ID ELP1_ARATH Reviewed; 1319 AA.
AC Q9FNA4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 127.
DE RecName: Full=Elongator complex protein 1;
DE Short=AtELP1;
DE AltName: Full=Elongator component 1;
DE AltName: Full=Protein ABA-OVERLY SENSITIVE 1;
DE AltName: Full=Protein ELONGATA 2;
GN Name=ELP1; Synonyms=ABO1, ELO2; OrderedLocusNames=At5g13680;
GN ORFNames=MSH12.15;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16943431; DOI=10.1128/mcb.00433-06;
RA Chen Z., Zhang H., Jablonowski D., Zhou X., Ren X., Hong X., Schaffrath R.,
RA Zhu J.-K., Gong Z.;
RT "Mutations in ABO1/ELO2, a subunit of holo-Elongator, increase abscisic
RT acid sensitivity and drought tolerance in Arabidopsis thaliana.";
RL Mol. Cell. Biol. 26:6902-6912(2006).
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, SUBUNIT, 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).
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. Required for auxin distribution or
CC signaling. Prevents abscisic acid (ABA) signaling leading to stomatal
CC closure and seedling growth inhibition. Involved in oxidative stress
CC signaling. Prevents anthocyanin accumulation.
CC {ECO:0000250|UniProtKB:O95163, ECO:0000269|PubMed:15894610,
CC ECO:0000269|PubMed:16943431, ECO:0000269|PubMed:19500300,
CC ECO:0000269|PubMed:20080602}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:O95163}.
CC -!- SUBUNIT: Homodimer (By similarity). Component of the elongator complex
CC which consists of ELP1/ELO2, ELP2, ELP3/ELO3, ELP4/ELO1, ELP5, and
CC ELP6. {ECO:0000250|UniProtKB:O95163, ECO:0000269|PubMed:20080602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in meristematic tissues of in roots,
CC stems, leaves, seedlings, cotyledons, guard cells, floral buds,
CC flowers, siliques, and shoot apices. {ECO:0000269|PubMed:15894610,
CC ECO:0000269|PubMed:16943431, ECO:0000269|PubMed:19500300,
CC 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. Increased abscisic acid (ABA) sensitivity and drought
CC tolerance. Higher resistance to oxidative stress mediated by methyl
CC viologen (MV) that blocks electron transport during photosynthesis and
CC by CsCl in light. Accumulates anthocyanins.
CC {ECO:0000269|PubMed:15894610, ECO:0000269|PubMed:16943431,
CC ECO:0000269|PubMed:19500300, ECO:0000269|PubMed:20080602}.
CC -!- SIMILARITY: Belongs to the ELP1/IKA1 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:O95163}.
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; AB006704; BAB08695.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91927.1; -; Genomic_DNA.
DR RefSeq; NP_196872.1; NM_121371.3.
DR AlphaFoldDB; Q9FNA4; -.
DR SMR; Q9FNA4; -.
DR STRING; 3702.Q9FNA4; -.
DR iPTMnet; Q9FNA4; -.
DR PaxDb; 3702-AT5G13680-1; -.
DR ProteomicsDB; 222320; -.
DR EnsemblPlants; AT5G13680.1; AT5G13680.1; AT5G13680.
DR GeneID; 831213; -.
DR Gramene; AT5G13680.1; AT5G13680.1; AT5G13680.
DR KEGG; ath:AT5G13680; -.
DR Araport; AT5G13680; -.
DR TAIR; AT5G13680; ABO1.
DR eggNOG; KOG1920; Eukaryota.
DR HOGENOM; CLU_001477_0_0_1; -.
DR InParanoid; Q9FNA4; -.
DR OMA; WRESLYC; -.
DR OrthoDB; 316709at2759; -.
DR PhylomeDB; Q9FNA4; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q9FNA4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNA4; baseline and differential.
DR Genevisible; Q9FNA4; 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:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0080178; P:5-carbamoylmethyl uridine residue modification; IMP:TAIR.
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:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:UniProtKB.
DR GO; GO:0048530; P:fruit morphogenesis; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0031538; P:negative regulation of anthocyanin metabolic process; IMP:UniProtKB.
DR GO; GO:0035265; P:organ growth; IMP:TAIR.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010928; P:regulation of auxin mediated signaling pathway; 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:0006400; P:tRNA modification; IMP:TAIR.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 1.25.40.470; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR006849; Elp1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR12747; ELONGATOR COMPLEX PROTEIN 1; 1.
DR PANTHER; PTHR12747:SF0; ELONGATOR COMPLEX PROTEIN 1; 1.
DR Pfam; PF04762; IKI3; 1.
DR PIRSF; PIRSF017233; IKAP; 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Auxin signaling pathway; Cytoplasm;
KW Nucleus; Reference proteome; Repeat; tRNA processing; WD repeat.
FT CHAIN 1..1319
FT /note="Elongator complex protein 1"
FT /id="PRO_0000416788"
FT REPEAT 73..112
FT /note="WD 1"
FT REPEAT 171..217
FT /note="WD 2"
FT REPEAT 272..314
FT /note="WD 3"
FT REPEAT 316..339
FT /note="WD 4"
FT REPEAT 521..561
FT /note="WD 5"
FT REPEAT 640..685
FT /note="WD 6"
FT REPEAT 1265..1302
FT /note="WD 7"
FT REGION 884..1319
FT /note="Mediates dimerization"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT REGION 1188..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1319 AA; 146626 MW; A3E276897220AFB1 CRC64;
MKNLKLFSEV PQNIQLHSTE EVVQFAAYDI DQSRLFFASS ANFVYALQLS SFQNESAGAK
SAMPVEVCSI DIEPGDFITA FDYLAEKESL LIGTSHGLLL VHNVESDVTE LVGNIEGGVK
CISPNPTGDL LGLITGLGQL LVMTYDWALM YEKALGEVPE GGYVRETNDL SVNCGGISIS
WRGDGKYFAT MGEVYESGCM SKKIKIWESD SGALQSSSET KEFTQGILEW MPSGAKIAAV
YKRKSDDSSP SIAFFERNGL ERSSFRIGEP EDATESCENL KWNSASDLLA GVVSCKTYDA
IRVWFFSNNH WYLKQEIRYP REAGVTVMWD PTKPLQLICW TLSGQVSVRH FMWVTAVMED
STAFVIDNSK ILVTPLSLSL MPPPMYLFSL SFSSAVRDIA YYSRNSKNCL AVFLSDGNLS
FVEFPAPNTW EDLEGKDFSV EISDCKTALG SFVHLLWLDV HSLLCVSAYG SSHNKCLSSG
GYDTELHGSY LQEVEVVCHE DHVPDQVTCS GFKASITFQT LLESPVLALA WNPSKRDSAF
VEFEGGKVLG YASRSEIMET RSSDDSVCFP STCPWVRVAQ VDASGVHKPL ICGLDDMGRL
SINGKNLCNN CSSFSFYSEL ANEVVTHLII LTKQDFLFIV DTKDVLNGDV ALGNVFFVID
GRRRDEENMS YVNIWERGAK VIGVLNGDEA AVILQTMRGN LECIYPRKLV LSSITNALAQ
QRFKDAFNLV RRHRIDFNVI VDLYGWQAFL QSAVAFVEQV NNLNHVTEFV CAMKNEDVTE
TLYKKFSFSK KGDEVFRVKD SCSNKVSSVL QAIRKALEEH IPESPSRELC ILTTLARSDP
PAIEESLLRI KSVREMELLN SSDDIRKKSC PSAEEALKHL LWLLDSEAVF EAALGLYDLN
LAAIVALNSQ RDPKEFLPYL QELEKMPESL MHFKIDIKLQ RFDSALRNIV SAGVGYFPDC
MNLIKKNPQL FPLGLLLITD PEKKLVVLEA WADHLIDEKR FEDAATTYLC CCKLEKASKA
YRECGDWSGV LRVGALMKLG KDEILKLAYE LCEEVNALGK PAEAAKIALE YCSDISGGIS
LLINAREWEE ALRVAFLHTA DDRISVVKSS ALECASGLVS EFKESIEKVG KYLTRYLAVR
QRRLLLAAKL KSEERSVVDL DDDTASEASS NLSGMSAYTL GTRRGSAASV SSSNATSRAR
DLRRQRKSGK IRAGSAGEEM ALVDHLKGMR MTDGGKRELK SLLICLVTLG EMESAQKLQQ
TAENFQVSQV AAVELAHDTV SSESVDEEVY CFERYAQKTR STARDSDAFS WMLKVFISP
//
