GenomeNet

Database: UniProt
Entry: P26010
LinkDB: P26010
Original site: P26010 
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   10-APR-2019, entry version 193.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   repeats 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
RT   repeats 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;
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
RT   subunit 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
RT   project: 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
RP   INTEGRIN 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
RT   hairy leukemic cells is a new integrin containing the beta 7
RT   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.,
RA   Chung E., Reitano K.N., Kottilil S., Goode D.J., Fauci A.S.;
RT   "HIV-1 envelope protein binds to and signals through integrin
RT   alpha4beta7, 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-
RT   binding repeats in filamin: implication on filamin-mediated receptor
RT   clustering and 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
RT   with 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).
CC       Integrin alpha-4/beta-7 interacts with the cell surface adhesion
CC       molecules MADCAM1 which is normally expressed by the vascular
CC       endothelium of the gastrointestinal tract. Interacts also with
CC       VCAM1 and fibronectin, an extracellular matrix component. It
CC       recognizes one or more domains within the alternatively spliced
CC       CS-1 region of fibronectin. Interactions involves the tripeptide
CC       L-D-T in MADCAM1, and L-D-V in fibronectin. Binds to HIV-1 gp120,
CC       thereby allowing the virus to enter GALT, which is thought to be
CC       the major trigger of AIDS disease. Interaction would involve a
CC       tripeptide L-D-I in HIV-1 gp120. Integrin alpha-E/beta-7 (HML-1)
CC       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. Integrin alpha-4/beta-7
CC       interacts with MADCAM1, VCAM1, fibronectin, and may also interact
CC       with HIV-1 gp120. Interacts with FLNA (via filamin repeats 4, 9,
CC       12, 17, 19, 21, and 23) (PubMed:19828450).
CC       {ECO:0000269|PubMed:1542691, ECO:0000269|PubMed:18264102,
CC       ECO:0000269|PubMed:19828450}.
CC   -!- INTERACTION:
CC       P21333:FLNA; NbExp=6; IntAct=EBI-702932, EBI-350432;
CC       P13612:ITGA4; NbExp=6; IntAct=EBI-702932, EBI-703044;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       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
CC       site (MIDAS), and the adjacent to MIDAS site (ADMIDAS). In the
CC       absence of a ligand or in calcium-dependent binding, only ADMIDAS
CC       is occupied. In magnesium-dependent binding all three sites bind
CC       metal ions. LIMBS positively modify ligand binding whereas ADMIDAS
CC       negatively modify ligand binding.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
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   UniGene; Hs.654470; -.
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   ProteinModelPortal; P26010; -.
DR   SMR; P26010; -.
DR   BioGrid; 109901; 6.
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; DB05802; MLN-02.
DR   DrugBank; DB05122; R1295.
DR   DrugBank; DB09033; Vedolizumab.
DR   GuidetoPHARMACOLOGY; 2461; -.
DR   iPTMnet; P26010; -.
DR   PhosphoSitePlus; P26010; -.
DR   BioMuta; ITGB7; -.
DR   DMDM; 124973; -.
DR   jPOST; P26010; -.
DR   MaxQB; P26010; -.
DR   PaxDb; P26010; -.
DR   PeptideAtlas; P26010; -.
DR   PRIDE; P26010; -.
DR   ProteomicsDB; 54307; -.
DR   ProteomicsDB; 54308; -. [P26010-2]
DR   DNASU; 3695; -.
DR   Ensembl; ENST00000267082; ENSP00000267082; ENSG00000139626. [P26010-1]
DR   Ensembl; ENST00000422257; ENSP00000408741; ENSG00000139626. [P26010-1]
DR   Ensembl; ENST00000550743; ENSP00000455374; ENSG00000139626. [P26010-2]
DR   GeneID; 3695; -.
DR   KEGG; hsa:3695; -.
DR   UCSC; uc001scc.4; human. [P26010-1]
DR   CTD; 3695; -.
DR   DisGeNET; 3695; -.
DR   EuPathDB; HostDB:ENSG00000139626.15; -.
DR   GeneCards; ITGB7; -.
DR   HGNC; HGNC:6162; ITGB7.
DR   HPA; HPA042277; -.
DR   MIM; 147559; gene.
DR   neXtProt; NX_P26010; -.
DR   OpenTargets; ENSG00000139626; -.
DR   PharmGKB; PA29961; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P26010; -.
DR   KO; K06590; -.
DR   OMA; FWVTLQA; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P26010; -.
DR   TreeFam; TF105392; -.
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   ChiTaRS; ITGB7; human.
DR   EvolutionaryTrace; P26010; -.
DR   GeneWiki; ITGB7; -.
DR   GenomeRNAi; 3695; -.
DR   PRO; PR:P26010; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000139626; Expressed in 182 organ(s), highest expression level in material anatomical entity.
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; IBA:GO_Central.
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:0030198; P:extracellular matrix organization; TAS:Reactome.
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:0050776; P:regulation of immune response; TAS:Reactome.
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   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; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Host cell receptor for virus entry; Integrin; Magnesium; Membrane;
KW   Metal-binding; Phosphoprotein; Polymorphism; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000269|PubMed:1542691,
FT                                ECO:0000269|PubMed:1750505}.
FT   CHAIN        20    798       Integrin beta-7.
FT                                /FTId=PRO_0000016352.
FT   TOPO_DOM     20    723       Extracellular. {ECO:0000255}.
FT   TRANSMEM    724    746       Helical. {ECO:0000255}.
FT   TOPO_DOM    747    798       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   METAL       159    159       Magnesium; MIDAS motif. {ECO:0000250}.
FT   METAL       161    161       Magnesium; MIDAS motif. {ECO:0000250}.
FT   METAL       163    163       Magnesium; MIDAS motif. {ECO:0000250}.
FT   METAL       166    166       Magnesium or calcium; ADMIDAS motif.
FT                                {ECO:0000250}.
FT   METAL       167    167       Magnesium or calcium; ADMIDAS motif.
FT                                {ECO:0000250}.
FT   METAL       198    198       Magnesium; LIMBS motif. {ECO:0000250}.
FT   METAL       254    254       Magnesium; LIMBS motif. {ECO:0000250}.
FT   METAL       256    256       Magnesium; LIMBS motif. {ECO:0000250}.
FT   METAL       259    259       Magnesium; LIMBS motif. {ECO:0000250}.
FT   METAL       289    289       Magnesium; MIDAS motif. {ECO:0000250}.
FT   MOD_RES     778    778       Phosphotyrosine; by Tyr-kinases.
FT                                {ECO:0000250}.
FT   CARBOHYD     68     68       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    477    477       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   VAR_SEQ     501    648       Missing (in isoform Short).
FT                                {ECO:0000303|PubMed:2040616}.
FT                                /FTId=VSP_002753.
FT   VARIANT     672    672       H -> Y (in dbSNP:rs11539433).
FT                                /FTId=VAR_049637.
FT   MUTAGEN     159    159       D->A: Loss of integrin alpha-E/beta-7
FT                                binding to E-cadherin and of integrin
FT                                alpha-4/beta-7 binding to MADCAM1.
FT                                {ECO:0000269|PubMed:10837471}.
FT   CONFLICT     34     34       W -> A (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND      102    105       {ECO:0000244|PDB:3V4V}.
FT   TURN        114    116       {ECO:0000244|PDB:3V4V}.
FT   STRAND      117    119       {ECO:0000244|PDB:3V4V}.
FT   STRAND      127    131       {ECO:0000244|PDB:3V4V}.
FT   STRAND      138    145       {ECO:0000244|PDB:3V4V}.
FT   STRAND      152    159       {ECO:0000244|PDB:3V4V}.
FT   HELIX       162    164       {ECO:0000244|PDB:3V4V}.
FT   HELIX       165    173       {ECO:0000244|PDB:3V4V}.
FT   HELIX       176    182       {ECO:0000244|PDB:3V4V}.
FT   TURN        183    185       {ECO:0000244|PDB:3V4V}.
FT   STRAND      189    196       {ECO:0000244|PDB:3V4V}.
FT   TURN        202    204       {ECO:0000244|PDB:3V4V}.
FT   HELIX       209    213       {ECO:0000244|PDB:3V4V}.
FT   STRAND      219    221       {ECO:0000244|PDB:3V4V}.
FT   STRAND      228    237       {ECO:0000244|PDB:3V4V}.
FT   HELIX       240    246       {ECO:0000244|PDB:3V4V}.
FT   STRAND      255    259       {ECO:0000244|PDB:3V4V}.
FT   HELIX       261    270       {ECO:0000244|PDB:3V4V}.
FT   HELIX       272    275       {ECO:0000244|PDB:3V4V}.
FT   STRAND      279    290       {ECO:0000244|PDB:3V4V}.
FT   HELIX       297    299       {ECO:0000244|PDB:3V4V}.
FT   TURN        300    302       {ECO:0000244|PDB:3V4V}.
FT   STRAND      317    319       {ECO:0000244|PDB:3V4V}.
FT   HELIX       320    324       {ECO:0000244|PDB:3V4V}.
FT   HELIX       330    339       {ECO:0000244|PDB:3V4V}.
FT   STRAND      342    348       {ECO:0000244|PDB:3V4V}.
FT   STRAND      350    352       {ECO:0000244|PDB:3V4V}.
FT   HELIX       353    360       {ECO:0000244|PDB:3V4V}.
FT   STRAND      367    370       {ECO:0000244|PDB:3V4V}.
FT   HELIX       378    390       {ECO:0000244|PDB:3V4V}.
FT   STRAND      393    396       {ECO:0000244|PDB:3V4V}.
FT   STRAND      404    408       {ECO:0000244|PDB:3V4V}.
FT   STRAND      413    415       {ECO:0000244|PDB:3V4V}.
FT   STRAND      423    428       {ECO:0000244|PDB:3V4V}.
FT   STRAND      436    445       {ECO:0000244|PDB:3V4V}.
FT   STRAND      454    460       {ECO:0000244|PDB:3V4V}.
FT   STRAND      465    469       {ECO:0000244|PDB:3V4V}.
FT   STRAND      777    786       {ECO:0000244|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
//
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