ITAE_MOUSE
ID ITAE_MOUSE Reviewed; 1167 AA.
AC Q60677; B1AUD5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Integrin alpha-E;
DE AltName: Full=Integrin alpha M290;
DE AltName: CD_antigen=CD103;
DE Contains:
DE RecName: Full=Integrin alpha-E light chain;
DE Contains:
DE RecName: Full=Integrin alpha-E heavy chain;
DE Flags: Precursor;
GN Name=Itgae;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AKR/J;
RX PubMed=7882170; DOI=10.1016/1074-7613(94)90070-1;
RA Smith T.J., Ducharme L.A., Shaw S.K., Parker C.M., Brenner M.B.,
RA Kilshaw P.J., Weis J.H.;
RT "Murine M290 integrin expression modulated by mast cell activation.";
RL Immunity 1:393-403(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Integrin alpha-E/beta-7 is a receptor for E-cadherin. It
CC mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell
CC monolayers. Mice expressing a null mutation of the alpha-E subunit gene
CC exhibit a marked reduction in the numbers of intraepithelial
CC lymphocytes in the gut and in the development of gut-associated
CC lymphoid aggregates, supporting a specific role for this integrin in
CC mediating retention of lymphocytes in the intestinal wall.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC is composed of a heavy and a light chains linked by a disulfide bond.
CC Alpha-E associates with beta-7.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
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DR EMBL; U12236; AAC52142.1; -; mRNA.
DR EMBL; AL670399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24995.1; -.
DR RefSeq; NP_032425.2; NM_008399.2.
DR AlphaFoldDB; Q60677; -.
DR SMR; Q60677; -.
DR BioGRID; 200821; 2.
DR ComplexPortal; CPX-3127; Integrin alphaE-beta7 complex.
DR STRING; 10090.ENSMUSP00000006101; -.
DR GlyGen; Q60677; 17 sites.
DR iPTMnet; Q60677; -.
DR PhosphoSitePlus; Q60677; -.
DR EPD; Q60677; -.
DR MaxQB; Q60677; -.
DR PaxDb; Q60677; -.
DR PRIDE; Q60677; -.
DR ProteomicsDB; 268893; -.
DR Antibodypedia; 10997; 1083 antibodies from 44 providers.
DR DNASU; 16407; -.
DR Ensembl; ENSMUST00000006101; ENSMUSP00000006101; ENSMUSG00000005947.
DR GeneID; 16407; -.
DR KEGG; mmu:16407; -.
DR UCSC; uc007jzy.2; mouse.
DR CTD; 3682; -.
DR MGI; MGI:1298377; Itgae.
DR VEuPathDB; HostDB:ENSMUSG00000005947; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000161532; -.
DR HOGENOM; CLU_004111_0_0_1; -.
DR InParanoid; Q60677; -.
DR OMA; QICVPTK; -.
DR OrthoDB; 743479at2759; -.
DR PhylomeDB; Q60677; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR BioGRID-ORCS; 16407; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Itgae; mouse.
DR PRO; PR:Q60677; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60677; protein.
DR Bgee; ENSMUSG00000005947; Expressed in seminiferous tubule of testis and 77 other tissues.
DR Genevisible; Q60677; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.130; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 4.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 2.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 6.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Integrin; Magnesium; Membrane; Metal-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..1167
FT /note="Integrin alpha-E"
FT /id="PRO_0000016286"
FT CHAIN 20..181
FT /note="Integrin alpha-E light chain"
FT /id="PRO_0000016287"
FT CHAIN 183..1167
FT /note="Integrin alpha-E heavy chain"
FT /id="PRO_0000016288"
FT TOPO_DOM 20..1114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1115..1137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1138..1167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 27..81
FT /note="FG-GAP 1"
FT REPEAT 84..142
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 193..382
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 383..435
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 438..491
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 492..552
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 555..619
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 623..683
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 149..192
FT /note="X-domain (extra domain)"
FT REGION 163..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1140..1144
FT /note="GFFKR motif"
FT COMPBIAS 168..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 518
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 522
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 578
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 582
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 586
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 654
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 968
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1013
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1055
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1086
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..83
FT /evidence="ECO:0000250"
FT DISULFID 130..164
FT /evidence="ECO:0000250"
FT DISULFID 698..754
FT /evidence="ECO:0000250"
FT DISULFID 814..820
FT /evidence="ECO:0000250"
FT DISULFID 884..898
FT /evidence="ECO:0000250"
FT DISULFID 998..1023
FT /evidence="ECO:0000250"
FT DISULFID 1031..1047
FT /evidence="ECO:0000250"
FT CONFLICT 22
FT /note="L -> M (in Ref. 1; AAC52142)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="Q -> L (in Ref. 1; AAC52142)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> G (in Ref. 1; AAC52142)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="A -> R (in Ref. 1; AAC52142)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="H -> R (in Ref. 1; AAC52142)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="V -> I (in Ref. 1; AAC52142)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="K -> N (in Ref. 1; AAC52142)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="G -> V (in Ref. 1; AAC52142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1167 AA; 128906 MW; 7534783B341175E5 CRC64;
MKWLFHTLLC MASLKPQGAF NLDVDWAWVT ALQPGAPAVL SSLLHQDPSN NQTCLLVARR
SSNRNTAALY RCAISISPDE IACQPVEHIC MPKGRYQGVT LVGNHNGVLV CIQVQARKFR
SLNSELTGAC SLLTPNLDLQ AQAYFSDLEG FLDPGAHVDS GDYCRSKGGS TGEEKKSARR
RRTVEEEDEE EDGTEIAIVL DGSGSIEPSD FQKAKNFIST MMRNFYEKCF ECNFALVQYG
AVIQTEFDLQ ESRDINASLA KVQSIVQVKE VTKTASAMQH VLDNIFIPSR GSRKKALKVM
VVLTDGDIFG DPLNLTTVIN SPKMQGVVRF AIGVGDAFKN NNTYRELKLI ASDPKEAHTF
KVTNYSALDG LLSKLQQHIV HMEGTVGDAL QYQLAQTGFS AQILDKGQVL LGTVGAFNWS
GGALLYSTQN GRGCFLNQTA KEDSRTVQYS YLGYSLAVLH KAHGVSYVAG APRHKLRGAV
FELRKEDREE DAFVRRIEGE QMGSYFGSVL CPVDIDMDGT TDFLLVAAPF YHIRGEEGRV
YVYQVPEQDA SFSLAHTLSG HPGLTNSRFG FAMAAVGDIN QDKFTDVAIG APLEGFGAGD
GASYGSVYIY NGHSGGLYDS PSQQIRASSV ASGLHYFGMS VSGGLDFNGD GLADITVGSR
DSAVVLRSRP VVDLTVSMTF TPDALPMVFI GKMDVKLCFE VDSSGVASEP GLREMFLNFT
VDVDVTKQRQ RLQCEDSSGC QSCLRKWNGG SFLCEHFWLI STEELCEEDC FSNITIKVTY
EFQTSGGRRD YPNPTLDHYK EPSAIFQLPY EKDCKNKVFC IAEIQLTTNI SQQELVVGVT
KEVTMNISLT NSGEDSYMTN MALNYPRNLQ FKKIQKPVSP DVQCDDPKPV ASVLVMNCKI
GHPILKRSSV NVSVTWQLEE SVFPNRTADI TVTISNSNEK SLARETRSLQ FRHAFIAVLS
RPSVMYMNTS QSPSDHKEFF FNVHGENLFG AVFQLQICVP IKLQDFQIVR VKNLTKTQDH
TECTQSQEPA CGSDPVQHVK EWHSVVCAIT SNKENVTVAA EISVGHTKQL LRDVSELPIL
GEISFNKSLY EGLNAENHRT KITVIFLKEE ETRSLPLIIG SSIGGLLVLV VIIAILFKCG
FFKRKYQQLN LESTRRAQLK ADSLLQD