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P26010 (ITB7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin beta-7
Alternative name(s):
Gut homing receptor beta subunit
Gene names
Name:ITGB7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length798 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Integrin alpha-4/beta-7 (Peyer patches-specific homing receptor LPAM-1) is an adhesion molecule that mediates lymphocyte migration and homing to gut-associated lymphoid tissue (GALT). Integrin alpha-4/beta-7 interacts with the cell surface adhesion molecules MADCAM1 which is normally expressed by the vascular endothelium of the gastrointestinal tract. Interacts also with VCAM1 and fibronectin, an extracellular matrix component. It recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin. Interactions involves the tripeptide L-D-T in MADCAM1, and L-D-V in fibronectin. Binds to HIV-1 gp120, thereby allowing the virus to enter GALT, which is thought to be the major trigger of AIDS disease. Interaction would involve a tripeptide L-D-I in HIV-1 gp120. Integrin alpha-E/beta-7 (HML-1) is a receptor for E-cadherin.

Subunit structure

Heterodimer of an alpha and a beta subunit. Beta-7 associates with either alpha-4 or alpha-E. Integrin alpha-4/beta-7 interacts with MADCAM1, VCAM, fibronectin, and may also interact with HIV-1 gp120. Ref.6 Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in a variety of leukocyte lines.

Induction

Integrin alpha-E/beta-7 is induced by TGFB1. Ref.6

Domain

Domain I contains three cation-binding sites: the ligand-integrin-binding site (LIMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent to MIDAS site (ADMIDAS). In the absence of a ligand or in calcium-dependent binding, only ADMIDAS is occupied. In magnesium-dependent binding all three sites bind metal ions. LIMBS positively modify ligand binding whereas ADMIDAS negatively modify ligand binding.

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandMagnesium
Metal-binding
   Molecular functionHost cell receptor for virus entry
Integrin
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Traceable author statement Ref.3. Source: ProtInc

cell-matrix adhesion

Inferred from electronic annotation. Source: InterPro

extracellular matrix organization

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte migration

Inferred from electronic annotation. Source: Ensembl

multicellular organismal development

Inferred from electronic annotation. Source: InterPro

regulation of immune response

Traceable author statement. Source: Reactome

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integrin complex

Traceable author statement Ref.3. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FLNAP213336EBI-702932,EBI-350432

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P26010-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P26010-2)

The sequence of this isoform differs from the canonical sequence as follows:
     501-648: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.6 Ref.7
Chain20 – 798779Integrin beta-7
PRO_0000016352

Regions

Topological domain20 – 723704Extracellular Potential
Transmembrane724 – 74623Helical; Potential
Topological domain747 – 79852Cytoplasmic Potential
Domain150 – 389240VWFA
Repeat478 – 52649I
Repeat527 – 56539II
Repeat566 – 60439III
Repeat605 – 64036IV
Region478 – 640163Cysteine-rich tandem repeats

Sites

Metal binding1591Magnesium; MIDAS motif By similarity
Metal binding1611Magnesium; MIDAS motif By similarity
Metal binding1631Magnesium; MIDAS motif By similarity
Metal binding1661Magnesium or calcium; ADMIDAS motif By similarity
Metal binding1671Magnesium or calcium; ADMIDAS motif By similarity
Metal binding1981Magnesium; LIMBS motif By similarity
Metal binding2541Magnesium; LIMBS motif By similarity
Metal binding2561Magnesium; LIMBS motif By similarity
Metal binding2591Magnesium; LIMBS motif By similarity
Metal binding2891Magnesium; MIDAS motif By similarity

Amino acid modifications

Modified residue7781Phosphotyrosine; by Tyr-kinases By similarity
Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Potential
Glycosylation4341N-linked (GlcNAc...) Potential
Glycosylation4771N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation5901N-linked (GlcNAc...) Potential
Glycosylation6651N-linked (GlcNAc...) Potential
Glycosylation6741N-linked (GlcNAc...) Potential
Disulfide bond45 ↔ 476 By similarity
Disulfide bond51 ↔ 61 By similarity
Disulfide bond54 ↔ 91 By similarity
Disulfide bond64 ↔ 80 By similarity
Disulfide bond216 ↔ 223 By similarity
Disulfide bond271 ↔ 311 By similarity
Disulfide bond412 ↔ 428 By similarity
Disulfide bond448 ↔ 688 By similarity
Disulfide bond474 ↔ 478 By similarity
Disulfide bond488 ↔ 500 By similarity
Disulfide bond497 ↔ 537 By similarity
Disulfide bond502 ↔ 511 By similarity
Disulfide bond513 ↔ 527 By similarity
Disulfide bond543 ↔ 548 By similarity
Disulfide bond545 ↔ 574 By similarity
Disulfide bond550 ↔ 559 By similarity
Disulfide bond561 ↔ 566 By similarity
Disulfide bond580 ↔ 585 By similarity
Disulfide bond582 ↔ 613 By similarity
Disulfide bond587 ↔ 596 By similarity
Disulfide bond598 ↔ 605 By similarity
Disulfide bond619 ↔ 624 By similarity
Disulfide bond621 ↔ 666 By similarity
Disulfide bond626 ↔ 635 By similarity
Disulfide bond638 ↔ 641 By similarity
Disulfide bond645 ↔ 654 By similarity

Natural variations

Alternative sequence501 – 648148Missing in isoform Short.
VSP_002753
Natural variant6721H → Y.
Corresponds to variant rs11539433 [ dbSNP | Ensembl ].
VAR_049637

Experimental info

Mutagenesis1591D → A: Loss of integrin alpha-E/beta-7 binding to E-cadherin and of integrin alpha-4/beta-7 binding to MADCAM1. Ref.8
Sequence conflict341W → A AA sequence Ref.7

Secondary structure

....................................................................... 798
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: CBE275E0E9992385

FASTA79886,903
        10         20         30         40         50         60 
MVALPMVLVL LLVLSRGESE LDAKIPSTGD ATEWRNPHLS MLGSCQPAPS CQKCILSHPS 

        70         80         90        100        110        120 
CAWCKQLNFT ASGEAEARRC ARREELLARG CPLEELEEPR GQQEVLQDQP LSQGARGEGA 

       130        140        150        160        170        180 
TQLAPQRVRV TLRPGEPQQL QVRFLRAEGY PVDLYYLMDL SYSMKDDLER VRQLGHALLV 

       190        200        210        220        230        240 
RLQEVTHSVR IGFGSFVDKT VLPFVSTVPS KLRHPCPTRL ERCQSPFSFH HVLSLTGDAQ 

       250        260        270        280        290        300 
AFEREVGRQS VSGNLDSPEG GFDAILQAAL CQEQIGWRNV SRLLVFTSDD TFHTAGDGKL 

       310        320        330        340        350        360 
GGIFMPSDGH CHLDSNGLYS RSTEFDYPSV GQVAQALSAA NIQPIFAVTS AALPVYQELS 

       370        380        390        400        410        420 
KLIPKSAVGE LSEDSSNVVQ LIMDAYNSLS STVTLEHSSL PPGVHISYES QCEGPEKREG 

       430        440        450        460        470        480 
KAEDRGQCNH VRINQTVTFW VSLQATHCLP EPHLLRLRAL GFSEELIVEL HTLCDCNCSD 

       490        500        510        520        530        540 
TQPQAPHCSD GQGHLQCGVC SCAPGRLGRL CECSVAELSS PDLESGCRAP NGTGPLCSGK 

       550        560        570        580        590        600 
GHCQCGRCSC SGQSSGHLCE CDDASCERHE GILCGGFGRC QCGVCHCHAN RTGRACECSG 

       610        620        630        640        650        660 
DMDSCISPEG GLCSGHGRCK CNRCQCLDGY YGALCDQCPG CKTPCERHRD CAECGAFRTG 

       670        680        690        700        710        720 
PLATNCSTAC AHTNVTLALA PILDDGWCKE RTLDNQLFFF LVEDDARGTV VLRVRPQEKG 

       730        740        750        760        770        780 
ADHTQAIVLG CVGGIVAVGL GLVLAYRLSV EIYDRREYSR FEKEQQQLNW KQDSNPLYKS 

       790 
AITTTINPRF QEADSPTL 

« Hide

Isoform Short [UniParc].

Checksum: B247895C3772178D
Show »

FASTA65071,582

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of a novel beta 2-related integrin transcript from T lymphocytes: homology of integrin cysteine-rich repeats to domain III of laminin B chains."
Yuan Q., Jiang W.-M., Krissansen G.W., Watson J.D.
Int. Immunol. 2:1097-1108(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: T-cell.
[2]"Cloning and sequence analysis of a novel beta 2-related integrin transcript from T lymphocytes: homology of integrin cysteine-rich repeats to domain III of laminin B chains."
Yuan Q., Jiang W.-M., Krissansen G.W., Watson J.D.
Int. Immunol. 3:1373-1374(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Complete amino acid sequence of an integrin beta subunit (beta 7) identified in leukocytes."
Erle D.J., Rueegg C., Sheppard D., Pytela R.
J. Biol. Chem. 266:11009-11016(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Leukocyte.
[4]"The gene organization of the human beta 7 subunit, the common beta subunit of the leukocyte integrins HML-1 and LPAM-1."
Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D., Krissansen G.W.
Int. Immunol. 4:1031-1040(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Tissue: Colon.
[6]"A family of beta 7 integrins on human mucosal lymphocytes."
Parker C.M., Cepek K.L., Russell G.J., Shaw S.K., Posnett D.N., Schwarting R., Brenner M.B.
Proc. Natl. Acad. Sci. U.S.A. 89:1924-1928(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-36, INTERACTION WITH INTEGRIN ALPHA-4 AND INTEGRIN ALPHA-E, INDUCTION.
[7]"HML-1 antigen on mucosa-associated T cells, activated cells, and hairy leukemic cells is a new integrin containing the beta 7 subunit."
Micklem K.J., Dong Y., Willis A., Pulford K.A., Visser L., Duerkop H., Poppema S., Stein H., Mason D.Y.
Am. J. Pathol. 139:1297-1301(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-34.
Tissue: Leukemia.
[8]"The role of alpha and beta chains in ligand recognition by beta 7 integrins."
Higgins J.M.G., Cernadas M., Tan K., Irie A., Wang J.-H., Takada Y., Brenner M.B.
J. Biol. Chem. 275:25652-25664(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-159.
[9]"Integrins: bidirectional, allosteric signaling machines."
Hynes R.O.
Cell 110:673-687(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[10]"HIV-1 envelope protein binds to and signals through integrin alpha4beta7, the gut mucosal homing receptor for peripheral T cells."
Arthos J., Cicala C., Martinelli E., Macleod K., Van Ryk D., Wei D., Xiao Z., Veenstra T.D., Conrad T.P., Lempicki R.A., McLaughlin S., Pascuccio M., Gopaul R., McNally J., Cruz C.C., Censoplano N., Chung E., Reitano K.N. expand/collapse author list , Kottilil S., Goode D.J., Fauci A.S.
Nat. Immunol. 9:301-309(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 GP120.
[11]"The molecular basis of filamin binding to integrins and competition with talin."
Kiema T., Lad Y., Jiang P., Oxley C.L., Baldassarre M., Wegener K.L., Campbell I.D., Ylanne J., Calderwood D.A.
Mol. Cell 21:337-347(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 768-798.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68892 mRNA. Translation: AAA59184.1.
S80335 mRNA. Translation: AAB21332.1.
M62880 mRNA. Translation: AAA59185.1.
L23823 expand/collapse EMBL AC list , L23810, L23811, L23812, L23813, L23814, L23815, L23816, L23817, L23818, L23819, L23820, L23821, L23822 Genomic DNA. Translation: AAA36118.1.
S49378 expand/collapse EMBL AC list , S49364, S49365, S49366, S49367, S49368, S49369, S49370, S49371, S49373, S49374, S49375, S49376, S49377 Genomic DNA. Translation: AAB23688.1.
BC015916 mRNA. Translation: AAH15916.1.
PIRA40526.
RefSeqNP_000880.1. NM_000889.2.
XP_005268908.1. XM_005268851.1.
XP_005268909.1. XM_005268852.2.
UniGeneHs.654470.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BRQX-ray2.10C/D768-798[»]
3V4PX-ray3.15B/D20-512[»]
3V4VX-ray3.10B/D20-512[»]
ProteinModelPortalP26010.
SMRP26010. Positions 42-783.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109901. 5 interactions.
DIPDIP-34970N.
IntActP26010. 3 interactions.
MINTMINT-258650.
STRING9606.ENSP00000267082.

Chemistry

BindingDBP26010.
ChEMBLCHEMBL2095184.

PTM databases

PhosphoSiteP26010.

Polymorphism databases

DMDM124973.

Proteomic databases

PaxDbP26010.
PRIDEP26010.

Protocols and materials databases

DNASU3695.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267082; ENSP00000267082; ENSG00000139626. [P26010-1]
ENST00000338737; ENSP00000345501; ENSG00000139626. [P26010-2]
ENST00000422257; ENSP00000408741; ENSG00000139626. [P26010-1]
ENST00000550743; ENSP00000455374; ENSG00000139626. [P26010-2]
GeneID3695.
KEGGhsa:3695.
UCSCuc001scc.3. human. [P26010-1]

Organism-specific databases

CTD3695.
GeneCardsGC12M053585.
HGNCHGNC:6162. ITGB7.
HPAHPA042277.
MIM147559. gene.
neXtProtNX_P26010.
PharmGKBPA29961.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287997.
HOGENOMHOG000252936.
HOVERGENHBG006190.
InParanoidP26010.
KOK06590.
OMADHTQAIV.
OrthoDBEOG7T7GSB.
PhylomeDBP26010.
TreeFamTF105392.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.
SignaLinkP26010.

Gene expression databases

ArrayExpressP26010.
BgeeP26010.
CleanExHS_ITGB7.
GenevestigatorP26010.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR015812. Integrin_bsu.
IPR015437. Integrin_bsu-7.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]
PANTHERPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF27. PTHR10082:SF27. 1 hit.
PfamPF08725. Integrin_b_cyt. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFPIRSF002512. Integrin_B. 1 hit.
PRINTSPR01186. INTEGRINB.
SMARTSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITGB7. human.
EvolutionaryTraceP26010.
GeneWikiITGB7.
GenomeRNAi3695.
NextBio14483.
PROP26010.
SOURCESearch...

Entry information

Entry nameITB7_HUMAN
AccessionPrimary (citable) accession number: P26010
Secondary accession number(s): Q9UCP7, Q9UCS7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM