ITB7_MOUSE
ID ITB7_MOUSE Reviewed; 806 AA.
AC P26011; Q3U2M1; Q64656;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Integrin beta-7;
DE AltName: Full=Integrin beta-P;
DE AltName: Full=M290 IEL antigen;
DE Flags: Precursor;
GN Name=Itgb7;
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].
RX PubMed=1518854; DOI=10.1073/pnas.89.17.8254;
RA Hu M.C.T., Crowe D.T., Weissman I.L., Holzmann B.;
RT "Cloning and expression of mouse integrin beta p(beta 7): a functional role
RT in Peyer's patch-specific lymphocyte homing.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8254-8258(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1559978; DOI=10.1016/s0021-9258(18)42524-0;
RA Yuan Q., Jiang W.-M., Leung E., Hollander D., Watson J.D., Krissansen G.W.;
RT "Molecular cloning of the mouse integrin beta 7 subunit.";
RL J. Biol. Chem. 267:7352-7358(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1381390;
RA Gurish M.F., Bell A.F., Smith T.J., Ducharme L.A., Wang R.K., Weis J.H.;
RT "Expression of murine beta 7, alpha 4, and beta 1 integrin genes by rodent
RT mast cells.";
RL J. Immunol. 149:1964-1972(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Colon;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [6]
RP NUCLEOTIDE SEQUENCE OF 1-90, AND PROTEIN SEQUENCE OF 20-32.
RX PubMed=1710115; DOI=10.1016/0006-291x(91)90448-g;
RA Yuan Q., Jiang W.-M., Hollander D., Leung E., Watson J.D., Krissansen G.W.;
RT "Identity between the novel integrin beta 7 subunit and an antigen found
RT highly expressed on intraepithelial lymphocytes in the small intestine.";
RL Biochem. Biophys. Res. Commun. 176:1443-1449(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE OF 1-67.
RX PubMed=8318458; DOI=10.1093/intimm/5.5.551;
RA Leung E., Mead P.E., Yuan Q., Jiang W.M., Watson J.D., Krissansen G.W.;
RT "The mouse beta 7 integrin gene promoter: transcriptional regulation of the
RT leukocyte integrins LPAM-1 and M290.";
RL Int. Immunol. 5:551-558(1993).
CC -!- FUNCTION: Integrin alpha-4/beta-7 (Peyer patches-specific homing
CC receptor LPAM-1) is involved in adhesive interactions of leukocytes. It
CC is a receptor for fibronectin and recognizes one or more domains within
CC the alternatively spliced CS-1 region of fibronectin. Integrin alpha-
CC 4/beta-7 is also a receptor for MADCAM1 and VCAM1. It recognizes the
CC sequence L-D-T in MADCAM1. Integrin alpha-E/beta-7 is a receptor for E-
CC cadherin.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-7 associates
CC with either alpha-4 or alpha-E. Interacts with FLNA (via filamin
CC repeats 4, 9, 12, 17, 19, 21, and 23). {ECO:0000250|UniProtKB:P26010}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M68903; AAA02749.1; -; mRNA.
DR EMBL; M95632; AAA39323.1; -; mRNA.
DR EMBL; M95633; AAA39324.1; -; mRNA.
DR EMBL; S44607; AAB23193.1; -; mRNA.
DR EMBL; AK078871; BAC37433.1; -; mRNA.
DR EMBL; AK154766; BAE32815.1; -; mRNA.
DR EMBL; AK155207; BAE33119.1; -; mRNA.
DR EMBL; BC011184; AAH11184.1; -; mRNA.
DR EMBL; S63504; AAB27396.1; -; Genomic_DNA.
DR CCDS; CCDS49740.1; -.
DR PIR; A46271; A46271.
DR PIR; I54754; I54754.
DR RefSeq; NP_038594.2; NM_013566.2.
DR AlphaFoldDB; P26011; -.
DR SMR; P26011; -.
DR ComplexPortal; CPX-3077; integrin alpha4-beta7 complex.
DR ComplexPortal; CPX-3127; Integrin alphaE-beta7 complex.
DR STRING; 10090.ENSMUSP00000001327; -.
DR BindingDB; P26011; -.
DR ChEMBL; CHEMBL2111481; -.
DR GlyGen; P26011; 8 sites.
DR iPTMnet; P26011; -.
DR PhosphoSitePlus; P26011; -.
DR EPD; P26011; -.
DR jPOST; P26011; -.
DR MaxQB; P26011; -.
DR PaxDb; P26011; -.
DR PeptideAtlas; P26011; -.
DR PRIDE; P26011; -.
DR ProteomicsDB; 301693; -.
DR Antibodypedia; 26942; 529 antibodies from 38 providers.
DR DNASU; 16421; -.
DR Ensembl; ENSMUST00000001327; ENSMUSP00000001327; ENSMUSG00000001281.
DR GeneID; 16421; -.
DR KEGG; mmu:16421; -.
DR UCSC; uc012aaa.1; mouse.
DR CTD; 3695; -.
DR MGI; MGI:96616; Itgb7.
DR VEuPathDB; HostDB:ENSMUSG00000001281; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01030000234611; -.
DR HOGENOM; CLU_011772_2_1_1; -.
DR InParanoid; P26011; -.
DR OMA; VDFWVTL; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P26011; -.
DR TreeFam; TF105392; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR BioGRID-ORCS; 16421; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Itgb7; mouse.
DR PRO; PR:P26011; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P26011; protein.
DR Bgee; ENSMUSG00000001281; Expressed in blood and 128 other tissues.
DR ExpressionAtlas; P26011; baseline and differential.
DR Genevisible; P26011; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0034669; C:integrin alpha4-beta7 complex; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0003366; P:cell-matrix adhesion involved in ameboidal cell migration; ISO:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0050900; P:leukocyte migration; IMP:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:0043113; P:receptor clustering; ISO:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0072678; P:T cell migration; IMP:MGI.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015437; Integrin_bsu-7.
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:SF36; PTHR10082:SF36; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF08725; Integrin_b_cyt; 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; 4.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Integrin; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1710115"
FT CHAIN 20..806
FT /note="Integrin beta-7"
FT /id="PRO_0000016353"
FT TOPO_DOM 20..724
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..806
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 150..389
FT /note="VWFA"
FT REPEAT 478..526
FT /note="I"
FT REPEAT 527..565
FT /note="II"
FT REPEAT 566..604
FT /note="III"
FT REPEAT 605..640
FT /note="IV"
FT REGION 98..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..640
FT /note="Cysteine-rich tandem repeats"
FT REGION 786..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..476
FT /evidence="ECO:0000250"
FT DISULFID 51..61
FT /evidence="ECO:0000250"
FT DISULFID 54..91
FT /evidence="ECO:0000250"
FT DISULFID 64..80
FT /evidence="ECO:0000250"
FT DISULFID 216..223
FT /evidence="ECO:0000250"
FT DISULFID 271..311
FT /evidence="ECO:0000250"
FT DISULFID 412..428
FT /evidence="ECO:0000250"
FT DISULFID 448..688
FT /evidence="ECO:0000250"
FT DISULFID 474..478
FT /evidence="ECO:0000250"
FT DISULFID 488..500
FT /evidence="ECO:0000250"
FT DISULFID 497..537
FT /evidence="ECO:0000250"
FT DISULFID 502..511
FT /evidence="ECO:0000250"
FT DISULFID 513..527
FT /evidence="ECO:0000250"
FT DISULFID 543..548
FT /evidence="ECO:0000250"
FT DISULFID 545..574
FT /evidence="ECO:0000250"
FT DISULFID 550..559
FT /evidence="ECO:0000250"
FT DISULFID 561..566
FT /evidence="ECO:0000250"
FT DISULFID 580..585
FT /evidence="ECO:0000250"
FT DISULFID 582..613
FT /evidence="ECO:0000250"
FT DISULFID 587..596
FT /evidence="ECO:0000250"
FT DISULFID 598..605
FT /evidence="ECO:0000250"
FT DISULFID 619..624
FT /evidence="ECO:0000250"
FT DISULFID 621..666
FT /evidence="ECO:0000250"
FT DISULFID 626..635
FT /evidence="ECO:0000250"
FT DISULFID 638..641
FT /evidence="ECO:0000250"
FT DISULFID 645..654
FT /evidence="ECO:0000250"
FT CONFLICT 81
FT /note="A -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="A -> G (in Ref. 3; AAB23193)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="Missing (in Ref. 2; AAA02749)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="S -> C (in Ref. 3; AAB23193)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="R -> H (in Ref. 2; AAA02749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 87411 MW; E793A3F3BA0B5C18 CRC64;
MVDSSTVLIF LLVLGGGQSE LDTKITSSGE AAEWEDPDLS LQGSCQPVPS CQKCILSHPS
CAWCKQLNFT ASGEAEARRC ARREELLARG CPAQELEEPR GRQEVLQDKP LSQGDRGEGA
TQLAPQRIRV TLRPGEPQKF RVRFLRAAGY PVDLYYLMDL SYSMKDDLER VRQLGHALLV
RLQEVTHSVR IGFGSFVDKT VLPFVSTVPS KLHHPCPSRL ERCQPPFSFH HVLSLTGDAQ
AFEREVGRQN VSGNLDSPEG GFDAILQAAL CQEQIGWRNV SRLLVFTSDD TFHTAGDGKL
GGIFMPSDGR CHLDSNGVYT NSAEFDYPSV GQVAQALTAA NIQPIFAVTG ATLPVYQELR
QLIPKSAVGE LSEDSSNVVQ LIMDAYDSLS STVTLEHSPL PPGVSISFES HCKGPEKTEG
EAGDRGQCND VRVNQTVDFW VTLQATHCLP EAHVLRLWAL GFSEELTVEL HTVCDCNCGD
AQPHAPYCSD GQGDLQCGIC SCAPGRLGQL CECSEADLSS PDLESGCRAP NGTGPLCSGK
GRCQCGRCSC SGQSSGRLCE CDDASCERHE GILCGGFGHC QCGVCHCHAN HTGRACECSK
SVDSCVSPEG GLCSGHGYCK CNRCQCLDGY YGALCDQCLG CKSPCEQYRD CAECGAFGTG
PLAANCSVVC ADVNVTLTLA PNLDDGWCKE RTIDNQLFFF LVEHAASGIV LRVRPQEKGV
DHTRAIILGC TGGIVAVGLG LVLAYRLSVE IYDRREYRRF EKEQQQLNWK QDNNPLYKSA
ITTTVNPRFQ GTNGRSPSLS LTREAD
