EIF3A_DROYA
ID EIF3A_DROYA Reviewed; 1137 AA.
AC B4PTS9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=GE25350;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000160; EDW95662.1; -; Genomic_DNA.
DR RefSeq; XP_002095950.1; XM_002095914.2.
DR AlphaFoldDB; B4PTS9; -.
DR SMR; B4PTS9; -.
DR STRING; 7245.FBpp0270360; -.
DR PRIDE; B4PTS9; -.
DR EnsemblMetazoa; FBtr0271868; FBpp0270360; FBgn0242428.
DR GeneID; 6535294; -.
DR KEGG; dya:Dyak_GE25350; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_1_1_1; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 152929at2759; -.
DR PhylomeDB; B4PTS9; -.
DR ChiTaRS; eIF3-S10; fly.
DR Proteomes; UP000002282; Chromosome 3R.
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; Phosphoprotein; Protein biosynthesis;
KW RNA-binding.
FT CHAIN 1..1137
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366345"
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..1137
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 923..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1085
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1137
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 1137 AA; 133645 MW; D4A8627E00F2ACF4 CRC64;
MARYTQRPEN ALKRANEFIE VGKPLRALDT LQEVFRNKRW NYAYSETVIE PLMFKYLYLC
VELKKSHIAK EGLFQYRNMF QLVNVNSLEN VIRGYLKMAE EHTEAAQAQS SAAVAVLELD
DLDNIATPES ILMSAVCGED AQDRSDRTIL LPWVKFLWES YCQCLELLRV NTHCEALYHD
IARMAFHFCL KYNRKSEFRR LCDKLRKHLE DICKSSNQTT GVSINKVETQ QLCLDTRLYL
LDSAIQMELW QEAYRAIEDI HGLMALSKKT PVPKTMANYY QKLAMVFSKA GNQLFHAAAL
LKLFQLTREL KKNLTKDDLQ RMAAHVLLAT LSIPLPSAHP EFDRFIEADK SPLEKAQKLA
VLLGLPQPPT RVSLIREVVR LNVPQLVSED FRNLYNWLEV DFNPLNLCKR IQSIVDFIEN
GPENALLTPY IQSLKDVTIM RLIRQISQVY ESIEFQRLMQ LASFCNIFEL EKLLVESVRH
NDMQIRIDHQ KNSIYFGTDL TESQREYRPD GPALQSMPSE QIRSQLVNMS TVLTRAVSIV
YPNRERDQRA KLRTQMVNHY HEIKDREHQR ILQRQKIIED RKEYIEKQNN AREEEEARRQ
EEESRKAKLA EQKRLEQEQE ERERKRHQNE IQAIREKSLK EKVQQISQTA HGKKMLSKLD
EEGIKKLDAE QIAKRESEEL QREAKELQSK LKSQEKKIDY FERAKRLEEI PLFEKYLAEK
QVKDKEFWEA TEKTRIENAI AERKDAVGQQ ERLKRMYPDR DEFLDALKKE RASLYVEKLK
KFEAALEAER KKRLADRIIR RREERRQAFL REKEEERLRK EEEIRLAQAA EERAAAEARR
LEREAEDEKR RAQYEKQRAK EEEAERKIKE DRERLARELA SERERTEKER DTWRPRGGDR
PSAPSGGSGE WRRGAPTVNN ERGIERGGDR IERGGDRIER GGERIERGGD RDRKDNEGAD
SSWRVRREPD SQRAAAPKDS GAPQSRDEKW RRGGERDRDF RNDGARRDRD DGPRRDRDDG
PRRDRDDERS GFRRNDGPRR TEEPQRETGG NWRDAPRHAD RENRRTAGGE RRDRDVRETR
GDQRGPAPKE AVSSGGGGNW RTTPAAREEK PATKRDQPQE KENKAADDGE WTSVKRR
