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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
 
 
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