EIF3A_DROME
ID EIF3A_DROME Reviewed; 1140 AA.
AC Q9VN25; Q0KID1; Q494J3; Q8IH03; Q8SYE5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
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};
GN ORFNames=CG9805 {ECO:0000312|FlyBase:FBgn0037249};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-1140.
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH PIX.
RX PubMed=17392269; DOI=10.1074/jbc.m701361200;
RA Andersen D.S., Leevers S.J.;
RT "The essential Drosophila ATP-binding cassette domain protein, pixie, binds
RT the 40 S ribosome in an ATP-dependent manner and is required for
RT translation initiation.";
RL J. Biol. Chem. 282:14752-14760(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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 (By similarity) (PubMed:17392269). The eIF-3 complex
CC interacts with pix (By similarity) (PubMed:17392269).
CC {ECO:0000255|HAMAP-Rule:MF_03000, ECO:0000269|PubMed:17392269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9VN25-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VN25-2; Sequence=VSP_036575;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN71260.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF52126.1; -; Genomic_DNA.
DR EMBL; AY071601; AAL49223.1; -; mRNA.
DR EMBL; BT001505; AAN71260.1; ALT_INIT; mRNA.
DR EMBL; BT023783; AAZ41792.1; -; mRNA.
DR RefSeq; NP_649470.2; NM_141213.4. [Q9VN25-1]
DR RefSeq; NP_730838.3; NM_168999.3. [Q9VN25-1]
DR AlphaFoldDB; Q9VN25; -.
DR SMR; Q9VN25; -.
DR BioGRID; 65782; 26.
DR IntAct; Q9VN25; 22.
DR MINT; Q9VN25; -.
DR STRING; 7227.FBpp0078584; -.
DR iPTMnet; Q9VN25; -.
DR PaxDb; Q9VN25; -.
DR PRIDE; Q9VN25; -.
DR EnsemblMetazoa; FBtr0078944; FBpp0078584; FBgn0037249. [Q9VN25-1]
DR EnsemblMetazoa; FBtr0346646; FBpp0312226; FBgn0037249. [Q9VN25-1]
DR GeneID; 40563; -.
DR KEGG; dme:Dmel_CG9805; -.
DR UCSC; CG9805-RA; d. melanogaster. [Q9VN25-1]
DR UCSC; CG9805-RB; d. melanogaster.
DR CTD; 8661; -.
DR FlyBase; FBgn0037249; eIF3a.
DR VEuPathDB; VectorBase:FBgn0037249; -.
DR eggNOG; KOG2072; Eukaryota.
DR GeneTree; ENSGT00730000111063; -.
DR HOGENOM; CLU_002096_1_0_1; -.
DR InParanoid; Q9VN25; -.
DR OMA; VMYQTTA; -.
DR PhylomeDB; Q9VN25; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR SignaLink; Q9VN25; -.
DR BioGRID-ORCS; 40563; 1 hit in 1 CRISPR screen.
DR ChiTaRS; eIF3-S10; fly.
DR GenomeRNAi; 40563; -.
DR PRO; PR:Q9VN25; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037249; Expressed in eye disc (Drosophila) and 22 other tissues.
DR Genevisible; Q9VN25; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IBA:GO_Central.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; ISS:FlyBase.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..1140
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366337"
FT DOMAIN 319..501
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 588..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..1140
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..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"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:18327897"
FT VAR_SEQ 163..230
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_036575"
FT CONFLICT 1106
FT /note="A -> P (in Ref. 3; AAL49223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1132
FT /note="G -> S (in Ref. 3; AAL49223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1140 AA; 133880 MW; E249F68B8861B6DC 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 KLRNQMVNHY HEIKDREHQR ILQRQKIIED RKEYIEKQNN AREEEEARRQ
EEESRKAKLA EQKRLEQEQE ERERKRHQNE IQAIREKSLK EKVQQISQTA HGKKMLSKLD
EEGIKKLDAE QIAKRESEEL QREAKELQSK LKSQEKKIDY FERAKRLEEI PLFEKYLAEK
QVKDKEFWEA TEKTRIENAI AERKDAVAQQ ERLKRMYPDR DEFLEALKKE RASLYVEKLK
KFEAALEAER KKRLADRIIR RREERRQAFL REKEEERLRK EEEIRLAQAA EERAAAEARR
LEREAEDEKR RAQYEKQRAK EEEAERKIKE DRDRLSRELA SERERTEKDR DTWRPRGGDR
PSASNGGSSE WRRAAPAASE RNDRGGERIE RGGERIERGG ERLERGGERI ERGGDRDRKD
NEGADSSWRV RREPDSQRAA APKDSGAPQS RDDKWRRGGE RDRDFRIDGA RRDRDDGPRR
DRDDGPRRDR DDERGGFRRA DGARRTDEPQ RETGGNWRDA PRHADRETRR PAERRDRDVR
ETRGDQRGSA PKEAASGGVG GNWRTAPATR EEKPAAKRDQ AQEKENKAGD DGEWTSVKRR
