EIF3A_DROSE
ID EIF3A_DROSE Reviewed; 1141 AA.
AC B4I3P3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 61.
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=GM10701;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDW54836.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH480821; EDW54836.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002038299.1; XM_002038263.1.
DR AlphaFoldDB; B4I3P3; -.
DR SMR; B4I3P3; -.
DR STRING; 7238.B4I3P3; -.
DR PRIDE; B4I3P3; -.
DR ChiTaRS; eIF3-S10; fly.
DR Proteomes; UP000001292; 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 PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1141
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366341"
FT DOMAIN 319..501
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 588..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1089
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
SQ SEQUENCE 1141 AA; 133915 MW; 3283D35FB40B1157 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 HGLMALSKKT PVPKTMANYY QKLAMVFSKA GNQLFHAAAL
LKLFQLTREL KKNLTKDDLQ RMAAHVLLAT LSIPLPSAHP EFDRFIEADK SPLEKAQKLA
VLLGLPQPPT RVSLIREVVR LNVPQLVSED FRNLYNWLEV DFNPLNLCKR IQSIVDFIEN
GPENALLTPY IQSLKDVTIM RLIRQISQVY ESIKFQRLLQ LASFCNIFEL EKLLVESVRH
NDMQIRIDHQ KNSIYFGTDL TESQREYRPD GPALQSMPSE QIRSQLVNMS TVLTRAVSIV
YPNRERDQRA KLRNQMVSQY HEIKDREHQR ILQRQKIIED RKEYIEKQNN AREEEEARRQ
EEESRKAKLA EQKRLEQEQE ERERKRHQNE IQAIREKSLK EKVQQISQTA HGKKMLSKLD
EEGIKKLDAE QIAKRESEEL QREAKELQSK LKSQEKKIDY FERAKRLEEI PLFEKYLAEK
QVKDKEFWEA TEKTRIENAI AERMDAVAQQ ERLKRMYPDR DEFLEALKKE RASLYVEKLK
KFEAALEAER KKRLADRIVR RREERRQAFL REKEEERLRK EEEIRLAQAA EERAAAEARR
LEREAEDEKR RAQYEKQRAK EEEAERKIKE DRDRLSRELA SERERTEKER DTWRPRGGDR
PSASAGGSSE WRRAAPAVSE RNDRGGERIE RGGDRVERGG ERIERGGERI ERGGDRDRKD
NEGADSSWRV RREPDTQRAA APKDSGAPQS RDDKWRRGGE RDRDFRNDGA RRDRDDGPRR
DRDDGPRRDR DDERGGFRRN DGPRRTDEPQ RESGGNWRDA PRHADRENRR PAGERRDRDV
RETRGDQRGS APKEAASGGG GGNWRNAPAT REEKPAAKRD QAQEKENKAG DDGEWTSVKR
R
