ID   ELP6_ARATH              Reviewed;         262 AA.
AC   Q8L9Y2; C0Z343; Q9SN32;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Elongator complex protein 6;
DE            Short=AtELP6;
DE   AltName: Full=Elongator component 6;
DE   AltName: Full=UPF0405 protein ELP6;
GN   Name=ELP6; OrderedLocusNames=At4g10090; ORFNames=F28M11.10;
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 [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; TISSUE=Rosette leaf;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=19500300; DOI=10.1111/j.1365-313x.2009.03931.x;
RA   Zhou X., Hua D., Chen Z., Zhou Z., Gong Z.;
RT   "Elongator mediates ABA responses, oxidative stress resistance and
RT   anthocyanin biosynthesis in Arabidopsis.";
RL   Plant J. 60:79-90(2009).
RN   [8]
RP   SUBUNIT, AND INTERACTION WITH ELP4.
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).
CC   -!- FUNCTION: Component of the elongator complex which is required for
CC       multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC       uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC       (5-carbamoylmethyl uridine) (By similarity). The elongator complex
CC       catalyzes formation of carboxymethyluridine in the wobble base at
CC       position 34 in tRNAs (By similarity). Promotes organ development by
CC       modulating cell division rate. Involved in oxidative stress signaling.
CC       Prevents anthocyanins accumulation (PubMed:19500300).
CC       {ECO:0000250|UniProtKB:Q0PNE2, ECO:0000269|PubMed:19500300}.
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis. {ECO:0000250|UniProtKB:Q0PNE2}.
CC   -!- SUBUNIT: Component of the elongator complex which consists of
CC       ELP1/ELO2, ELP2, ELP3/ELO3, ELP4/ELO1, ELP5, and ELP6. Interacts
CC       directly with ELP4. {ECO:0000269|PubMed:20080602}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, flowers,
CC       siliques and guard cells. {ECO:0000269|PubMed:19500300}.
CC   -!- DISRUPTION PHENOTYPE: Narrow leaves and reduced root growth that
CC       results from a decreased cell division rate. Higher resistance to
CC       oxidative stress mediated by methyl viologen (MV) that blocks electron
CC       transport during photosynthesis and by CsCl in light. Accumulates
CC       anthocyanins. {ECO:0000269|PubMed:19500300}.
CC   -!- SIMILARITY: Belongs to the ELP6 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:Q0PNE2}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAH57122.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB39761.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78132.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL049487; CAB39761.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161516; CAB78132.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82837.1; -; Genomic_DNA.
DR   EMBL; AK319007; BAH57122.1; ALT_FRAME; mRNA.
DR   EMBL; AK227863; BAE99839.1; -; mRNA.
DR   EMBL; BT024488; ABD19669.1; -; mRNA.
DR   EMBL; AY088150; AAM65695.1; -; mRNA.
DR   PIR; T04059; T04059.
DR   RefSeq; NP_567351.1; NM_117077.4.
DR   AlphaFoldDB; Q8L9Y2; -.
DR   SMR; Q8L9Y2; -.
DR   STRING; 3702.AT4G10090.1; -.
DR   PaxDb; Q8L9Y2; -.
DR   PRIDE; Q8L9Y2; -.
DR   ProteomicsDB; 222318; -.
DR   EnsemblPlants; AT4G10090.1; AT4G10090.1; AT4G10090.
DR   GeneID; 826600; -.
DR   Gramene; AT4G10090.1; AT4G10090.1; AT4G10090.
DR   KEGG; ath:AT4G10090; -.
DR   Araport; AT4G10090; -.
DR   TAIR; locus:2124651; AT4G10090.
DR   eggNOG; KOG4723; Eukaryota.
DR   HOGENOM; CLU_092581_1_0_1; -.
DR   InParanoid; Q8L9Y2; -.
DR   OMA; MFTELNS; -.
DR   OrthoDB; 1272502at2759; -.
DR   PhylomeDB; Q8L9Y2; -.
DR   UniPathway; UPA00988; -.
DR   PRO; PR:Q8L9Y2; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8L9Y2; baseline and differential.
DR   Genevisible; Q8L9Y2; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR   GO; GO:0031538; P:negative regulation of anthocyanin metabolic process; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR   GO; GO:2000024; P:regulation of leaf development; IMP:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR   GO; GO:0010015; P:root morphogenesis; IMP:TAIR.
DR   GO; GO:0010016; P:shoot system morphogenesis; IMP:TAIR.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR018627; ELP6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR16184; PTHR16184; 1.
DR   Pfam; PF09807; ELP6; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Reference proteome; tRNA processing.
FT   CHAIN           1..262
FT                   /note="Elongator complex protein 6"
FT                   /id="PRO_0000416792"
FT   CONFLICT        211
FT                   /note="A -> S (in Ref. 3; BAH57122)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   262 AA;  29125 MW;  33E9579B2C0FD550 CRC64;
     MDRSLNLLDL ALGFDEQLAI PSPLNGKVIL IEDCVETSGS FVLHQLMKRV LSSNSSDALI
     FLAFARPFSH YDRILRKLGC NLATHKSNNR LVFFDMLMVK CSDGDQMEDN VSAVAKLFRE
     IQETVRKLQS VTSGNITVMV DDMSLLEIAT TGSNSDHVLD FLHYCHTLSS ESNCSLVILN
     HEDIYASMER PAFLLQMVCL ADVVIKAEPL ASGLANDVHG QLTVLNKGIS NSGRGSSRNK
     LQNFQFRIKE NGIDYFYPGC RS