidence="ECO:0000250"
FT DISULFID 630..702
FT /evidence="ECO:0000250"
FT DISULFID 649..678
FT /evidence="ECO:0000250"
FT CONFLICT 780
FT /note="Q -> R (in Ref. 2; ABH04286)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="L -> F (in Ref. 2; ABH04286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 788 AA; 85893 MW; FB9B5197BFF56EEB CRC64;
MGIELLCLFF LCLGRNDHVQ GGCAVGGAET CEDCLLIGPQ CAWCSQENFT HLSGVGERCD
TPANLLAKGC QLTFIENPVS QVEILTNKPL SIGRQKNSSD IVQISPQSLA LKLRPGLEQT
LQVQVRQTED YPVDLYYLMD LSASMDDDLN TIKELGSLLS KEMSKLTSNF RLGFGSFVEK
PISPFMKTTP EEIANPCSSI PYFCLPTFGF KHILPLTNDA ERFNEIVKNQ KISANIDTPE
GGFDAIMQAA VCKEKIGWRN DSLHLLVFVS DADSHFGMDS KLAGIVIPND GLCHLDSKNE
YSMSTILEYP TIGQLIDKLV QNNVLLIFAV TQEQVHLYEN YAKLIPGATV GVLQKDSGNI
LQLIISAYEE LRSEVELEVL GDTEGLNLSF TAICNTGIPV PHQKKCSHMK VGDTASFNVT
VSLPNCERRS RHIILKPVGL GDALEILVSP ECSCDCQKEV EVNSSKCNNG NGSFQCGVCA
CHPGHMGHHC ECGEDTLSTE SCKEAPGRPS CSGRGDCYCG QCVCHLSPYG NIYGPYCQCD
NFSCVRHKGL LCGDNGDCDC GECVCRSGWT GEYCNCTTST DPCVSEDGIL CSGRGDCVCG
KCICTNPGAS GPTCERCPTC GDPCNSKRSC IECYLSADGQ AQEECVDKCK LAGATINEEE
DFSKDSFVSC SLQGENECLI TFLLTTDNEG KTVIHSINEK DCPKPPNIPM IMLGVSLAIL
LIGVVLLCIW KLLVSFHDRK EVAKFEAERS KAKWQTGTNP LYRGSTSTFK NVTYKHKEKQ
KVDLSTDG
