ELP2_ARATH
ID ELP2_ARATH Reviewed; 838 AA.
AC F4I1S7; O22044; Q0WVT2; Q9XIC1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Elongator complex protein 2;
DE Short=AtELP2;
DE AltName: Full=Elongator component 2;
DE AltName: Full=Protein GREEN NPR1 SEEDLING ON SA MEDIUM 1;
GN Name=ELP2; Synonyms=GNS1; OrderedLocusNames=At1g49540;
GN ORFNames=F13F21.2, F14J22.24;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 515-838.
RX PubMed=9349257; DOI=10.1023/a:1005898805326;
RA Zhu X., Suzuki K., Saito T., Okada K., Tanaka K., Nakagawa T., Matsuda H.,
RA Kawamukai M.;
RT "Geranylgeranyl pyrophosphate synthase encoded by the newly isolated gene
RT GGPS6 from Arabidopsis thaliana is localized in mitochondria.";
RL Plant Mol. Biol. 35:331-341(1997).
RN [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20807211; DOI=10.1111/j.1365-313x.2010.04345.x;
RA DeFraia C.T., Zhang X., Mou Z.;
RT "Elongator subunit 2 is an accelerator of immune responses in Arabidopsis
RT thaliana.";
RL Plant J. 64:511-523(2010).
RN [7]
RP SUBUNIT.
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. Prevents abscisic acid (ABA) signaling
CC leading to stomatal closure and seedling growth inhibition. Involved in
CC oxidative stress signaling. Prevents anthocyanin accumulation.
CC Accelerator of defense gene induction required for rapid defense gene
CC induction, and for the establishment of both basal and effector-
CC triggered immunity (ETI), in a NPR1-independent manner, but is not
CC required for systemic acquired resistance (SAR) establishment
CC (PubMed:19500300, PubMed:20807211). {ECO:0000250|UniProtKB:Q6IA86,
CC ECO:0000269|PubMed:19500300, ECO:0000269|PubMed:20807211}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- SUBUNIT: Component of the elongator complex which consists of
CC ELP1/ELO2, ELP2, ELP3/ELO3, ELP4/ELO1, ELP5, and ELP6.
CC {ECO:0000269|PubMed:20080602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6IA86}. Nucleus
CC {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=F4I1S7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, flowers,
CC siliques and guard cells. {ECO:0000269|PubMed:19500300}.
CC -!- DOMAIN: Folds into a two seven-bladed beta-propeller structure which is
CC required for elongator complex assembly.
CC {ECO:0000250|UniProtKB:P42935}.
CC -!- DISRUPTION PHENOTYPE: Narrow leaves and reduced root growth that
CC results from a decreased cell division rate. Increased abscisic acid
CC (ABA) sensitivity and drought tolerance. Higher resistance to oxidative
CC stress mediated by methyl viologen (MV) that blocks electron transport
CC during photosynthesis and by CsCl in light. Accumulates anthocyanins.
CC Reduced defense gene induction kinetics and salicylic acid (SA)
CC accumulation mediated by pathogens (e.g. Pseudomonas syringae pv.
CC maculicola) accompanied by an enhanced susceptibility in npr1 deficient
CC plants. {ECO:0000269|PubMed:19500300, ECO:0000269|PubMed:20807211}.
CC -!- MISCELLANEOUS: [Isoform 1]: No experimental confirmation available.
CC -!- SIMILARITY: Belongs to the WD repeat ELP2 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:Q6IA86}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43147.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA23158.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007504; AAD43147.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32440.1; -; Genomic_DNA.
DR EMBL; AK226658; BAE98766.1; -; mRNA.
DR EMBL; AB000835; BAA23158.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_175377.2; NM_103842.3. [F4I1S7-1]
DR AlphaFoldDB; F4I1S7; -.
DR SMR; F4I1S7; -.
DR STRING; 3702.AT1G49540.2; -.
DR PaxDb; F4I1S7; -.
DR PRIDE; F4I1S7; -.
DR ProteomicsDB; 222287; -. [F4I1S7-1]
DR EnsemblPlants; AT1G49540.1; AT1G49540.1; AT1G49540. [F4I1S7-1]
DR GeneID; 841378; -.
DR Gramene; AT1G49540.1; AT1G49540.1; AT1G49540. [F4I1S7-1]
DR KEGG; ath:AT1G49540; -.
DR Araport; AT1G49540; -.
DR eggNOG; KOG1063; Eukaryota.
DR HOGENOM; CLU_006430_2_0_1; -.
DR InParanoid; F4I1S7; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:F4I1S7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I1S7; baseline and differential.
DR Genevisible; F4I1S7; 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:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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:0031349; P:positive regulation of defense response; 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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 5.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Cytoplasm; Nucleus;
KW Plant defense; Reference proteome; Repeat; tRNA processing; WD repeat.
FT CHAIN 1..838
FT /note="Elongator complex protein 2"
FT /id="PRO_0000416789"
FT REPEAT 17..56
FT /note="WD 1"
FT REPEAT 57..107
FT /note="WD 2"
FT REPEAT 115..157
FT /note="WD 3"
FT REPEAT 174..213
FT /note="WD 4"
FT REPEAT 219..267
FT /note="WD 5"
FT REPEAT 300..352
FT /note="WD 6"
FT REPEAT 361..401
FT /note="WD 7"
FT REPEAT 411..450
FT /note="WD 8"
FT REPEAT 464..505
FT /note="WD 9"
FT REPEAT 596..640
FT /note="WD 10"
FT REPEAT 643..682
FT /note="WD 11"
FT REPEAT 692..731
FT /note="WD 12"
FT REPEAT 737..781
FT /note="WD 13"
FT REPEAT 797..835
FT /note="WD 14"
FT CONFLICT 771
FT /note="S -> W (in Ref. 4; BAA23158)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="R -> Q (in Ref. 3; BAE98766)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 838 AA; 92681 MW; DCBA74539271B5B2 CRC64;
MSENTKVEAK RVFIGAGCNR VVNNVSWGAS GLVSFGAQNA VAVFCPKTAQ ILTTLPGHKA
SVNCTHWLPT SKFAFKAKKL DRQYLLSGDS DGIIILWELS TLNNDWRHVL QLPLSHKKGV
TCITAYMVSE TDAMFASASS DGVVNVWDVS FPSQPSEECK VVCLDSICVD TKAIVTLSLA
ELPQNPGRFA LALGGLDNKI KLYSGERTGK FTSVCELKGH TDWIRSLDFS LPLHTTEEIP
NSIMLVSSSQ DKVIRIWKLV LVGDVGSWRR EITLASYIEG PVFVSGTFTY QISVESVLIG
HEDWVYSVEW QPPVIDFIDG RLVNHQPLSI LSASMDKTMM IWRPEKKTGV WVNVVCVGEL
SHCALGFYGG HWSPNSLSIL AHGYGGAFHL WRNVSSSKES ENWQMQKVPS GHFAAVTDVT
WARTGEYLLS VSQDQTTRVF SAWKNDEGNE AEDEHWHELA RPQVHGHDIN CVAMVQGKGN
HRFVSGAEEK VVRVFEAPLS FLKTLNHTCA GGEGSFPEDL QADVQVLGAN MSALGLSQKP
IYLHSSSEPL ERNGGGEGLD TFETVPEAAP AELKEPPIED QLAFHTLWPE SHKLYGHGNE
LFSLCSDHKG NLVASSCKAQ SASMAEIWLW EVGTWKAVGR LQSHSLTVTH LEFSYDDTLL
LSVSRDRHFS VFSIQRTDNG EVSHKLMAKV EAHKRIIWAC SWNPFGHQFA TSSRDKTVKI
WSVENDARIK QILVLPPFGS SVTAVAWTGL DRNEKSGCVA VGMESGLIEL SNVKIIETEE
GTTATAALAL RLEPFMCHVS AVNRLAWRPT EKCESNQSLR WLTSCGDDNC VRVFNFKF
