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Database: UniProt
Entry: Q9Z0T9
LinkDB: Q9Z0T9
Original site: Q9Z0T9 
ID   ITB6_MOUSE              Reviewed;         787 AA.
AC   Q9Z0T9; Q544J9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   10-APR-2019, entry version 159.
DE   RecName: Full=Integrin beta-6;
DE   Flags: Precursor;
GN   Name=Itgb6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=11095652;
RA   Arend L.J., Smart A.M., Briggs J.P.;
RT   "Mouse beta(6) integrin sequence, pattern of expression, and role in
RT   kidney development.";
RL   J. Am. Soc. Nephrol. 11:2297-2305(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   FUNCTION.
RX   PubMed=10025398;
RA   Munger J.S., Huang X., Kawakatsu H., Griffiths M.J., Dalton S.L.,
RA   Wu J., Pittet J.F., Kaminski N., Garat C., Matthay M.A., Rifkin D.B.,
RA   Sheppard D.;
RT   "The integrin alpha v beta 6 binds and activates latent TGF beta 1: a
RT   mechanism for regulating pulmonary inflammation and fibrosis.";
RL   Cell 96:319-328(1999).
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 (PubMed:10025398). ITGAV:ITGB6 acts
CC       as 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 (PubMed:10025398). {ECO:0000250|UniProtKB:P18564,
CC       ECO:0000269|PubMed:10025398}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit
CC       (PubMed:10025398). Interacts with FLNB (By similarity). Interacts
CC       with HAX1 (By similarity). ITGAV:ITGB6 interacts with FBN1 (By
CC       similarity). ITGAV:ITGB6 interacts with TGFB1 (PubMed:10025398).
CC       {ECO:0000250|UniProtKB:P18564, ECO:0000269|PubMed:10025398}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Cell junction, focal adhesion
CC       {ECO:0000250|UniProtKB:P18564}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; AF115376; AAD17212.1; -; mRNA.
DR   EMBL; AK036439; BAC29430.1; -; mRNA.
DR   EMBL; BC049185; AAH49185.1; -; mRNA.
DR   CCDS; CCDS16060.1; -.
DR   RefSeq; NP_001153036.1; NM_001159564.1.
DR   RefSeq; NP_067334.1; NM_021359.3.
DR   RefSeq; XP_006498871.1; XM_006498808.3.
DR   RefSeq; XP_006498872.1; XM_006498809.1.
DR   RefSeq; XP_006498873.1; XM_006498810.3.
DR   RefSeq; XP_006498874.1; XM_006498811.2.
DR   UniGene; Mm.98193; -.
DR   ProteinModelPortal; Q9Z0T9; -.
DR   SMR; Q9Z0T9; -.
DR   ComplexPortal; CPX-3132; Integrin alphav-beta6 complex.
DR   STRING; 10090.ENSMUSP00000028348; -.
DR   CarbonylDB; Q9Z0T9; -.
DR   iPTMnet; Q9Z0T9; -.
DR   PhosphoSitePlus; Q9Z0T9; -.
DR   jPOST; Q9Z0T9; -.
DR   MaxQB; Q9Z0T9; -.
DR   PaxDb; Q9Z0T9; -.
DR   PRIDE; Q9Z0T9; -.
DR   Ensembl; ENSMUST00000028348; ENSMUSP00000028348; ENSMUSG00000026971.
DR   Ensembl; ENSMUST00000059888; ENSMUSP00000054944; ENSMUSG00000026971.
DR   GeneID; 16420; -.
DR   KEGG; mmu:16420; -.
DR   UCSC; uc008juj.2; mouse.
DR   CTD; 3694; -.
DR   MGI; MGI:96615; Itgb6.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; Q9Z0T9; -.
DR   KO; K06589; -.
DR   OMA; VSIPNCE; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; Q9Z0T9; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-MMU-1566948; Elastic fibre formation.
DR   Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-MMU-216083; Integrin cell surface interactions.
DR   Reactome; R-MMU-3000178; ECM proteoglycans.
DR   PRO; PR:Q9Z0T9; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000026971; Expressed in 108 organ(s), highest expression level in metanephros.
DR   ExpressionAtlas; Q9Z0T9; baseline and differential.
DR   Genevisible; Q9Z0T9; MM.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR   GO; GO:0034685; C:integrin alphav-beta6 complex; IDA:CAFA.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0005178; F:integrin binding; IPI:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:CAFA.
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; IMP:MGI.
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; IDA:CAFA.
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; Integrin; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    787       Integrin beta-6.
FT                                /FTId=PRO_0000016351.
FT   TOPO_DOM     22    708       Extracellular. {ECO:0000255}.
FT   TRANSMEM    709    729       Helical. {ECO:0000255}.
FT   TOPO_DOM    730    787       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      730    757       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    669       {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    701       {ECO:0000250}.
FT   DISULFID    649    677       {ECO:0000250}.
SQ   SEQUENCE   787 AA;  86042 MW;  C6438C6F1E6B7FBD CRC64;
     MGIELVCLFL LLLGRNDHVQ GGCAWGGAES CSDCLLTGPH CAWCSQENFT HLSGAGERCD
     TPANLLAKGC QLPFIENPVS RIEVLQNKPL SVGRQKNSSD IVQIAPQSLV LKLRPGREQT
     LQVQVRQTED YPVDLYYLMD LSASMDDDLN TIKELGSRLA KEMSKLTSNF RLGFGSFVEK
     PVSPFMKTTP EEITNPCSSI PYFCLPTFGF KHILPLTDDA ERFNEIVRKQ KISANIDTPE
     GGFDAIMQAA VCKEKIGWRN DSLHLLVFVS DADSHFGMDS KLAGIVIPND GLCHLDHRNE
     YSMSTVLEYP TIGQLIDKLV QNNVLLIFAV TQEQVHLYEN YAKLIPGATV GLLQKDSGNI
     LQLIISAYEE LRSEVELEVL GDTEGLNLSF TALCNNGVLF PHQKKCSHMK VGDTASFNVT
     VSVSNCEKRS RNLIIKPVGL GDTLEILVSA ECDCDCQREI ETNSSKCHNG NGSFQCGVCT
     CNPGHMGPHC ECGEDMVSTD SCKESPGHPS CSGRGDCYCG QCICHLSPYG SIYGPYCQCD
     NFSCLRHKGL LCGDNGDCDC GECVCRDGWT GEYCNCTTNR DSCTSEDGVL CSGRGDCVCG
     KCVCRNPGAS GPTCERCPTC GDPCNSKRSC IECYLSADGQ AQEECADKCK AIGATISEED
     FSKDTSVSCS LQGENECLIT FLITTDNEGK TIIHNINEKD CPKPPNIPMI MLGVSLAILL
     IGVVLLCIWK LLVSFHDRKE VAKFEAERSK AKWQTGTNPL YRGSTSTFKN VTYKHREKHK
     AGLSSDG
//
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