IF4B3_ARATH
ID IF4B3_ARATH Reviewed; 452 AA.
AC Q9SZP8; F4JUG0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Eukaryotic translation initiation factor 4B3 {ECO:0000303|PubMed:10600500};
DE Short=AtTif4B3 {ECO:0000303|PubMed:10600500};
DE Short=eIF4B3 {ECO:0000303|PubMed:10600500};
GN Name=EIF4B3 {ECO:0000303|PubMed:10600500};
GN OrderedLocusNames=At4g38710 {ECO:0000312|EMBL:AEE86967.1};
GN ORFNames=F20M13.270 {ECO:0000312|EMBL:CAB37527.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Chinese Spring;
RX PubMed=10600500; DOI=10.1006/bbrc.1999.1814;
RA Metz A.M., Wong K.C., Malmstrom S.A., Browning K.S.;
RT "Eukaryotic initiation factor 4B from wheat and Arabidopsis thaliana is a
RT member of a multigene family.";
RL Biochem. Biophys. Res. Commun. 266:314-321(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-270 AND SER-300, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP INTERACTION WITH MAD2.
RX PubMed=20706207; DOI=10.1038/msb.2010.53;
RA Van Leene J., Hollunder J., Eeckhout D., Persiau G., Van De Slijke E.,
RA Stals H., Van Isterdael G., Verkest A., Neirynck S., Buffel Y., De Bodt S.,
RA Maere S., Laukens K., Pharazyn A., Ferreira P.C.G., Eloy N., Renne C.,
RA Meyer C., Faure J.-D., Steinbrenner J., Beynon J., Larkin J.C.,
RA Van de Peer Y., Hilson P., Kuiper M., De Veylder L., Van Onckelen H.,
RA Inze D., Witters E., De Jaeger G.;
RT "Targeted interactomics reveals a complex core cell cycle machinery in
RT Arabidopsis thaliana.";
RL Mol. Syst. Biol. 6:397-397(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Promotes the eIF4F and eIF4A RNA-dependent ATP-hydrolysis
CC activity with different efficiency depending on mRNAs, thus providing
CC mRNA discrimination during initiation of translation.
CC {ECO:0000250|UniProtKB:Q9AUJ7}.
CC -!- SUBUNIT: Homodimer (By similarity). Nonspherical monomer. mRNA-
CC discriminating component of initiation complexes (By similarity).
CC Interacts with MAD2 (PubMed:20706207). {ECO:0000250|UniProtKB:Q9AUJ7,
CC ECO:0000250|UniProtKB:Q9SAD7, ECO:0000269|PubMed:20706207}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SZP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SZP8-2; Sequence=VSP_057921;
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9AUJ7}.
CC -!- SIMILARITY: Belongs to the eIF-4 subunit B family. {ECO:0000305}.
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DR EMBL; AL035540; CAB37527.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80535.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86967.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86968.1; -; Genomic_DNA.
DR EMBL; AY062647; AAL32725.1; -; mRNA.
DR EMBL; AY093255; AAM13254.1; -; mRNA.
DR PIR; T05699; T05699.
DR RefSeq; NP_001190956.1; NM_001204027.2. [Q9SZP8-2]
DR RefSeq; NP_195583.1; NM_120032.4. [Q9SZP8-1]
DR AlphaFoldDB; Q9SZP8; -.
DR IntAct; Q9SZP8; 1.
DR STRING; 3702.AT4G38710.2; -.
DR iPTMnet; Q9SZP8; -.
DR PaxDb; Q9SZP8; -.
DR PRIDE; Q9SZP8; -.
DR ProteomicsDB; 228875; -. [Q9SZP8-1]
DR EnsemblPlants; AT4G38710.1; AT4G38710.1; AT4G38710. [Q9SZP8-1]
DR EnsemblPlants; AT4G38710.2; AT4G38710.2; AT4G38710. [Q9SZP8-2]
DR GeneID; 830027; -.
DR Gramene; AT4G38710.1; AT4G38710.1; AT4G38710. [Q9SZP8-1]
DR Gramene; AT4G38710.2; AT4G38710.2; AT4G38710. [Q9SZP8-2]
DR KEGG; ath:AT4G38710; -.
DR Araport; AT4G38710; -.
DR TAIR; locus:2121264; AT4G38710.
DR eggNOG; ENOG502QWFU; Eukaryota.
DR OMA; WAIDSEE; -.
DR OrthoDB; 1368942at2759; -.
DR PhylomeDB; Q9SZP8; -.
DR PRO; PR:Q9SZP8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZP8; baseline and differential.
DR Genevisible; Q9SZP8; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR InterPro; IPR010433; EIF-4B_pln.
DR PANTHER; PTHR32091; PTHR32091; 1.
DR Pfam; PF06273; eIF-4B; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Initiation factor; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..452
FT /note="Eukaryotic translation initiation factor 4B3"
FT /id="PRO_0000434276"
FT REGION 20..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..179
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 215..222
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 28..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 383
FT /note="S -> SFSLHSYMEVDVLN (in isoform 2)"
FT /id="VSP_057921"
SQ SEQUENCE 452 AA; 48987 MW; 178EE61BC7E9EBCE CRC64;
MAAAVSSVWA KPGAWALEAE EHEAELKQQP SPTNQKSSAE DSSDFPSLAA AATTKTKKKK
GQTISLAEFA TYGTAKAKPA PQTERLTQAE LVALPTGPRE RSAEELDRSK LGGGFRSYGG
GRYGDESSSS RWGSSRVSED GERRGGGFNR DREPSRDSGP SRADEDDNWA AAKKPISGNG
FERRERGSGG GFFESQSQSK ADEVDSWVST KPSEPRRFVS SNGGGGDRFE KRGSFESLSR
NRDSQYGGGG GSESDTWGRR REESGAANGS PPPSGGSRPR LVLQPRTLPV AVVEVVKPES
PVLVIVEKPK GANPFGNARP REEVLAEKGQ DWKEIDEKLE AEKLKDIAAA MEKPNEKSTG
KMGFGLGNGR KDEERIERSW RKSTEHSEED AQEEEPAVEG AKKEETEDKP AVEEAKKEET
EGEQAVEEAK KEETGGEPAV EEAKKEETED KI
