EIF3A_DROWI
ID EIF3A_DROWI Reviewed; 1140 AA.
AC B4NIC3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=GK13753;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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; CH964272; EDW83705.1; -; Genomic_DNA.
DR RefSeq; XP_002072719.1; XM_002072683.2.
DR AlphaFoldDB; B4NIC3; -.
DR SMR; B4NIC3; -.
DR STRING; 7260.FBpp0242896; -.
DR EnsemblMetazoa; FBtr0244404; FBpp0242896; FBgn0215761.
DR GeneID; 6650110; -.
DR KEGG; dwi:6650110; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_1_1_1; -.
DR InParanoid; B4NIC3; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 152929at2759; -.
DR PhylomeDB; B4NIC3; -.
DR ChiTaRS; eIF3-S10; fly.
DR Proteomes; UP000007798; 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_0000366344"
FT DOMAIN 319..502
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 590..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1057
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 133443 MW; CB3BD9CEA3A5F1D0 CRC64;
MARYTQRPEN ALKRANEFIE VGKPLRALDT LQEVFRNKRW NYAYSETVIE PLMFKYLYLC
VELKKSHIAK EGLFQYRNMF QLVNVNSLEN VIRGYLKMAE EHTEAAQAQS SAAVAVLELD
DLDNIATPES ILMSAVCGED AQDRSDRTIL LPWVKFLWES YCQCLELLRV NTHCETLYHD
IARMAFQFCL KYNRKSEFRR LCDKLRKHLE DICKSSNQTT GVSINKVETQ QLCLDTRLYL
LDSAIQMELW QEAYKAIEDI HGLMALSKKT PVPKTMANYY QKLAMVFSKA GNQLFHAAAL
LKLFQLTREL KKNLTKDDLQ RMAAHVLLAT LSIPLPSAHP EFDRFIEADK SPLEKAQKLA
ILLGLPQPPT RVSLIREVVR LNVPQLVSED FRNLYNWLEV DFNPLNLCQR IQSVVDTIES
GPAETSLLTP YIQSLKDVTI MRLIRQISQV YESIEFKRLL ELASFCNVFE LEKLLVESVR
HNDMQIRIDH QKHCIYFGTD LTESQREYRP DGPTLQSMPS EQIRSQLVNM STVLTRAVSI
VYPDREREQR AKLRTQMVHH YHEIKDREHQ RILQRQKIIE DRKEFIEKQN NAREEEEARR
QEEESRKAKL AEQKRLEQEQ EERERKRHQN EIQAIREKSL KEKVQQISQT AHGKKMLSKL
DEEGIKKLDA EQIAKRENEE LQREAKELQS KLKSQEKKID YFERAKRLEE IPLFEKYLTE
KQVKDKEFWE ATEQTRIENA ITERKDAVSQ QERLKRMYPD RDEYLEALKK ERASLYLEKV
EKFEIALEVE RKKRLADRVI RRREERRQAH LREKEEERLR KEEEIRMAQA AEERAAAEAR
RLEREAEDEK RRAQYEKQRA KEEEAERKIK EDRDRLAREV AVERERSDKE RDTWRPRGDR
PEGRPSAAAG GGGASEWRRP APTADRADRD RGADRDRGAD RDRGADRDRG ADRERGADRD
RKDNEAGGAS DSWRVRREPD SQRNAAPKDG GGSSGGAQPS RDDKWRRGGD RERDRDFRND
GQGPRRGGDR EDDRDRGGFR RNDGPRRNEE QQRETGGNWR DAPRQSDNRD NRRPAGGDRR
DRDRDVRGAG PKEGGGGGGG NWRTAPAPRD EKPTTKQRDQ PQDKENKAGD DGEWTSVKRR
