EIF3A_ARATH
ID EIF3A_ARATH Reviewed; 987 AA.
AC Q9LD55;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 135.
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 large subunit;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=eIF-3-theta {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=p114;
GN Name=TIF3A1; OrderedLocusNames=At4g11420; ORFNames=F25E4.40;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11042177; DOI=10.1074/jbc.m007236200;
RA Burks E.A., Bezerra P.P., Le H., Gallie D.R., Browning K.S.;
RT "Plant initiation factor 3 subunit composition resembles mammalian
RT initiation factor 3 and has a novel subunit.";
RL J. Biol. Chem. 276:2122-2131(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP INTERACTION WITH TIF3H1.
RX PubMed=15548739; DOI=10.1105/tpc.104.026880;
RA Kim T.-H., Kim B.-H., Yahalom A., Chamovitz D.A., von Arnim A.G.;
RT "Translational regulation via 5' mRNA leader sequences revealed by
RT mutational analysis of the Arabidopsis translation initiation factor
RT subunit eIF3h.";
RL Plant Cell 16:3341-3356(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(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. Binds to the translation initiation factor TIF3H1
CC (PubMed:15548739). {ECO:0000255|HAMAP-Rule:MF_03000,
CC ECO:0000269|PubMed:15548739}.
CC -!- INTERACTION:
CC Q9LD55; F4K210: MAF19.20; NbExp=2; IntAct=EBI-7217371, EBI-7216904;
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; AF291711; AAG53635.1; -; mRNA.
DR EMBL; AL050399; CAB82147.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81243.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83010.1; -; Genomic_DNA.
DR PIR; T10562; T10562.
DR RefSeq; NP_192881.1; NM_117213.4.
DR AlphaFoldDB; Q9LD55; -.
DR SMR; Q9LD55; -.
DR BioGRID; 12045; 35.
DR IntAct; Q9LD55; 1.
DR MINT; Q9LD55; -.
DR STRING; 3702.AT4G11420.1; -.
DR iPTMnet; Q9LD55; -.
DR SwissPalm; Q9LD55; -.
DR PaxDb; Q9LD55; -.
DR PRIDE; Q9LD55; -.
DR ProteomicsDB; 221937; -.
DR EnsemblPlants; AT4G11420.1; AT4G11420.1; AT4G11420.
DR GeneID; 826746; -.
DR Gramene; AT4G11420.1; AT4G11420.1; AT4G11420.
DR KEGG; ath:AT4G11420; -.
DR Araport; AT4G11420; -.
DR TAIR; locus:2123076; AT4G11420.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_1_1_1; -.
DR InParanoid; Q9LD55; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR PhylomeDB; Q9LD55; -.
DR PRO; PR:Q9LD55; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9LD55; baseline and differential.
DR Genevisible; Q9LD55; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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:TAIR.
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; IDA:TAIR.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:TAIR.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; TAS:TAIR.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..987
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000123540"
FT DOMAIN 316..513
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 808..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..122
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 556..742
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 797..858
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 808..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 114300 MW; F38BA715209D55FB CRC64;
MANFAKPENA LKRADELINV GQKQDALQAL HDLITSKRYR AWQKPLEKIM FKYLDLCVDL
KRGRFAKDGL IQYRIVCQQV NVSSLEEVIK HFLHLATDKA EQARSQADAL EEALDVDDLE
ADRKPEDLQL SIVSGEKGKD RSDRELVTPW FKFLWETYRT VLEILRNNSK LEALYAMTAH
KAFQFCKQYK RTTEFRRLCE IIRNHLANLN KYRDQRDRPD LSAPESLQLY LDTRFDQLKV
ATELGLWQEA FRSVEDIYGL MCMVKKTPKS SLLMVYYSKL TEIFWISSSH LYHAYAWFKL
FSLQKNFNKN LSQKDLQLIA SSVVLAALSI PPFDRAQSAS HMELENEKER NLRMANLIGF
NLEPKFEGKD MLSRSALLSE LVSKGVLSCA SQEVKDLFHV LEHEFHPLDL GSKIQPLLEK
ISKSGGKLSS APSLPEVQLS QYVPSLEKLA TLRLLQQVSK IYQTIRIESL SQLVPFFQFS
EVEKISVDAV KNNFVAMKVD HMKGVVIFGN LGIESDGLRD HLAVFAESLS KVRAMLYPVP
SKASKLAGVI PNLADTVEKE HKRLLARKSI IEKRKEDQER QQLEMEREEE QKRLKLQKLT
EEAEQKRLAA ELAERRKQRI LREIEEKELE EAQALLEETE KRMKKGKKKP LLDGEKVTKQ
SVKERALTEQ LKERQEMEKK LQKLAKTMDY LERAKREEAA PLIEAAYQRR LVEEREFYER
EQQREVELSK ERHESDLKEK NRLSRMLGNK EIFQAQVISR RQAEFDRIRT EREERISKII
REKKQERDIK RKQIYYLKIE EERIRKLQEE EEARKQEEAE RLKKVEAERK ANLDKAFEKQ
RQREIELEEK SRREREELLR GTNAPPARLA EPTVTPVGTT APAAAAAAAG APAAPYVPKW
KRQTTEVSGP SAPTSSETDR RSNRGPPPGD DHWGSNRGAA QNTDRWTSNR ERSGPPAEGG
DRWGSGPRGS DDRRSTFGSS RPRPTQR
