EIF3A_DROPE
ID EIF3A_DROPE Reviewed; 1173 AA.
AC B4GDX4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 56.
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=GL22350;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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=EDW34635.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EDW34635.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; CH479182; EDW34635.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002017535.1; XM_002017499.1.
DR AlphaFoldDB; B4GDX4; -.
DR SMR; B4GDX4; -.
DR eggNOG; KOG2072; Eukaryota.
DR ChiTaRS; eIF3-S10; fly.
DR Proteomes; UP000008744; 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..1173
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366339"
FT DOMAIN 319..502
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 589..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 136774 MW; 0388E3613CA4CA99 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 IQSIVDIIET
GPTETNLLSP YIQSLKDVTI MRLIRQISQV YESIEFKRLL ELATFCNIFE LEKLLVESVR
HNDMQIRIDH QKNSIYFGTD LTESQREYRP DGPALQSMPS EQIRSQLVNM STVLTRAVSI
VYPNRERDQR AKLRTQMVHH YHEIKDREHQ RILQRQKIIE DRKEYIEKQN NAREEEEARR
QEEESRKAKL AEQKRLELEQ EERERKRHQN EIQAIKEKSL KEKVQQISQT AHGKKMLSKL
DEEGIKKLDA EQIAKRESEE LQRERKELQS KLKSQEKKID YYERAKRLEE IPLFEKYLAE
KQVKDKEFWE ATEKTRIENA IAERKDAVSQ QERLKRMYPD RDEFLEALKK ERASLYVEKL
KKFEIALEAE RKKRLADRVI RRREERRQAF LREKEEERLR KEEEIRLAQA AEERAAAEAR
RLEREAEDEK RRAQYEKQRA KEEEAERKIK EDRDRLAREV AVERERSDKE RDTWRPRGGD
RPSAAAAGGG GGAGEWRRAA APIGDRNERA GDRIERGGER MERGGDRMER GGDRMERGGE
RTERGGDRMD RGGERMDRGG ERGERGADRD RERRDNEGAD SSWRVRREPD SQRGAGVKDA
SGSAAPPSRD DKWRRGGDRD RDRDRDFRND GPRRDRDDRD DRDRGGFRRN DGPRRNDDAA
PRETGGNWRD APRQSDRDNR RPAGDRRDRE VRGGDLRGPE SRAPKEGGPS GGTGTAAGGG
GNWRTAPGPR DEPAPKRDQP QDKGKFSLTP VQL
