ITB6_MOUSE
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 03-AUG-2022, entry version 177.
DE RecName: Full=Integrin beta-6;
DE Flags: Precursor;
GN Name=Itgb6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=11095652; DOI=10.1681/asn.v11122297;
RA Arend L.J., Smart A.M., Briggs J.P.;
RT "Mouse beta(6) integrin sequence, pattern of expression, and role in kidney
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT 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 expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
RX PubMed=10025398; DOI=10.1016/s0092-8674(00)80545-0;
RA Munger J.S., Huang X., Kawakatsu H., Griffiths M.J., Dalton S.L., Wu J.,
RA Pittet J.F., Kaminski N., Garat C., Matthay M.A., Rifkin D.B., 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 sequence
CC R-G-D in its ligands (PubMed:10025398). 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 (PubMed:10025398).
CC {ECO:0000250|UniProtKB:P18564, ECO:0000269|PubMed:10025398}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:10025398).
CC Interacts with FLNB (By similarity). Interacts with HAX1 (By
CC similarity). ITGAV:ITGB6 interacts with FBN1 (By similarity).
CC 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 protein.
CC Cell junction, focal adhesion {ECO:0000250|UniProtKB:P18564}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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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 AlphaFoldDB; Q9Z0T9; -.
DR SMR; Q9Z0T9; -.
DR ComplexPortal; CPX-3132; Integrin alphav-beta6 complex.
DR STRING; 10090.ENSMUSP00000028348; -.
DR CarbonylDB; Q9Z0T9; -.
DR GlyGen; Q9Z0T9; 9 sites.
DR iPTMnet; Q9Z0T9; -.
DR PhosphoSitePlus; Q9Z0T9; -.
DR jPOST; Q9Z0T9; -.
DR MaxQB; Q9Z0T9; -.
DR PaxDb; Q9Z0T9; -.
DR PRIDE; Q9Z0T9; -.
DR ProteomicsDB; 268902; -.
DR ABCD; Q9Z0T9; 11 sequenced antibodies.
DR Antibodypedia; 33727; 350 antibodies from 28 providers.
DR DNASU; 16420; -.
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 VEuPathDB; HostDB:ENSMUSG00000026971; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR InParanoid; Q9Z0T9; -.
DR OMA; LSGPHCA; -.
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-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 16420; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9Z0T9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z0T9; protein.
DR Bgee; ENSMUSG00000026971; Expressed in right kidney and 90 other tissues.
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; IDA:MGI.
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: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:0060348; P:bone development; IMP:MGI.
DR GO; GO:0060435; P:bronchiole development; IDA:MGI.
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:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:MGI.
DR GO; GO:0070166; P:enamel mineralization; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0060022; P:hard palate development; IGI:MGI.
DR GO; GO:0006955; P:immune response; IGI:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0061520; P:Langerhans cell differentiation; IGI:MGI.
DR GO; GO:0048286; P:lung alveolus development; IDA:MGI.
DR GO; GO:0055091; P:phospholipid homeostasis; IMP:MGI.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IGI:MGI.
DR GO; GO:0009611; P:response to wounding; IDA:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
DR GO; GO:0043129; P:surfactant homeostasis; IMP:MGI.
DR GO; GO:0071604; P:transforming growth factor beta production; IDA:CAFA.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
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; Integrin;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..787
FT /note="Integrin beta-6"
FT /id="PRO_0000016351"
FT TOPO_DOM 22..708
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..787
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 730..757
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..669
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..701
FT /evidence="ECO:0000250"
FT DISULFID 649..677
FT /evidence="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
