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Database: UniProt
Entry: Q8SQB8
LinkDB: Q8SQB8
Original site: Q8SQB8 
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   10-APR-2019, entry version 115.
DE   RecName: Full=Integrin beta-6;
DE   Flags: Precursor;
GN   Name=ITGB6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
CC       sequence R-G-D in its ligands (By similarity). ITGAV:ITGB6 acts as
CC       a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent
CC       cell adhesion to FBN1 (By similarity). Integrin alpha-V:beta-6
CC       (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming
CC       growth factor beta-1 (TGF-beta-1) from regulatory Latency-
CC       associated peptide (LAP), thereby playing a key role in TGF-beta-1
CC       activation (By similarity). {ECO:0000250|UniProtKB:P18564,
CC       ECO:0000250|UniProtKB:Q9Z0T9}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By
CC       similarity). Interacts with FLNB. Interacts with HAX1. ITGAV:ITGB6
CC       interacts with FBN1 (By similarity). ITGAV:ITGB6 interacts with
CC       TGFB1 (By similarity). {ECO:0000250|UniProtKB:P18564,
CC       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.
CC       {ECO:0000305}.
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   UniGene; Bt.9972; -.
DR   ProteinModelPortal; 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   VGNC; VGNC:30331; ITGB6.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; Q8SQB8; -.
DR   KO; K06589; -.
DR   OMA; VSIPNCE; -.
DR   OrthoDB; 473040at2759; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-BTA-1566948; Elastic fibre formation.
DR   Reactome; R-BTA-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-BTA-216083; Integrin cell surface interactions.
DR   Reactome; R-BTA-3000178; ECM proteoglycans.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000009080; Expressed in 6 organ(s), highest expression level in skeletal muscle tissue.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR   GO; GO:0034685; C:integrin alphav-beta6 complex; ISS:UniProtKB.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0006954; P:inflammatory response; IEA:Ensembl.
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   GO; GO:0038044; P:transforming growth factor-beta secretion; IEA:Ensembl.
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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Host cell receptor for virus entry;
KW   Host-virus interaction; Integrin; Membrane; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    788       Integrin beta-6.
FT                                /FTId=PRO_0000244819.
FT   TOPO_DOM     22    709       Extracellular. {ECO:0000255}.
FT   TRANSMEM    710    730       Helical. {ECO:0000255}.
FT   TOPO_DOM    731    788       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      131    371       VWFA.
FT   REPEAT      456    501       I.
FT   REPEAT      502    543       II.
FT   REPEAT      544    582       III.
FT   REPEAT      583    619       IV.
FT   REGION      456    619       Cysteine-rich tandem repeats.
FT   REGION      731    758       Interaction with HAX1. {ECO:0000250}.
FT   CARBOHYD     48     48       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     97     97       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    260    260       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    387    387       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    418    418       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    463    463       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    471    471       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    541    541       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    575    575       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     23    454       {ECO:0000250}.
FT   DISULFID     31     41       {ECO:0000250}.
FT   DISULFID     34     70       {ECO:0000250}.
FT   DISULFID     44     59       {ECO:0000250}.
FT   DISULFID    197    204       {ECO:0000250|UniProtKB:P18564}.
FT   DISULFID    252    293       {ECO:0000250|UniProtKB:P18564}.
FT   DISULFID    394    406       {ECO:0000250}.
FT   DISULFID    426    670       {ECO:0000250}.
FT   DISULFID    452    456       {ECO:0000250}.
FT   DISULFID    467    479       {ECO:0000250}.
FT   DISULFID    476    511       {ECO:0000250}.
FT   DISULFID    481    490       {ECO:0000250}.
FT   DISULFID    492    502       {ECO:0000250}.
FT   DISULFID    517    522       {ECO:0000250}.
FT   DISULFID    519    552       {ECO:0000250}.
FT   DISULFID    524    537       {ECO:0000250}.
FT   DISULFID    539    544       {ECO:0000250}.
FT   DISULFID    558    563       {ECO:0000250}.
FT   DISULFID    560    591       {ECO:0000250}.
FT   DISULFID    565    574       {ECO:0000250}.
FT   DISULFID    576    583       {ECO:0000250}.
FT   DISULFID    597    602       {ECO:0000250}.
FT   DISULFID    599    645       {ECO:0000250}.
FT   DISULFID    604    614       {ECO:0000250}.
FT   DISULFID    617    620       {ECO:0000250}.
FT   DISULFID    624    633       {ECO:0000250}.
FT   DISULFID    630    702       {ECO:0000250}.
FT   DISULFID    649    678       {ECO:0000250}.
FT   CONFLICT    780    780       Q -> R (in Ref. 2; ABH04286).
FT                                {ECO:0000305}.
FT   CONFLICT    784    784       L -> F (in Ref. 2; ABH04286).
FT                                {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
//
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