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Protein

Integrin beta-7

Gene

ITGB7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi159Magnesium; MIDAS motifBy similarity1
Metal bindingi161Magnesium; MIDAS motifBy similarity1
Metal bindingi163Magnesium; MIDAS motifBy similarity1
Metal bindingi166Magnesium or calcium; ADMIDAS motifBy similarity1
Metal bindingi167Magnesium or calcium; ADMIDAS motifBy similarity1
Metal bindingi198Magnesium; LIMBS motifBy similarity1
Metal bindingi254Magnesium; LIMBS motifBy similarity1
Metal bindingi256Magnesium; LIMBS motifBy similarity1
Metal bindingi259Magnesium; LIMBS motifBy similarity1
Metal bindingi289Magnesium; MIDAS motifBy similarity1

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • signaling receptor activity Source: InterPro
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • cell adhesion Source: ProtInc
  • cell-matrix adhesion Source: UniProtKB
  • cell-matrix adhesion involved in ameboidal cell migration Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • heterotypic cell-cell adhesion Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • leukocyte tethering or rolling Source: UniProtKB
  • receptor clustering Source: UniProtKB
  • regulation of immune response Source: Reactome
  • substrate adhesion-dependent cell spreading Source: UniProtKB
  • T cell migration Source: Ensembl

Keywordsi

Molecular functionHost cell receptor for virus entry, Integrin, Receptor
Biological processCell adhesion
LigandMagnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-HSA-216083 Integrin cell surface interactions
SignaLinkiP26010
SIGNORiP26010

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin beta-7
Alternative name(s):
Gut homing receptor beta subunit
Gene namesi
Name:ITGB7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000139626.15
HGNCiHGNC:6162 ITGB7
MIMi147559 gene
neXtProtiNX_P26010

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 723ExtracellularSequence analysisAdd BLAST704
Transmembranei724 – 746HelicalSequence analysisAdd BLAST23
Topological domaini747 – 798CytoplasmicSequence analysisAdd BLAST52

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi159D → A: Loss of integrin alpha-E/beta-7 binding to E-cadherin and of integrin alpha-4/beta-7 binding to MADCAM1. 1 Publication1

Organism-specific databases

DisGeNETi3695
OpenTargetsiENSG00000139626
PharmGKBiPA29961

Chemistry databases

ChEMBLiCHEMBL2979
DrugBankiDB05802 MLN-02
DB05122 R1295
DB09033 Vedolizumab
GuidetoPHARMACOLOGYi2461

Polymorphism and mutation databases

BioMutaiITGB7
DMDMi124973

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
ChainiPRO_000001635220 – 798Integrin beta-7Add BLAST779

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi45 ↔ 476By similarity
Disulfide bondi51 ↔ 61By similarity
Disulfide bondi54 ↔ 91By similarity
Disulfide bondi64 ↔ 80By similarity
Glycosylationi68N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi216 ↔ 223By similarity
Disulfide bondi271 ↔ 311By similarity
Glycosylationi279N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi412 ↔ 428By similarity
Glycosylationi434N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi448 ↔ 688By similarity
Disulfide bondi474 ↔ 478By similarity
Glycosylationi477N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi488 ↔ 500By similarity
Disulfide bondi497 ↔ 537By similarity
Disulfide bondi502 ↔ 511By similarity
Disulfide bondi513 ↔ 527By similarity
Glycosylationi531N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi543 ↔ 548By similarity
Disulfide bondi545 ↔ 574By similarity
Disulfide bondi550 ↔ 559By similarity
Disulfide bondi561 ↔ 566By similarity
Disulfide bondi580 ↔ 585By similarity
Disulfide bondi582 ↔ 613By similarity
Disulfide bondi587 ↔ 596By similarity
Glycosylationi590N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi598 ↔ 605By similarity
Disulfide bondi619 ↔ 624By similarity
Disulfide bondi621 ↔ 666By similarity
Disulfide bondi626 ↔ 635By similarity
Disulfide bondi638 ↔ 641By similarity
Disulfide bondi645 ↔ 654By similarity
Glycosylationi665N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi674N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei778Phosphotyrosine; by Tyr-kinasesBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP26010
PaxDbiP26010
PeptideAtlasiP26010
PRIDEiP26010

PTM databases

iPTMnetiP26010
PhosphoSitePlusiP26010

Expressioni

Tissue specificityi

Expressed in a variety of leukocyte lines.

Inductioni

Integrin alpha-E/beta-7 is induced by TGFB1.1 Publication

Gene expression databases

BgeeiENSG00000139626
CleanExiHS_ITGB7
ExpressionAtlasiP26010 baseline and differential
GenevisibleiP26010 HS

Organism-specific databases

HPAiHPA042277

Interactioni

Subunit structurei

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, VCAM1, fibronectin, and may also interact with HIV-1 gp120. Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) (PubMed:19828450).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109901, 6 interactors
CORUMiP26010
DIPiDIP-34970N
ELMiP26010
IntActiP26010, 3 interactors
MINTiP26010
STRINGi9606.ENSP00000267082

Chemistry databases

BindingDBiP26010

Structurei

Secondary structure

1798
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi102 – 105Combined sources4
Turni114 – 116Combined sources3
Beta strandi117 – 119Combined sources3
Beta strandi127 – 131Combined sources5
Beta strandi138 – 145Combined sources8
Beta strandi152 – 159Combined sources8
Helixi162 – 164Combined sources3
Helixi165 – 173Combined sources9
Helixi176 – 182Combined sources7
Turni183 – 185Combined sources3
Beta strandi189 – 196Combined sources8
Turni202 – 204Combined sources3
Helixi209 – 213Combined sources5
Beta strandi219 – 221Combined sources3
Beta strandi228 – 237Combined sources10
Helixi240 – 246Combined sources7
Beta strandi255 – 259Combined sources5
Helixi261 – 270Combined sources10
Helixi272 – 275Combined sources4
Beta strandi279 – 290Combined sources12
Helixi297 – 299Combined sources3
Turni300 – 302Combined sources3
Beta strandi317 – 319Combined sources3
Helixi320 – 324Combined sources5
Helixi330 – 339Combined sources10
Beta strandi342 – 348Combined sources7
Beta strandi350 – 352Combined sources3
Helixi353 – 360Combined sources8
Beta strandi367 – 370Combined sources4
Helixi378 – 390Combined sources13
Beta strandi393 – 396Combined sources4
Beta strandi404 – 408Combined sources5
Beta strandi413 – 415Combined sources3
Beta strandi423 – 428Combined sources6
Beta strandi436 – 445Combined sources10
Beta strandi454 – 460Combined sources7
Beta strandi465 – 469Combined sources5
Beta strandi777 – 786Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BRQX-ray2.10C/D768-798[»]
3V4PX-ray3.15B/D20-512[»]
3V4VX-ray3.10B/D20-512[»]
ProteinModelPortaliP26010
SMRiP26010
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26010

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini150 – 389VWFAAdd BLAST240
Repeati478 – 526IAdd BLAST49
Repeati527 – 565IIAdd BLAST39
Repeati566 – 604IIIAdd BLAST39
Repeati605 – 640IVAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni478 – 640Cysteine-rich tandem repeatsAdd BLAST163

Domaini

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 similaritiesi

Belongs to the integrin beta chain family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1226 Eukaryota
ENOG410XP60 LUCA
GeneTreeiENSGT00760000119064
HOGENOMiHOG000252936
HOVERGENiHBG006190
InParanoidiP26010
KOiK06590
OMAiTLCDCNC
OrthoDBiEOG091G029W
PhylomeDBiP26010
TreeFamiTF105392

Family and domain databases

Gene3Di3.40.50.410, 1 hit
InterProiView protein in InterPro
IPR013111 EGF_extracell
IPR033760 Integrin_beta_N
IPR015812 Integrin_bsu
IPR015437 Integrin_bsu-7
IPR014836 Integrin_bsu_cyt_dom
IPR012896 Integrin_bsu_tail
IPR036349 Integrin_bsu_tail_dom_sf
IPR002369 Integrin_bsu_VWA
IPR032695 Integrin_dom_sf
IPR016201 PSI
IPR036465 vWFA_dom_sf
PANTHERiPTHR10082 PTHR10082, 1 hit
PTHR10082:SF36 PTHR10082:SF36, 1 hit
PfamiView protein in Pfam
PF07974 EGF_2, 1 hit
PF08725 Integrin_b_cyt, 1 hit
PF00362 Integrin_beta, 1 hit
PF17205 PSI_integrin, 1 hit
PIRSFiPIRSF002512 Integrin_B, 1 hit
PRINTSiPR01186 INTEGRINB
SMARTiView protein in SMART
SM00187 INB, 1 hit
SM01241 Integrin_b_cyt, 1 hit
SM01242 Integrin_B_tail, 1 hit
SM00423 PSI, 1 hit
SUPFAMiSSF53300 SSF53300, 1 hit
SSF69179 SSF69179, 1 hit
SSF69687 SSF69687, 1 hit
PROSITEiView protein in PROSITE
PS00022 EGF_1, 4 hits
PS01186 EGF_2, 1 hit
PS00243 INTEGRIN_BETA, 3 hits

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P26010-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVALPMVLVL LLVLSRGESE LDAKIPSTGD ATEWRNPHLS MLGSCQPAPS
60 70 80 90 100
CQKCILSHPS CAWCKQLNFT ASGEAEARRC ARREELLARG CPLEELEEPR
110 120 130 140 150
GQQEVLQDQP LSQGARGEGA TQLAPQRVRV TLRPGEPQQL QVRFLRAEGY
160 170 180 190 200
PVDLYYLMDL SYSMKDDLER VRQLGHALLV RLQEVTHSVR IGFGSFVDKT
210 220 230 240 250
VLPFVSTVPS KLRHPCPTRL ERCQSPFSFH HVLSLTGDAQ AFEREVGRQS
260 270 280 290 300
VSGNLDSPEG GFDAILQAAL CQEQIGWRNV SRLLVFTSDD TFHTAGDGKL
310 320 330 340 350
GGIFMPSDGH CHLDSNGLYS RSTEFDYPSV GQVAQALSAA NIQPIFAVTS
360 370 380 390 400
AALPVYQELS KLIPKSAVGE LSEDSSNVVQ LIMDAYNSLS STVTLEHSSL
410 420 430 440 450
PPGVHISYES QCEGPEKREG KAEDRGQCNH VRINQTVTFW VSLQATHCLP
460 470 480 490 500
EPHLLRLRAL GFSEELIVEL HTLCDCNCSD TQPQAPHCSD GQGHLQCGVC
510 520 530 540 550
SCAPGRLGRL CECSVAELSS PDLESGCRAP NGTGPLCSGK GHCQCGRCSC
560 570 580 590 600
SGQSSGHLCE CDDASCERHE GILCGGFGRC QCGVCHCHAN RTGRACECSG
610 620 630 640 650
DMDSCISPEG GLCSGHGRCK CNRCQCLDGY YGALCDQCPG CKTPCERHRD
660 670 680 690 700
CAECGAFRTG PLATNCSTAC AHTNVTLALA PILDDGWCKE RTLDNQLFFF
710 720 730 740 750
LVEDDARGTV VLRVRPQEKG ADHTQAIVLG CVGGIVAVGL GLVLAYRLSV
760 770 780 790
EIYDRREYSR FEKEQQQLNW KQDSNPLYKS AITTTINPRF QEADSPTL
Length:798
Mass (Da):86,903
Last modified:May 1, 1992 - v1
Checksum:iCBE275E0E9992385
GO
Isoform Short (identifier: P26010-2) [UniParc]FASTAAdd to basket

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

Show »
Length:650
Mass (Da):71,582
Checksum:iB247895C3772178D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34W → A AA sequence (PubMed:1750505).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049637672H → Y. Corresponds to variant dbSNP:rs11539433Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002753501 – 648Missing in isoform Short. 1 PublicationAdd BLAST148

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68892 mRNA Translation: AAA59184.1
S80335 mRNA Translation: AAB21332.1
M62880 mRNA Translation: AAA59185.1
L23823
, L23810, L23811, L23812, L23813, L23814, L23815, L23816, L23817, L23818, L23819, L23820, L23821, L23822 Genomic DNA Translation: AAA36118.1
S49378
, S49364, S49365, S49366, S49367, S49368, S49369, S49370, S49371, S49373, S49374, S49375, S49376, S49377 Genomic DNA Translation: AAB23688.1
BC015916 mRNA Translation: AAH15916.1
CCDSiCCDS8849.1 [P26010-1]
PIRiA40526
RefSeqiNP_000880.1, NM_000889.2 [P26010-1]
XP_005268908.1, XM_005268851.3 [P26010-1]
XP_005268909.1, XM_005268852.4 [P26010-1]
UniGeneiHs.654470

Genome annotation databases

EnsembliENST00000267082; ENSP00000267082; ENSG00000139626 [P26010-1]
ENST00000422257; ENSP00000408741; ENSG00000139626 [P26010-1]
ENST00000550743; ENSP00000455374; ENSG00000139626 [P26010-2]
GeneIDi3695
KEGGihsa:3695
UCSCiuc001scc.4 human [P26010-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiITB7_HUMAN
AccessioniPrimary (citable) accession number: P26010
Secondary accession number(s): Q9UCP7, Q9UCS7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 23, 2018
This is version 185 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health