ELP3_ARATH
ID ELP3_ARATH Reviewed; 565 AA.
AC Q93ZR1; Q9FK40;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Elongator complex protein 3 {ECO:0000303|PubMed:20398216};
DE Short=AtELP3 {ECO:0000303|PubMed:20398216};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:D5VRB9};
DE AltName: Full=Elongator component 3 {ECO:0000303|PubMed:20398216};
DE AltName: Full=Protein ELONGATA 3 {ECO:0000303|PubMed:15894610};
DE AltName: Full=Protein ENHANCER-OF-ASYMMETRIC-LEAVES-TWO1 {ECO:0000303|PubMed:21700721};
DE AltName: Full=tRNA uridine(34) acetyltransferase {ECO:0000305};
GN Name=HAG3 {ECO:0000303|PubMed:12466527};
GN Synonyms=EAST1 {ECO:0000303|PubMed:21700721},
GN ELO3 {ECO:0000303|PubMed:15894610}, ELP3 {ECO:0000303|PubMed:20398216};
GN OrderedLocusNames=At5g50320 {ECO:0000312|Araport:AT5G50320};
GN ORFNames=MXI22.3 {ECO:0000312|EMBL:BAB09451.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASP-331, DISRUPTION PHENOTYPE,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RX PubMed=15894610; DOI=10.1073/pnas.0502600102;
RA Nelissen H., Fleury D., Bruno L., Robles P., de Veylder L., Traas J.,
RA Micol J., Van Montagu M., Inze D., Van Lijsebettens M.;
RT "The elongata mutants identify a functional Elongator complex in plants
RT with a role in cell proliferation during organ growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7754-7759(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 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 [5]
RP NOMENCLATURE.
RX PubMed=12466527; DOI=10.1093/nar/gkf660;
RA Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT "Analysis of histone acetyltransferase and histone deacetylase families of
RT Arabidopsis thaliana suggests functional diversification of chromatin
RT modification among multicellular eukaryotes.";
RL Nucleic Acids Res. 30:5036-5055(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20398216; DOI=10.1111/j.1365-2958.2010.07163.x;
RA Mehlgarten C., Jablonowski D., Wrackmeyer U., Tschitschmann S.,
RA Sondermann D., Jaeger G., Gong Z., Bystroem A.S., Schaffrath R.,
RA Breunig K.D.;
RT "Elongator function in tRNA wobble uridine modification is conserved
RT between yeast and plants.";
RL Mol. Microbiol. 76:1082-1094(2010).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE ELONGATOR COMPLEX, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20080602; DOI=10.1073/pnas.0913559107;
RA Nelissen H., De Groeve S., Fleury D., Neyt P., Bruno L., Bitonti M.B.,
RA Vandenbussche F., Van der Straeten D., Yamaguchi T., Tsukaya H.,
RA Witters E., De Jaeger G., Houben A., Van Lijsebettens M.;
RT "Plant Elongator regulates auxin-related genes during RNA polymerase II
RT transcription elongation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1678-1683(2010).
RN [8]
RP INTERACTION WITH IYO.
RX PubMed=21620701; DOI=10.1016/j.cub.2011.04.041;
RA Sanmartin M., Sauer M., Munoz A., Zouhar J., Ordonez A., van de Ven W.T.,
RA Caro E., de la Paz Sanchez M., Raikhel N.V., Gutierrez C.,
RA Sanchez-Serrano J.J., Rojo E.;
RT "A molecular switch for initiating cell differentiation in Arabidopsis.";
RL Curr. Biol. 21:999-1008(2011).
RN [9]
RP FUNCTION, MUTAGENESIS OF ARG-200, AND DISRUPTION PHENOTYPE.
RX PubMed=21700721; DOI=10.1093/pcp/pcr083;
RA Kojima S., Iwasaki M., Takahashi H., Imai T., Matsumura Y., Fleury D.,
RA Van Lijsebettens M., Machida Y., Machida C.;
RT "Asymmetric leaves2 and Elongator, a histone acetyltransferase complex,
RT mediate the establishment of polarity in leaves of Arabidopsis thaliana.";
RL Plant Cell Physiol. 52:1259-1273(2011).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=22404109; DOI=10.1111/j.1365-313x.2012.04984.x;
RA Tran H.T., Nimick M., Uhrig R.G., Templeton G., Morrice N., Gourlay R.,
RA DeLong A., Moorhead G.B.;
RT "Arabidopsis thaliana histone deacetylase 14 (HDA14) is an alpha-tubulin
RT deacetylase that associates with PP2A and enriches in the microtubule
RT fraction with the putative histone acetyltransferase ELP3.";
RL Plant J. 71:263-272(2012).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=22026817; DOI=10.1111/j.1365-313x.2011.04831.x;
RA Xu D., Huang W., Li Y., Wang H., Huang H., Cui X.;
RT "Elongator complex is critical for cell cycle progression and leaf
RT patterning in Arabidopsis.";
RL Plant J. 69:792-808(2012).
RN [12]
RP FUNCTION, MUTAGENESIS OF GLU-423, AND TISSUE SPECIFICITY.
RX PubMed=23969312; DOI=10.1016/j.ydbio.2013.08.008;
RA Skylar A., Matsuwaka S., Wu X.;
RT "ELONGATA3 is required for shoot meristem cell cycle progression in
RT Arabidopsis thaliana seedlings.";
RL Dev. Biol. 382:436-445(2013).
RN [13]
RP FUNCTION.
RX PubMed=25907565; DOI=10.1093/pcp/pcv054;
RA Fina J.P., Casati P.;
RT "HAG3, a histone acetyltransferase, affects UV-B responses by negatively
RT regulating the expression of DNA repair enzymes and sunscreen content in
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 56:1388-1400(2015).
CC -!- FUNCTION: Catalytic tRNA acetyltransferase subunit of the elongator
CC complex which is required for multiple tRNA modifications, including
CC mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-
CC methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl
CC uridine) (PubMed:20398216). In the elongator complex, acts as a tRNA
CC uridine(34) acetyltransferase by mediating formation of
CC carboxymethyluridine in the wobble base at position 34 in tRNAs (By
CC similarity). Promotes organ development by modulating cell division
CC rate (PubMed:20080602). Required for auxin distribution or signaling
CC (PubMed:20080602). Required for meristem cell cycle activation at the
CC time of germination (PubMed:23969312). Mediates the establishment of
CC leaf polarity independently of AS2 and the ta-siRNA-related pathway
CC (PubMed:21700721). Indirectly involved in negatively regulating the
CC expression of genes that participate in UV-B responses, such as DNA
CC repair enzymes and enzymes that participate in sunscreen pigment
CC biosynthesis (PubMed:25907565). {ECO:0000250|UniProtKB:D5VRB9,
CC ECO:0000269|PubMed:20080602, ECO:0000269|PubMed:20398216,
CC ECO:0000269|PubMed:21700721, ECO:0000269|PubMed:23969312,
CC ECO:0000269|PubMed:25907565}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in
CC tRNA = 5'-deoxyadenosine + carboxymethyluridine(34) in tRNA + CoA + 2
CC H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407,
CC Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315,
CC ChEBI:CHEBI:74882; Evidence={ECO:0000250|UniProtKB:D5VRB9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021;
CC Evidence={ECO:0000250|UniProtKB:D5VRB9};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q02908};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:Q02908};
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q9H9T3}.
CC -!- SUBUNIT: Component of the elongator complex which consists of
CC ELP1/ELO2, ELP2, ELP3/ELO3, ELP4/ELO1, ELP5, and ELP6
CC (PubMed:20080602). Interacts with IYO (PubMed:21620701).
CC {ECO:0000269|PubMed:20080602, ECO:0000269|PubMed:21620701}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20080602,
CC ECO:0000269|PubMed:22026817, ECO:0000269|PubMed:22404109}. Cytoplasm
CC {ECO:0000269|PubMed:22404109}. Note=Localized in euchromatin during
CC interphase. {ECO:0000269|PubMed:20080602}.
CC -!- TISSUE SPECIFICITY: Expressed in meristematic tissues of in roots,
CC leaves, seedlings, cotyledons, floral buds and shoot apices
CC (PubMed:15894610, PubMed:20080602, PubMed:23969312). Expressed in the
CC shoot meristem and the emerging leaves immediately after germination
CC (PubMed:23969312). In the root, expressed in the transition zone and
CC the upper meristematic zone (PubMed:23969312).
CC {ECO:0000269|PubMed:15894610, ECO:0000269|PubMed:20080602,
CC ECO:0000269|PubMed:23969312}.
CC -!- DISRUPTION PHENOTYPE: Slow growing rate associated with pale-green and
CC downwardly curled narrow leaves and reduced root growth that results
CC from a decreased cell division rate and a reduced apical dominance.
CC Defect in tRNA wobble uridine modification. Filamentous leaves with
CC abaxialized epidermis in AS2 defective plants.
CC {ECO:0000269|PubMed:15894610, ECO:0000269|PubMed:20080602,
CC ECO:0000269|PubMed:20398216, ECO:0000269|PubMed:21700721}.
CC -!- SIMILARITY: Belongs to the ELP3 family. {ECO:0000305}.
CC -!- CAUTION: The elongator complex was originally thought to play a role in
CC transcription elongation. However, it is no longer thought to play a
CC direct role in this process and its primary function is thought to be
CC in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL06951.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ964958; CAI79647.1; -; mRNA.
DR EMBL; AB012248; BAB09451.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95925.1; -; Genomic_DNA.
DR EMBL; AY054293; AAL06951.1; ALT_INIT; mRNA.
DR EMBL; AY056323; AAL07172.1; -; mRNA.
DR EMBL; AY133528; AAM91358.1; -; mRNA.
DR RefSeq; NP_568725.1; NM_124412.3.
DR AlphaFoldDB; Q93ZR1; -.
DR SMR; Q93ZR1; -.
DR BioGRID; 20344; 3.
DR IntAct; Q93ZR1; 3.
DR STRING; 3702.AT5G50320.1; -.
DR iPTMnet; Q93ZR1; -.
DR PaxDb; Q93ZR1; -.
DR PRIDE; Q93ZR1; -.
DR ProteomicsDB; 221890; -.
DR EnsemblPlants; AT5G50320.1; AT5G50320.1; AT5G50320.
DR GeneID; 835098; -.
DR Gramene; AT5G50320.1; AT5G50320.1; AT5G50320.
DR KEGG; ath:AT5G50320; -.
DR Araport; AT5G50320; -.
DR TAIR; locus:2177477; AT5G50320.
DR eggNOG; KOG2535; Eukaryota.
DR HOGENOM; CLU_025983_2_1_1; -.
DR InParanoid; Q93ZR1; -.
DR OMA; TFETRPD; -.
DR OrthoDB; 320059at2759; -.
DR PhylomeDB; Q93ZR1; -.
DR BRENDA; 2.3.1.48; 399.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q93ZR1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93ZR1; baseline and differential.
DR Genevisible; Q93ZR1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0106261; F:tRNA uridine(34) acetyltransferase activity; IEA:RHEA.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0009294; P:DNA-mediated transformation; IMP:TAIR.
DR GO; GO:0035265; P:organ growth; IMP:TAIR.
DR GO; GO:0010928; P:regulation of auxin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:2000025; P:regulation of leaf formation; IMP:UniProtKB.
DR GO; GO:0090708; P:specification of plant organ axis polarity; IMP:UniProtKB.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR039661; ELP3.
DR InterPro; IPR034687; ELP3-like.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032432; Radical_SAM_C.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR11135; PTHR11135; 1.
DR PANTHER; PTHR11135:SF7; PTHR11135:SF7; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF16199; Radical_SAM_C; 1.
DR PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 1.
DR SFLD; SFLDF00344; ELP3-like; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR01211; ELP3; 1.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acyltransferase; Auxin signaling pathway; Cytoplasm; Iron;
KW Iron-sulfur; Metal-binding; Nucleus; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..565
FT /note="Elongator complex protein 3"
FT /id="PRO_0000232128"
FT DOMAIN 100..390
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 414..565
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q02908"
FT BINDING 127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q02908"
FT BINDING 130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q02908"
FT BINDING 182
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 492..495
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 515..517
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 548
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT MUTAGEN 200
FT /note="R->W: In east1-1; slow growth associated with pale-
FT green and downwardly curled leaves."
FT /evidence="ECO:0000269|PubMed:21700721"
FT MUTAGEN 331
FT /note="D->N: In elo3-1; reduced cell proliferation."
FT /evidence="ECO:0000269|PubMed:15894610"
FT MUTAGEN 423
FT /note="E->K: In elo3-14; reduced tissue proliferation in
FT the meristem."
FT /evidence="ECO:0000269|PubMed:23969312"
SQ SEQUENCE 565 AA; 63694 MW; 8F993E4D41CF4B05 CRC64;
MATAVVMNGE LKKQPRPGKG GYQGRGLTEE EARVRAISEI VSTMIERSHR NENVDLNAIK
TAACRKYGLA RAPKLVEMIA ALPDSERETL LPKLRAKPVR TASGIAVVAV MSKPHRCPHI
ATTGNICVYC PGGPDSDFEY STQSYTGYEP TSMRAIRARY NPYVQARSRI DQLKRLGHSV
DKVEFILMGG TFMSLPAEYR DFFIRNLHDA LSGHTSANVE EAVAYSEHSA TKCIGMTIET
RPDYCLGPHL RQMLIYGCTR LEIGVQSTYE DVARDTNRGH TVAAVADCFC LAKDAGFKVV
AHMMPDLPNV GVERDMESFK EFFESPSFRA DGLKIYPTLV IRGTGLYELW KTGRYRNYPP
EQLVDIVARI LSMVPPWTRV YRVQRDIPMP LVTSGVEKGN LRELALARMD DLGLKCRDVR
TREAGIQDIH HKIKPEQVEL VRRDYTANEG WETFLSYEDT RQDILVGLLR LRKCGKNVTC
PELMGKCSVV RELHVYGTAV PVHGRDADKL QHQGYGTLLM EEAERIARRE HRSNKIGVIS
GVGTRHYYRK LGYELEGPYM VKHLL
