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ELP1_ARATH
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   03-AUG-2022, entry version 120.
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}.
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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.AT5G13680.1; -.
DR   iPTMnet; Q9FNA4; -.
DR   PaxDb; Q9FNA4; -.
DR   PRIDE; Q9FNA4; -.
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; locus:2173199; AT5G13680.
DR   eggNOG; KOG1920; Eukaryota.
DR   HOGENOM; CLU_001477_0_0_1; -.
DR   InParanoid; Q9FNA4; -.
DR   OMA; DMNILHD; -.
DR   OrthoDB; 180136at2759; -.
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:0005829; C:cytosol; IBA:GO_Central.
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:0000049; F:tRNA binding; IBA:GO_Central.
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:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR006849; Elp1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR12747; PTHR12747; 1.
DR   Pfam; PF04762; IKI3; 1.
DR   PIRSF; PIRSF017233; IKAP; 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
 
 
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