EIF3A_DROVI
ID EIF3A_DROVI Reviewed; 1138 AA.
AC B4M693;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
GN Name=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
GN Synonyms=eIF3-S10 {ECO:0000255|HAMAP-Rule:MF_03000}; ORFNames=GJ10729;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. The eIF-3 complex interacts with pix.
CC {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
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DR EMBL; CH940652; EDW59169.1; -; Genomic_DNA.
DR RefSeq; XP_002056057.1; XM_002056021.2.
DR AlphaFoldDB; B4M693; -.
DR SMR; B4M693; -.
DR STRING; 7244.FBpp0225146; -.
DR PRIDE; B4M693; -.
DR EnsemblMetazoa; FBtr0226654; FBpp0225146; FBgn0198006.
DR GeneID; 6633030; -.
DR KEGG; dvi:6633030; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; B4M693; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 152929at2759; -.
DR PhylomeDB; B4M693; -.
DR ChiTaRS; eIF3-S10; fly.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT CHAIN 1..1138
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366343"
FT DOMAIN 319..502
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 590..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..985
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 133726 MW; 612931610FD92632 CRC64;
MARYTQRPEN ALKRANEFIE VGKPLRALDT LQEVFRNKRW NYAYSETVIE PLMFKYLYLC
VELKKSHIAK EGLFQYRNMF QLVNVNSLEN VIRGYLKMAE EHTEAAQAQS SAAVAVLELD
DLDNIATPES ILMSAVCGED AQDRSDRTIL LPWVKFLWES YCQCLELLRV NTHCEALYHD
IARMAFQFCL KYNRKSEFRR LCDKLRKHLE DICKSSNQTT GVSINKVETQ QLCLDTRLYL
LDSAIQMELW QEAYKAIEDI HGLMAMSKKT PVPKTMANYY QKLAMVFSKA GNQLFHAAAL
LKLFQLTREL KKNLTKDDLQ RMAAHVLLAT LSIPLPSAHP EFDRFIEADK SPLEKAQKLA
VLLGLPQPPT RVSLIREVVR LNVPNLVSDE FRNLYNWLEV DFNPLNLCKR IQSIVDTIES
SETENTLLTP YIQSLKDVTI MRLIRQISQV YESIEFKRLL ELAPFCNIFE LEKLLVESVR
HNDMQIRIDH QRNSIYFGTD LTESQREYRP DGPTLQSMPS EQIRSQLVNM STVLTRAVSI
VYPNRERDQR AKLRTQMVQH YHEIKDREHQ RILQRQKIIE DRKEFIEKQN NAREEEEARR
HEEESRKAKL AEQKRLEQEQ EERERKRHEN EIQAIKEKSL KEKVQQISQT AHGKKMLSKL
DEEGIKKLDA EQIAMRESEE LQRERKELQS KLKSQEKKID YFERAKRIEE IPLFEKYLAE
KNVKDKEFWE ATEQTRIENA IAERKDAVSQ QDRLKRMYPD RDEYLEALKK ERASLYVEKL
KKFDIALAEE RKKRLADRVV RRREERRQAY LRAKEEERFR KEEEIRHARE AEERAAAEAR
RLEREAEDEK RRQQYEKQRA KEEEAERKIQ EDRERLAREV AVERERSEKE RDVWRPRADR
VERPSAAPAG GASEWRRNAP PTDRNERTDR GDRNDRNDRN DRNDRNDRND RNDRNDRPER
AERKENDGGA DSSWRVRREP ESQRGTGAGM DRSERGGGGA PSGRDDKWRR GGDRSERLGG
DRDRDSFRRN DGPRRDDDRG GFRRDDQPQR ETGSNWRDSP RQNDRDNRRT TGERRDVRGA
GPKEGGGGVS GGGAGGGGGN WRTAPSPREE KAPPKREQAQ DKENKAGDDG EWTSVKRR
