ITB7_HUMAN
ID ITB7_HUMAN Reviewed; 798 AA.
AC P26010; Q9UCP7; Q9UCS7;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Integrin beta-7;
DE AltName: Full=Gut homing receptor beta subunit;
DE Flags: Precursor;
GN Name=ITGB7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=T-cell;
RX PubMed=2083230; DOI=10.1093/intimm/2.11.1097;
RA Yuan Q., Jiang W.-M., Krissansen G.W., Watson J.D.;
RT "Cloning and sequence analysis of a novel beta 2-related integrin
RT transcript from T lymphocytes: homology of integrin cysteine-rich repeats
RT to domain III of laminin B chains.";
RL Int. Immunol. 2:1097-1108(1990).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=1777426; DOI=10.1093/intimm/3.12.1373;
RA Yuan Q., Jiang W.-M., Krissansen G.W., Watson J.D.;
RT "Cloning and sequence analysis of a novel beta 2-related integrin
RT transcript from T lymphocytes: homology of integrin cysteine-rich repeats
RT to domain III of laminin B chains.";
RL Int. Immunol. 3:1373-1374(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=Leukocyte;
RX PubMed=2040616; DOI=10.1016/s0021-9258(18)99120-9;
RA Erle D.J., Rueegg C., Sheppard D., Pytela R.;
RT "Complete amino acid sequence of an integrin beta subunit (beta 7)
RT identified in leukocytes.";
RL J. Biol. Chem. 266:11009-11016(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1382574; DOI=10.1093/intimm/4.9.1031;
RA Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D.,
RA Krissansen G.W.;
RT "The gene organization of the human beta 7 subunit, the common beta subunit
RT of the leukocyte integrins HML-1 and LPAM-1.";
RL Int. Immunol. 4:1031-1040(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC 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 [6]
RP PROTEIN SEQUENCE OF 20-36, INTERACTION WITH INTEGRIN ALPHA-4 AND INTEGRIN
RP ALPHA-E, AND INDUCTION.
RX PubMed=1542691; DOI=10.1073/pnas.89.5.1924;
RA Parker C.M., Cepek K.L., Russell G.J., Shaw S.K., Posnett D.N.,
RA Schwarting R., Brenner M.B.;
RT "A family of beta 7 integrins on human mucosal lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1924-1928(1992).
RN [7]
RP PROTEIN SEQUENCE OF 20-34.
RC TISSUE=Leukemia;
RX PubMed=1750505;
RA Micklem K.J., Dong Y., Willis A., Pulford K.A., Visser L., Duerkop H.,
RA Poppema S., Stein H., Mason D.Y.;
RT "HML-1 antigen on mucosa-associated T cells, activated cells, and hairy
RT leukemic cells is a new integrin containing the beta 7 subunit.";
RL Am. J. Pathol. 139:1297-1301(1991).
RN [8]
RP MUTAGENESIS OF ASP-159.
RX PubMed=10837471; DOI=10.1074/jbc.m001228200;
RA Higgins J.M.G., Cernadas M., Tan K., Irie A., Wang J.-H., Takada Y.,
RA Brenner M.B.;
RT "The role of alpha and beta chains in ligand recognition by beta 7
RT integrins.";
RL J. Biol. Chem. 275:25652-25664(2000).
RN [9]
RP REVIEW.
RX PubMed=12297042; DOI=10.1016/s0092-8674(02)00971-6;
RA Hynes R.O.;
RT "Integrins: bidirectional, allosteric signaling machines.";
RL Cell 110:673-687(2002).
RN [10]
RP INTERACTION WITH HIV-1 GP120.
RX PubMed=18264102; DOI=10.1038/ni1566;
RA Arthos J., Cicala C., Martinelli E., Macleod K., Van Ryk D., Wei D.,
RA Xiao Z., Veenstra T.D., Conrad T.P., Lempicki R.A., McLaughlin S.,
RA Pascuccio M., Gopaul R., McNally J., Cruz C.C., Censoplano N., Chung E.,
RA Reitano K.N., Kottilil S., Goode D.J., Fauci A.S.;
RT "HIV-1 envelope protein binds to and signals through integrin alpha4beta7,
RT the gut mucosal homing receptor for peripheral T cells.";
RL Nat. Immunol. 9:301-309(2008).
RN [11]
RP INTERACTION WITH FLNA.
RX PubMed=19828450; DOI=10.1074/jbc.m109.060954;
RA Ithychanda S.S., Hsu D., Li H., Yan L., Liu D.D., Liu D., Das M.,
RA Plow E.F., Qin J.;
RT "Identification and characterization of multiple similar ligand-binding
RT repeats in filamin: implication on filamin-mediated receptor clustering and
RT cross-talk.";
RL J. Biol. Chem. 284:35113-35121(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 768-798.
RX PubMed=16455489; DOI=10.1016/j.molcel.2006.01.011;
RA Kiema T., Lad Y., Jiang P., Oxley C.L., Baldassarre M., Wegener K.L.,
RA Campbell I.D., Ylanne J., Calderwood D.A.;
RT "The molecular basis of filamin binding to integrins and competition with
RT talin.";
RL Mol. Cell 21:337-347(2006).
CC -!- FUNCTION: Integrin alpha-4/beta-7 (Peyer patches-specific homing
CC receptor LPAM-1) is an adhesion molecule that mediates lymphocyte
CC migration and homing to gut-associated lymphoid tissue (GALT). Integrin
CC alpha-4/beta-7 interacts with the cell surface adhesion molecules
CC MADCAM1 which is normally expressed by the vascular endothelium of the
CC gastrointestinal tract. Interacts also with VCAM1 and fibronectin, an
CC extracellular matrix component. It recognizes one or more domains
CC within the alternatively spliced CS-1 region of fibronectin.
CC Interactions involves the tripeptide L-D-T in MADCAM1, and L-D-V in
CC fibronectin. Binds to HIV-1 gp120, thereby allowing the virus to enter
CC GALT, which is thought to be the major trigger of AIDS disease.
CC Interaction would involve a tripeptide L-D-I in HIV-1 gp120. Integrin
CC alpha-E/beta-7 (HML-1) is a receptor for E-cadherin.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-7 associates
CC with either alpha-4 or alpha-E. Integrin alpha-4/beta-7 interacts with
CC MADCAM1, VCAM1, fibronectin, and may also interact with HIV-1 gp120.
CC Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23)
CC (PubMed:19828450). {ECO:0000269|PubMed:1542691,
CC ECO:0000269|PubMed:18264102, ECO:0000269|PubMed:19828450}.
CC -!- INTERACTION:
CC P26010; P21333: FLNA; NbExp=6; IntAct=EBI-702932, EBI-350432;
CC P26010; P13612: ITGA4; NbExp=6; IntAct=EBI-702932, EBI-703044;
CC P26010-1; P21333: FLNA; NbExp=2; IntAct=EBI-15944630, EBI-350432;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P26010-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P26010-2; Sequence=VSP_002753;
CC -!- TISSUE SPECIFICITY: Expressed in a variety of leukocyte lines.
CC -!- INDUCTION: Integrin alpha-E/beta-7 is induced by TGFB1.
CC {ECO:0000269|PubMed:1542691}.
CC -!- DOMAIN: Domain I contains three cation-binding sites: the ligand-
CC integrin-binding site (LIMBS), the metal ion-dependent adhesion site
CC (MIDAS), and the adjacent to MIDAS site (ADMIDAS). In the absence of a
CC ligand or in calcium-dependent binding, only ADMIDAS is occupied. In
CC magnesium-dependent binding all three sites bind metal ions. LIMBS
CC positively modify ligand binding whereas ADMIDAS negatively modify
CC ligand binding.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; M68892; AAA59184.1; -; mRNA.
DR EMBL; S80335; AAB21332.1; -; mRNA.
DR EMBL; M62880; AAA59185.1; -; mRNA.
DR EMBL; L23823; AAA36118.1; -; Genomic_DNA.
DR EMBL; L23810; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23811; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23812; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23813; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23814; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23815; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23816; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23817; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23818; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23819; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23820; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23821; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; L23822; AAA36118.1; JOINED; Genomic_DNA.
DR EMBL; S49378; AAB23688.1; -; Genomic_DNA.
DR EMBL; S49364; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49365; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49366; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49367; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49368; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49369; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49370; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49371; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49373; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49374; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49375; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49376; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; S49377; AAB23688.1; JOINED; Genomic_DNA.
DR EMBL; BC015916; AAH15916.1; -; mRNA.
DR CCDS; CCDS8849.1; -. [P26010-1]
DR PIR; A40526; A40526.
DR RefSeq; NP_000880.1; NM_000889.2. [P26010-1]
DR RefSeq; XP_005268908.1; XM_005268851.3. [P26010-1]
DR RefSeq; XP_005268909.1; XM_005268852.4. [P26010-1]
DR PDB; 2BRQ; X-ray; 2.10 A; C/D=768-798.
DR PDB; 3V4P; X-ray; 3.15 A; B/D=20-512.
DR PDB; 3V4V; X-ray; 3.10 A; B/D=20-512.
DR PDBsum; 2BRQ; -.
DR PDBsum; 3V4P; -.
DR PDBsum; 3V4V; -.
DR AlphaFoldDB; P26010; -.
DR BMRB; P26010; -.
DR SMR; P26010; -.
DR BioGRID; 109901; 58.
DR ComplexPortal; CPX-1823; Integrin alpha4-beta7 complex.
DR ComplexPortal; CPX-1824; Integrin alphaE-beta7 complex.
DR CORUM; P26010; -.
DR DIP; DIP-34970N; -.
DR ELM; P26010; -.
DR IntAct; P26010; 3.
DR MINT; P26010; -.
DR STRING; 9606.ENSP00000267082; -.
DR BindingDB; P26010; -.
DR ChEMBL; CHEMBL2979; -.
DR DrugBank; DB05122; R1295.
DR DrugBank; DB09033; Vedolizumab.
DR DrugCentral; P26010; -.
DR GuidetoPHARMACOLOGY; 2461; -.
DR GlyGen; P26010; 8 sites.
DR iPTMnet; P26010; -.
DR PhosphoSitePlus; P26010; -.
DR BioMuta; ITGB7; -.
DR DMDM; 124973; -.
DR jPOST; P26010; -.
DR MassIVE; P26010; -.
DR MaxQB; P26010; -.
DR PaxDb; P26010; -.
DR PeptideAtlas; P26010; -.
DR PRIDE; P26010; -.
DR ProteomicsDB; 54307; -. [P26010-1]
DR ProteomicsDB; 54308; -. [P26010-2]
DR ABCD; P26010; 4 sequenced antibodies.
DR Antibodypedia; 26942; 529 antibodies from 38 providers.
DR DNASU; 3695; -.
DR Ensembl; ENST00000267082.10; ENSP00000267082.4; ENSG00000139626.16. [P26010-1]
DR Ensembl; ENST00000422257.7; ENSP00000408741.3; ENSG00000139626.16. [P26010-1]
DR Ensembl; ENST00000550743.6; ENSP00000455374.2; ENSG00000139626.16. [P26010-2]
DR GeneID; 3695; -.
DR KEGG; hsa:3695; -.
DR MANE-Select; ENST00000267082.10; ENSP00000267082.4; NM_000889.3; NP_000880.1.
DR UCSC; uc001scc.4; human. [P26010-1]
DR CTD; 3695; -.
DR DisGeNET; 3695; -.
DR GeneCards; ITGB7; -.
DR HGNC; HGNC:6162; ITGB7.
DR HPA; ENSG00000139626; Tissue enhanced (lymphoid).
DR MIM; 147559; gene.
DR neXtProt; NX_P26010; -.
DR OpenTargets; ENSG00000139626; -.
DR PharmGKB; PA29961; -.
DR VEuPathDB; HostDB:ENSG00000139626; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01030000234611; -.
DR HOGENOM; CLU_011772_2_1_1; -.
DR InParanoid; P26010; -.
DR OMA; VDFWVTL; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P26010; -.
DR TreeFam; TF105392; -.
DR PathwayCommons; P26010; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR SignaLink; P26010; -.
DR SIGNOR; P26010; -.
DR BioGRID-ORCS; 3695; 224 hits in 1068 CRISPR screens.
DR ChiTaRS; ITGB7; human.
DR EvolutionaryTrace; P26010; -.
DR GeneWiki; ITGB7; -.
DR GenomeRNAi; 3695; -.
DR Pharos; P26010; Tclin.
DR PRO; PR:P26010; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P26010; protein.
DR Bgee; ENSG00000139626; Expressed in granulocyte and 166 other tissues.
DR ExpressionAtlas; P26010; baseline and differential.
DR Genevisible; P26010; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0034669; C:integrin alpha4-beta7 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; IMP:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
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; IMP:UniProtKB.
DR GO; GO:0003366; P:cell-matrix adhesion involved in ameboidal cell migration; IMP:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0072678; P:T cell migration; IEA:Ensembl.
DR Gene3D; 3.40.50.410; -; 1.
DR IDEAL; IID00616; -.
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 3D-structure; Alternative splicing; Cell adhesion;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Integrin; Magnesium; Membrane;
KW Metal-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1542691,
FT ECO:0000269|PubMed:1750505"
FT CHAIN 20..798
FT /note="Integrin beta-7"
FT /id="PRO_0000016352"
FT TOPO_DOM 20..723
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..798
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..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..640
FT /note="Cysteine-rich tandem repeats"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000250"
FT MOD_RES 778
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
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 477
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 VAR_SEQ 501..648
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:2040616"
FT /id="VSP_002753"
FT VARIANT 672
FT /note="H -> Y (in dbSNP:rs11539433)"
FT /id="VAR_049637"
FT MUTAGEN 159
FT /note="D->A: Loss of integrin alpha-E/beta-7 binding to E-
FT cadherin and of integrin alpha-4/beta-7 binding to
FT MADCAM1."
FT /evidence="ECO:0000269|PubMed:10837471"
FT CONFLICT 34
FT /note="W -> A (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3V4V"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:3V4V"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:3V4V"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3V4V"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:3V4V"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 436..445
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:3V4V"
FT STRAND 777..786
FT /evidence="ECO:0007829|PDB:2BRQ"
SQ SEQUENCE 798 AA; 86903 MW; CBE275E0E9992385 CRC64;
MVALPMVLVL LLVLSRGESE LDAKIPSTGD ATEWRNPHLS MLGSCQPAPS CQKCILSHPS
CAWCKQLNFT ASGEAEARRC ARREELLARG CPLEELEEPR GQQEVLQDQP LSQGARGEGA
TQLAPQRVRV TLRPGEPQQL QVRFLRAEGY PVDLYYLMDL SYSMKDDLER VRQLGHALLV
RLQEVTHSVR IGFGSFVDKT VLPFVSTVPS KLRHPCPTRL ERCQSPFSFH HVLSLTGDAQ
AFEREVGRQS VSGNLDSPEG GFDAILQAAL CQEQIGWRNV SRLLVFTSDD TFHTAGDGKL
GGIFMPSDGH CHLDSNGLYS RSTEFDYPSV GQVAQALSAA NIQPIFAVTS AALPVYQELS
KLIPKSAVGE LSEDSSNVVQ LIMDAYNSLS STVTLEHSSL PPGVHISYES QCEGPEKREG
KAEDRGQCNH VRINQTVTFW VSLQATHCLP EPHLLRLRAL GFSEELIVEL HTLCDCNCSD
TQPQAPHCSD GQGHLQCGVC SCAPGRLGRL CECSVAELSS PDLESGCRAP NGTGPLCSGK
GHCQCGRCSC SGQSSGHLCE CDDASCERHE GILCGGFGRC QCGVCHCHAN RTGRACECSG
DMDSCISPEG GLCSGHGRCK CNRCQCLDGY YGALCDQCPG CKTPCERHRD CAECGAFRTG
PLATNCSTAC AHTNVTLALA PILDDGWCKE RTLDNQLFFF LVEDDARGTV VLRVRPQEKG
ADHTQAIVLG CVGGIVAVGL GLVLAYRLSV EIYDRREYSR FEKEQQQLNW KQDSNPLYKS
AITTTINPRF QEADSPTL
