GenomeNet

Database: UniProt
Entry: P26011
LinkDB: P26011
Original site: P26011 
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   10-APR-2019, entry version 182.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   role 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;
RA   Yuan Q., Jiang W.-M., Leung E., Hollander D., Watson J.D.,
RA   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.,
RA   Weis J.H.;
RT   "Expression of murine beta 7, alpha 4, and beta 1 integrin genes by
RT   rodent 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.,
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   [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
RT   project: 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.,
RA   Krissansen G.W.;
RT   "Identity between the novel integrin beta 7 subunit and an antigen
RT   found highly expressed on intraepithelial lymphocytes in the small
RT   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.,
RA   Krissansen G.W.;
RT   "The mouse beta 7 integrin gene promoter: transcriptional regulation
RT   of the 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
CC       leukocytes. It is a receptor for fibronectin and recognizes one or
CC       more domains within the alternatively spliced CS-1 region of
CC       fibronectin. Integrin alpha-4/beta-7 is also a receptor for
CC       MADCAM1 and VCAM1. It recognizes the sequence L-D-T in MADCAM1.
CC       Integrin alpha-E/beta-7 is a receptor for E-cadherin.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-7
CC       associates with either alpha-4 or alpha-E. Interacts with FLNA
CC       (via filamin repeats 4, 9, 12, 17, 19, 21, and 23).
CC       {ECO:0000250|UniProtKB:P26010}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
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   UniGene; Mm.58; -.
DR   ProteinModelPortal; 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   iPTMnet; P26011; -.
DR   PhosphoSitePlus; P26011; -.
DR   EPD; P26011; -.
DR   MaxQB; P26011; -.
DR   PaxDb; P26011; -.
DR   PeptideAtlas; P26011; -.
DR   PRIDE; P26011; -.
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   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P26011; -.
DR   KO; K06590; -.
DR   OMA; FWVTLQA; -.
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   ChiTaRS; Itgb7; mouse.
DR   PRO; PR:P26011; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000001281; Expressed in 128 organ(s), highest expression level in mesenteric lymph node.
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:0008305; C:integrin complex; IBA:GO_Central.
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; IPR040622; I-EGF_1.
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; PF18372; I-EGF_1; 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; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Integrin; Membrane; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000269|PubMed:1710115}.
FT   CHAIN        20    806       Integrin beta-7.
FT                                /FTId=PRO_0000016353.
FT   TOPO_DOM     20    724       Extracellular. {ECO:0000255}.
FT   TRANSMEM    725    745       Helical. {ECO:0000255}.
FT   TOPO_DOM    746    806       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      150    389       VWFA.
FT   REPEAT      478    526       I.
FT   REPEAT      527    565       II.
FT   REPEAT      566    604       III.
FT   REPEAT      605    640       IV.
FT   REGION      478    640       Cysteine-rich tandem repeats.
FT   CARBOHYD     68     68       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    250    250       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    279    279       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    434    434       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    531    531       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    590    590       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    665    665       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    674    674       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     45    476       {ECO:0000250}.
FT   DISULFID     51     61       {ECO:0000250}.
FT   DISULFID     54     91       {ECO:0000250}.
FT   DISULFID     64     80       {ECO:0000250}.
FT   DISULFID    216    223       {ECO:0000250}.
FT   DISULFID    271    311       {ECO:0000250}.
FT   DISULFID    412    428       {ECO:0000250}.
FT   DISULFID    448    688       {ECO:0000250}.
FT   DISULFID    474    478       {ECO:0000250}.
FT   DISULFID    488    500       {ECO:0000250}.
FT   DISULFID    497    537       {ECO:0000250}.
FT   DISULFID    502    511       {ECO:0000250}.
FT   DISULFID    513    527       {ECO:0000250}.
FT   DISULFID    543    548       {ECO:0000250}.
FT   DISULFID    545    574       {ECO:0000250}.
FT   DISULFID    550    559       {ECO:0000250}.
FT   DISULFID    561    566       {ECO:0000250}.
FT   DISULFID    580    585       {ECO:0000250}.
FT   DISULFID    582    613       {ECO:0000250}.
FT   DISULFID    587    596       {ECO:0000250}.
FT   DISULFID    598    605       {ECO:0000250}.
FT   DISULFID    619    624       {ECO:0000250}.
FT   DISULFID    621    666       {ECO:0000250}.
FT   DISULFID    626    635       {ECO:0000250}.
FT   DISULFID    638    641       {ECO:0000250}.
FT   DISULFID    645    654       {ECO:0000250}.
FT   CONFLICT     81     81       A -> E (in Ref. 6; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     81     81       A -> G (in Ref. 3; AAB23193).
FT                                {ECO:0000305}.
FT   CONFLICT    124    124       Missing (in Ref. 2; AAA02749).
FT                                {ECO:0000305}.
FT   CONFLICT    538    538       S -> C (in Ref. 3; AAB23193).
FT                                {ECO:0000305}.
FT   CONFLICT    557    557       R -> H (in Ref. 2; AAA02749).
FT                                {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
//
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