ELP4_ARATH
ID ELP4_ARATH Reviewed; 355 AA.
AC Q9C778; F4J676; Q4W0V9; Q8W4Q0;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Elongator complex protein 4;
DE Short=AtELP4;
DE AltName: Full=Elongator component 4;
DE AltName: Full=Protein ELONGATA 1;
GN Name=ELP4; Synonyms=ELO1; OrderedLocusNames=At3g11220; ORFNames=F11B9.14;
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] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and 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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] (ISOFORM 2).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17565971; DOI=10.1093/aob/mcm102;
RA Falcone A., Nelissen H., Fleury D., Van Lijsebettens M., Bitonti M.B.;
RT "Cytological investigations of the Arabidopsis thaliana elo1 mutant give
RT new insights into leaf lateral growth and Elongator function.";
RL Ann. Bot. 100:261-270(2007).
RN [6]
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 [7]
RP FUNCTION, SUBUNIT, INTERACTION WITH ELP6, TISSUE SPECIFICITY, AND
RP 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).
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 the formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (By similarity). Promotes organ development by
CC modulating cell division rate. May regulate mechanisms producing carbon
CC assimilates or importing sucrose. Involved in the repression of the
CC abscisic acid (ABA) signaling pathway during seed germination and
CC seedling growth. Required for auxin distribution or signaling. Involved
CC in oxidative stress signaling. Prevents anthocyanin accumulation.
CC {ECO:0000250|UniProtKB:Q96EB1, ECO:0000269|PubMed:15894610,
CC ECO:0000269|PubMed:17565971, ECO:0000269|PubMed:19500300,
CC ECO:0000269|PubMed:20080602}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q96EB1}.
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 directly with ELP6 (PubMed:20080602).
CC {ECO:0000269|PubMed:20080602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96EB1}. Nucleus
CC {ECO:0000250|UniProtKB:Q96EB1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C778-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C778-2; Sequence=VSP_042838;
CC -!- TISSUE SPECIFICITY: Expressed in meristematic tissues of roots, leaves,
CC stems, seedlings, cotyledons, flowers, siliques, guard cells, floral
CC buds, and shoot apices. {ECO:0000269|PubMed:15894610,
CC ECO:0000269|PubMed:19500300, ECO:0000269|PubMed:20080602}.
CC -!- DISRUPTION PHENOTYPE: Narrow leaves and reduced root growth that
CC results from a decreased cell division rate and a reduced apical
CC dominance. Delayed germination after imbibition. Enhancement of
CC germination and inhibition of leaf growth at high sucrose
CC concentrations. Hypersensitive to abscisic acid (ABA) in seed
CC germination and seedling growth. At the cellular level, hypotonic
CC vacuole, alterations in the size of grana and starch grains in the
CC chloroplasts, and massive presence of Golgi vesicles in the cytoplasm.
CC Higher resistance to oxidative stress mediated by methyl viologen (MV)
CC that blocks electron transport during photosynthesis and by CsCl in
CC light. Accumulates anthocyanins. {ECO:0000269|PubMed:15894610,
CC ECO:0000269|PubMed:17565971, ECO:0000269|PubMed:19500300,
CC ECO:0000269|PubMed:20080602}.
CC -!- SIMILARITY: Belongs to the ELP4 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:Q96EB1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ964957; CAI79646.1; -; mRNA.
DR EMBL; AC073395; AAG50962.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75015.1; -; Genomic_DNA.
DR EMBL; AY062115; AAL32987.1; -; mRNA.
DR EMBL; BT010161; AAQ22630.1; -; mRNA.
DR RefSeq; NP_566388.2; NM_111957.5. [Q9C778-1]
DR AlphaFoldDB; Q9C778; -.
DR SMR; Q9C778; -.
DR STRING; 3702.AT3G11220.2; -.
DR iPTMnet; Q9C778; -.
DR PRIDE; Q9C778; -.
DR ProteomicsDB; 220761; -. [Q9C778-1]
DR EnsemblPlants; AT3G11220.1; AT3G11220.1; AT3G11220. [Q9C778-1]
DR GeneID; 820292; -.
DR Gramene; AT3G11220.1; AT3G11220.1; AT3G11220. [Q9C778-1]
DR KEGG; ath:AT3G11220; -.
DR Araport; AT3G11220; -.
DR eggNOG; KOG3949; Eukaryota.
DR HOGENOM; CLU_031345_2_0_1; -.
DR InParanoid; Q9C778; -.
DR OMA; NTTMWDD; -.
DR OrthoDB; 973442at2759; -.
DR PhylomeDB; Q9C778; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q9C778; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C778; baseline and differential.
DR Genevisible; Q9C778; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071329; P:cellular response to sucrose stimulus; IMP:UniProtKB.
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:0010928; P:regulation of auxin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0043609; P:regulation of carbon utilization; IMP:UniProtKB.
DR GO; GO:2000024; P:regulation of leaf development; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008728; Elongator_complex_protein_4.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12896; PTHR12896; 1.
DR Pfam; PF05625; PAXNEB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing;
KW Auxin signaling pathway; Cytoplasm; Developmental protein; Nucleus;
KW Reference proteome; tRNA processing.
FT CHAIN 1..355
FT /note="Elongator complex protein 4"
FT /id="PRO_0000416790"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 192..354
FT /note="RNSSNIASIGRIAIQSFCSPLCEYSEKESDMLSFIRLLKSMLMVSNAVAIVT
FT FPPSLLSPSSSKRLQHMADTLLSIKAIPDGDKELEKLLTGYKDINGFLNIHKVARINTQ
FT VPVILEAKTFSMSLKKRRFLALECLNQAPVDGSSGTSYGTSGSCSSKSGALD -> RLC
FT GILSYLISITRSSFESINFVGHTYAANSAQAQFFLHLSYTSKLSLFIL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_042838"
FT CONFLICT 9
FT /note="S -> I (in Ref. 1; CAI79646)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="G -> R (in Ref. 4; AAL32987/AAQ22630)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Y -> F (in Ref. 1; CAI79646)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="D -> V (in Ref. 1; CAI79646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 38731 MW; 6A3D2CC74FF94E76 CRC64;
MAAPNVRSSS SFSRNISVVS SPQIPGLKSG PNGTAFISSG IRDLDRILGG GYPLGSLVMV
MEDPEAPHHM DLLRTYMSQG LVNNQPLLYA SPSKDPKGFL GTLPHPASSK EDKPTAPDPD
QGESLRIAWQ YRKYLENQKN AIDDYSNDFD MRKPLERQFL SGRPIDCVSL LDSSDLSIAQ
DHCATFLSKF PRNSSNIASI GRIAIQSFCS PLCEYSEKES DMLSFIRLLK SMLMVSNAVA
IVTFPPSLLS PSSSKRLQHM ADTLLSIKAI PDGDKELEKL LTGYKDINGF LNIHKVARIN
TQVPVILEAK TFSMSLKKRR FLALECLNQA PVDGSSGTSY GTSGSCSSKS GALDF
