EIF3A_DROAN
ID EIF3A_DROAN Reviewed; 1140 AA.
AC B3LY22;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=GF16808;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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; CH902617; EDV42878.1; -; Genomic_DNA.
DR RefSeq; XP_001954317.1; XM_001954281.2.
DR AlphaFoldDB; B3LY22; -.
DR SMR; B3LY22; -.
DR STRING; 7217.FBpp0120000; -.
DR EnsemblMetazoa; FBtr0121508; FBpp0120000; FBgn0093829.
DR GeneID; 6499602; -.
DR KEGG; dan:6499602; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_1_0_1; -.
DR InParanoid; B3LY22; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 152929at2759; -.
DR PhylomeDB; B3LY22; -.
DR ChiTaRS; eIF3-S10; fly.
DR Proteomes; UP000007801; 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..1140
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366334"
FT DOMAIN 319..502
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 589..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 133351 MW; 986BC86ABB83A360 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 FRNLYNWLEI DFNPLNLCKR IQSIVDIIEG
GPAESNLLTP YIQSLKDVTI MRLIRQISQV YESIEFKRLL ELASFCNIFE LEKLLVESVR
HNDMQIRIDH QKNSIYFGTD LTESQREYRP DGPSLQSMPS EQIRSQLVNM STVLTRAVSI
VYPNRERDQR AKLRTQMVHH YHEIKDREHQ RILQRQKIIE DRKEYIEKQN NAREEEEARR
QEEESRKAKL AEQKRLEQEQ EERERKRHQN EIQAIREKSL KEKVQQISQT AHGKKMLSKL
DEEGIKKLDA EQIAKRENEE LQREAKELQS KLKSQEKKVD YFERAKRLEE IPLFEKYLAE
KQVKDKEFWE ATEKTRIENA IAERKDAVSQ QERLKRMYPD RDEYLDALKK ERASLYVEKL
KKFEIALEVE RKKRLADRIV RRREERRQAF LREKEEERLR KEEEIRLAQA AEERAAAEAR
RLEREAEDEK RRAQYEKQRA KEEEAERKIK EDRERLAREV AVERERSEKE RDTWRPRGGD
RPSAPAGGAG EWRRAAPPAG ERNDRGAERS ERGGDRNERG GDRIERGGDR IERGGERAER
GGDRDRKDDG GADSSWRVRR EPDSQRAAGA KDAGGAPASR DDKWRRGGDR ERDRDFRNDG
PRRDRDDRDD RDRGGFRRND GPRRNDEPQR ETGGNWRDAP RQSDRDNRRP GGERRDRDGR
DVRGDQRGPA SKEAGGGGGG GNWRTAPAPR DEKPAAKRDQ PQDKENKGGD DGEWTSVKRR
