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Reviewed, UniProtKB/Swiss-Prot P38570 (ITAE_HUMAN)

Last modified June 16, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Integrin alpha-E
Alternative name(s):
    Mucosal lymphocyte 1 antigen
    HML-1 antigen
    Integrin alpha-IEL
    CD_antigen=CD103
Cleaved into the following 2 chains:
    1- Recommended name:
            Integrin alpha-E light chain
    2- Recommended name:
            Integrin alpha-E heavy chain
Gene names
Name: ITGAE
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1179 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-E/beta-7 is a receptor for E-cadherin. It mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell monolayers.

Subunit structure

Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of an heavy and a light chains linked by a disulfide bond. Alpha-E associates with beta-7.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed on a subclass of T-lymphocytes known as intra-epithelial lymphocytes which are located between mucosal epithelial cells.

Induction

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

Domain

The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.

Sequence similarities

Belongs to the integrin alpha chain family.

Contains 5 FG-GAP repeats.

Contains 1 VWFA domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
   LigandCalcium
Magnesium
   Molecular functionIntegrin
Receptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegrin complex Ref.1

Traceable author statement. Source: ProtInc

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.1
Chain19 – 11791161Integrin alpha-E
PRO_0000016283
Chain19 – 177159Integrin alpha-E light chain
PRO_0000016284
Chain179 – 1177999Integrin alpha-E heavy chain
PRO_0000016285

Regions

Topological domain19 – 11241106Extracellular Potential
Transmembrane1125 – 114723 Potential
Topological domain1148 – 117932Cytoplasmic Potential
Domain200 – 391192VWFA
Repeat401 – 45656FG-GAP 1
Repeat457 – 50650FG-GAP 2
Repeat510 – 57162FG-GAP 3
Repeat573 – 63866FG-GAP 4
Repeat641 – 69353FG-GAP 5
Calcium binding522 – 5309 Potential
Calcium binding586 – 5949 Potential
Calcium binding654 – 6629 Potential
Region145 – 19955X-domain (extra domain)
Motif1150 – 11545GFFKR motif
Compositional bias181 – 19818Glu-rich (acidic)

Amino acid modifications

Glycosylation491N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation7261N-linked (GlcNAc...) Potential
Glycosylation7821N-linked (GlcNAc...) Potential
Glycosylation8571N-linked (GlcNAc...) Potential
Glycosylation9341N-linked (GlcNAc...) Potential
Glycosylation9541N-linked (GlcNAc...) Potential
Glycosylation10651N-linked (GlcNAc...) Potential
Glycosylation10961N-linked (GlcNAc...) Potential
Disulfide bond70 ↔ 79 By similarity
Disulfide bond126 ↔ 159 By similarity
Disulfide bond706 ↔ 762 By similarity
Disulfide bond823 ↔ 829 By similarity
Disulfide bond893 ↔ 907 By similarity
Disulfide bond1008 ↔ 1033 By similarity
Disulfide bond1041 ↔ 1057 By similarity

Natural variations

Natural variant3601D → E
VAR_008884
Natural variant4771I → V: dbSNP rs220479. Ref.1 Ref.4
VAR_054889
Natural variant4821R → Q: dbSNP rs2272606. Ref.1 Ref.4
VAR_054890
Natural variant8921Q → H: dbSNP rs3744679.
VAR_020037
Natural variant9501R → W: dbSNP rs1716. Ref.5
VAR_034025
Natural variant10191V → A: dbSNP rs2976230. Ref.1 Ref.4
VAR_054891
Natural variant10411C → S
VAR_008885

Experimental info

Mutagenesis2081D → A: Loss of E-cadherin binding. Ref.7
Mutagenesis3161F → A: Loss of E-cadherin binding. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P38570-1 [UniParc].

Last modified April 14, 2009. Version 3.
Checksum: 6645F8FFF9A0F045

FASTA1,179130,159
        10         20         30         40         50         60 
MWLFHTLLCI ASLALLAAFN VDVARPWLTP KGGAPFVLSS LLHQDPSTNQ TWLLVTSPRT 

        70         80         90        100        110        120 
KRTPGPLHRC SLVQDEILCH PVEHVPIPKG RHRGVTVVRS HHGVLICIQV LVRRPHSLSS 

       130        140        150        160        170        180 
ELTGTCSLLG PDLRPQAQAN FFDLENLLDP DARVDTGDCY SNKEGGGEDD VNTARQRRAL 

       190        200        210        220        230        240 
EKEEEEDKEE EEDEEEEEAG TEIAIILDGS GSIDPPDFQR AKDFISNMMR NFYEKCFECN 

       250        260        270        280        290        300 
FALVQYGGVI QTEFDLRDSQ DVMASLARVQ NITQVGSVTK TASAMQHVLD SIFTSSHGSR 

       310        320        330        340        350        360 
RKASKVMVVL TDGGIFEDPL NLTTVINSPK MQGVERFAIG VGEEFKSART ARELNLIASD 

       370        380        390        400        410        420 
PDETHAFKVT NYMALDGLLS KLRYNIISME GTVGDALHYQ LAQIGFSAQI LDERQVLLGA 

       430        440        450        460        470        480 
VGAFDWSGGA LLYDTRSRRG RFLNQTAAAA ADAEAAQYSY LGYAVAVLHK TCSLSYIAGA 

       490        500        510        520        530        540 
PRYKHHGAVF ELQKEGREAS FLPVLEGEQM GSYFGSELCP VDIDMDGSTD FLLVAAPFYH 

       550        560        570        580        590        600 
VHGEEGRVYV YRLSEQDGSF SLARILSGHP GFTNARFGFA MAAMGDLSQD KLTDVAIGAP 

       610        620        630        640        650        660 
LEGFGADDGA SFGSVYIYNG HWDGLSASPS QRIRASTVAP GLQYFGMSMA GGFDISGDGL 

       670        680        690        700        710        720 
ADITVGTLGQ AVVFRSRPVV RLKVSMAFTP SALPIGFNGV VNVRLCFEIS SVTTASESGL 

       730        740        750        760        770        780 
REALLNFTLD VDVGKQRRRL QCSDVRSCLG CLREWSSGSQ LCEDLLLMPT EGELCEEDCF 

       790        800        810        820        830        840 
SNASVKVSYQ LQTPEGQTDH PQPILDRYTE PFAIFQLPYE KACKNKLFCV AELQLATTVS 

       850        860        870        880        890        900 
QQELVVGLTK ELTLNINLTN SGEDSYMTSM ALNYPRNLQL KRMQKPPSPN IQCDDPQPVA 

       910        920        930        940        950        960 
SVLIMNCRIG HPVLKRSSAH VSVVWQLEEN AFPNRTADIT VTVTNSNERR SLANETHTLQ 

       970        980        990       1000       1010       1020 
FRHGFVAVLS KPSIMYVNTG QGLSHHKEFL FHVHGENLFG AEYQLQICVP TKLRGLQVVA 

      1030       1040       1050       1060       1070       1080 
VKKLTRTQAS TVCTWSQERA CAYSSVQHVE EWHSVSCVIA SDKENVTVAA EISWDHSEEL 

      1090       1100       1110       1120       1130       1140 
LKDVTELQIL GEISFNKSLY EGLNAENHRT KITVVFLKDE KYHSLPIIIK GSVGGLLVLI 

      1150       1160       1170 
VILVILFKCG FFKRKYQQLN LESIRKAQLK SENLLEEEN 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the human mucosal lymphocyte integrin alpha E subunit. Unusual structure and restricted RNA distribution."
Shaw S.K., Cepek K.L., Murphy E.A., Russell G.J., Brenner M.B., Parker C.M.
J. Biol. Chem. 269:6016-6025(1994) [PubMed: 8119947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-38 AND 179-188, VARIANTS VAL-477; GLN-482 AND ALA-1019.
Tissue: Leukemia and Lymphocyte.
[2]Parker C.M.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 88-114.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-477; GLN-482 AND ALA-1019.
[5]"The genomic region encompassing the nephropathic cystinosis gene (CTNS): complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion."
Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V.B., McDowell G., Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A., Green E.D.
Genome Res. 10:165-173(2000) [PubMed: 10673275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-1179, VARIANT TRP-950.
Tissue: Fetal kidney.
[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: 1542691] [Abstract]
Cited for: INTERACTION WITH INTEGRIN BETA-7, INDUCTION.
[7]"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: 10837471] [Abstract]
Cited for: MUTAGENESIS OF ASP-208 AND PHE-316.
+Additional computationally mapped references.

Cross-references

Sequence databases

L25851 mRNA. Translation: AAB59359.2.
AC116914 Genomic DNA. No translation available.
BC113436 mRNA. Translation: AAI13437.1.
BC117207 mRNA. Translation: AAI17208.1.
AF168787 Genomic DNA. Translation: AAF43107.1.
IPIIPI00007205.
PIRA53213.
RefSeqNP_002199.3.
UniGeneHs.513867

3D structure databases

HSSPHSSP built from PDB template 1BHQ based on UniProtKB P11215.
ModBaseSearch...

Protein-protein interaction databases

IntActP38570. 1 interaction.

Proteomic databases

PRIDEP38570.

Genome annotation databases

EnsemblENSG00000083457. Homo sapiens. [Contig view]
GeneID3682.
KEGGhsa:3682.

Organism-specific databases

GeneCardsGC17M003564.
H-InvDBHIX0013432.
HGNCHGNC:6147. ITGAE.
MIM604682. gene.
PharmGKBPA29947.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP38570.
HOVERGENP38570.
OMAP38570. ELTGTCS.

Enzyme and pathway databases

ReactomeREACT_13552. Integrin cell surface interactions.

Gene expression databases

ArrayExpressP38570.
BgeeP38570.
CleanExHS_ITGAE.
GermOnlineENSG00000083457. Homo sapiens.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR013513. Integrin_alpha_C.
IPR018184. Integrin_alpha_C_CS.
IPR002035. VWF_A.
[Graphical view]
PfamPF01839. FG-GAP. 2 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PRINTSPR01185. INTEGRINA.
SMARTSM00191. Int_alpha. 4 hits.
SM00327. VWA. 1 hit.
[Graphical view]
PROSITEPS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio14411.
SOURCESearch...

Entry information

Entry nameITAE_HUMAN
AccessionPrimary (citable) accession number: P38570
Secondary accession number(s): Q17RS6, Q9NZU9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 14, 2009
Last modified: June 16, 2009
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents