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Database: UniProt
Entry: A0A2K5VBE9_MACFA
LinkDB: A0A2K5VBE9_MACFA
Original site: A0A2K5VBE9_MACFA 
ID   A0A2K5VBE9_MACFA        Unreviewed;      1195 AA.
AC   A0A2K5VBE9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Integrin subunit alpha E {ECO:0000313|Ensembl:ENSMFAP00000022052.2};
GN   Name=ITGAE {ECO:0000313|Ensembl:ENSMFAP00000022052.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000022052.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000022052.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000022052.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC       {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
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DR   AlphaFoldDB; A0A2K5VBE9; -.
DR   STRING; 9541.ENSMFAP00000022052; -.
DR   Ensembl; ENSMFAT00000030179.2; ENSMFAP00000022052.2; ENSMFAG00000035926.2.
DR   VEuPathDB; HostDB:ENSMFAG00000035926; -.
DR   GeneTree; ENSGT00940000161532; -.
DR   Proteomes; UP000233100; Chromosome 16.
DR   Bgee; ENSMFAG00000035926; Expressed in thymus and 12 other cell types or tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd01469; vWA_integrins_alpha_subunit; 1.
DR   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR   Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF79; INTEGRIN ALPHA-E; 1.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF00357; Integrin_alpha; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00191; Int_alpha; 4.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 2.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS51470; FG_GAP; 3.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   ECO:0000256|RuleBase:RU003762};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003762};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003762}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..1195
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030051425"
FT   TRANSMEM        1143..1163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   DOMAIN          221..401
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REPEAT          516..576
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          579..643
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          647..707
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REGION          177..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..219
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1195 AA;  131385 MW;  6FED405385CCD1AF CRC64;
     MCLTCLGSHA AASAPAPARM WLVHTLLCMA SLAPLAAFNV DVARPWLTPK GGAPFVLSSL
     LHQDPGTNHT WLLVTSPRTE RTPVPLHRCS LVQDEILCHS VEHVPIPKGR HRGVTVARSH
     HGVLICIQVL ARRPYSLSSE FTGTCGLLGP DLRPQAQANF FDLENLLDPD ARVDTGDCYS
     NKEGSRGEDV NTARRRRALE KEEEEEDEEE EEDEEGEAGT EIAIILDGSG SIDPPDFQRA
     KDFISNMMRN FYEKCFECNF ALVQYGGVIQ TEFDLRDSQD VMASLAKVQN ITQVGSVTKT
     ASAMQHVLDN IFTSSHGSRR KASKVMVVLT DGGIFEDPLD LTTVINSPKM HGVERFAIGV
     GEEFKSARTE RELNLIASDP DETHAFKVTN YMALDGLLSK LRYNIISMEG TVGDALHYQL
     AQIGFSAQIL DEVLLGAVGA FDWSGGALLY NTRSRRGRFL NQTAAAADGE AAQYSYLGYA
     VAVLHKTCSV SYVAGAPRYK HHGAVFELQK EGTETSFLPV LEGEQMGSYF GSELCPVDID
     MDGTTDFLLV AAPFYHVHGE EGRVYVYRLS EQDGSFSLAR ILSGHPGFAS ARFGFAMAAV
     GDISQDKLTD VAIGAPLEGF GAGDGASFGS VYIYNGHWDG LSASPSQRIR ASAVAPGLQY
     FGMSVAGGFD ISGDGLADIT VGTLGRAVVF RSRPVVRLEV SMAFTPSALP IGFNGVVNVR
     LCFEISSVTT VSASGLRGAF LNFTLDVDVG KERKRLQCSD GRSCLGCLRE WSSGSRLCED
     LLFVPTEGEP REEDCFSNAT VKVGYQLQTP EGQTDHPQPI LDRYAETFAI FQLPYEKACK
     NKLFCVAELQ LATTVSQQEL VVGLTKELTL NISLTNSGED SYMTSMALNY PRNLQFKRMQ
     KPPSPNIQCD DPQPAASVLV MTCRIGHPVL RRSSAHVSVV WQLEENAFPN RTADITVTVT
     NSNERRSVAE ETHTLQFRHG FVAVLSKPSI MYVHTGQVLS HHKEFVFHIH GENLFGAEYQ
     LRICVPTKLR GLQIVTVKNL TRTQAFTVCT WSQERACGFI PVQHVEEWHS VSCVIASDNE
     NVTVAAEISV DHSEELLKDV TELQILGEIS FNKSLYEGLN AENHRTKITV VFLKDEKYHS
     LPVIIKGSIG GLLVLIVILV ILFKCGFFKR KYQQLNLENI RKAQLKSETL LEEEN
//
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