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RVE1_ARATH
ID   RVE1_ARATH              Reviewed;         387 AA.
AC   F4KGY6; Q93WC6; Q9FFI1;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Protein REVEILLE 1;
GN   Name=RVE1; OrderedLocusNames=At5g17300; ORFNames=MKP11.15;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-387.
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   [4]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19805390; DOI=10.1073/pnas.0813035106;
RA   Rawat R., Schwartz J., Jones M.A., Sairanen I., Cheng Y., Andersson C.R.,
RA   Zhao Y., Ljung K., Harmer S.L.;
RT   "REVEILLE1, a Myb-like transcription factor, integrates the circadian clock
RT   and auxin pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16883-16888(2009).
RN   [5]
RP   FUNCTION, INDUCTION BY COLD, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=23240770; DOI=10.1111/pce.12054;
RA   Meissner M., Orsini E., Ruschhaupt M., Melchinger A.E., Hincha D.K.,
RA   Heyer A.G.;
RT   "Mapping quantitative trait loci for freezing tolerance in a recombinant
RT   inbred line population of Arabidopsis thaliana accessions Tenela and C24
RT   reveals REVEILLE1 as negative regulator of cold acclimation.";
RL   Plant Cell Environ. 36:1256-1267(2013).
CC   -!- FUNCTION: Morning-phased transcription factor integrating the circadian
CC       clock and auxin pathways. Binds to the evening element (EE) of
CC       promoters. Does not act within the central clock, but regulates free
CC       auxin levels in a time-of-day specific manner. Positively regulates the
CC       expression of YUC8 during the day, but has no effect during the night.
CC       Negative regulator of freezing tolerance. {ECO:0000269|PubMed:19805390,
CC       ECO:0000269|PubMed:23240770}.
CC   -!- INTERACTION:
CC       F4KGY6; Q9XGN1: TTG1; NbExp=4; IntAct=EBI-15194459, EBI-395803;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC   -!- INDUCTION: Circadian-regulation. Peak of transcript abundance near
CC       subjective dawn. Down-regulated and strongly decreased amplitude of
CC       circadian oscillation upon cold treatment.
CC       {ECO:0000269|PubMed:19805390, ECO:0000269|PubMed:23240770}.
CC   -!- DISRUPTION PHENOTYPE: No effect on the regulation of core clock
CC       associated genes, but shorter hypocotyl length and higher freezing
CC       tolerance. Rve1 and rve2 double mutant has no alteration in the period
CC       or phase of the clock. Rve1, rve2 and rve7 triple mutant has no
CC       alteration in the period or phase of the clock.
CC       {ECO:0000269|PubMed:19805390, ECO:0000269|PubMed:23240770}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK55663.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB10517.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB005238; BAB10517.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92410.1; -; Genomic_DNA.
DR   EMBL; AF378860; AAK55663.1; ALT_INIT; mRNA.
DR   EMBL; AY050467; AAK91480.1; -; mRNA.
DR   RefSeq; NP_568344.2; NM_121736.3.
DR   AlphaFoldDB; F4KGY6; -.
DR   SMR; F4KGY6; -.
DR   BioGRID; 16871; 51.
DR   IntAct; F4KGY6; 44.
DR   STRING; 3702.AT5G17300.1; -.
DR   PaxDb; F4KGY6; -.
DR   PRIDE; F4KGY6; -.
DR   ProteomicsDB; 228042; -.
DR   EnsemblPlants; AT5G17300.1; AT5G17300.1; AT5G17300.
DR   GeneID; 831595; -.
DR   Gramene; AT5G17300.1; AT5G17300.1; AT5G17300.
DR   KEGG; ath:AT5G17300; -.
DR   Araport; AT5G17300; -.
DR   TAIR; locus:2167210; AT5G17300.
DR   eggNOG; KOG0724; Eukaryota.
DR   HOGENOM; CLU_030536_0_0_1; -.
DR   InParanoid; F4KGY6; -.
DR   OrthoDB; 1118093at2759; -.
DR   PRO; PR:F4KGY6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KGY6; baseline and differential.
DR   Genevisible; F4KGY6; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:TAIR.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR   GO; GO:0010600; P:regulation of auxin biosynthetic process; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR006447; Myb_dom_plants.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR   PROSITE; PS51294; HTH_MYB; 1.
PE   1: Evidence at protein level;
KW   Biological rhythms; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..387
FT                   /note="Protein REVEILLE 1"
FT                   /id="PRO_0000424835"
FT   DOMAIN          50..104
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        77..100
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  42981 MW;  FFA9AF9E52ECB33F CRC64;
     MASSPLTANV QGTNASLRNR DEETADKQIQ FNDQSFGGND YAPKVRKPYT ITKERERWTD
     EEHKKFVEAL KLYGRAWRRI EEHVGSKTAV QIRSHAQKFF SKVAREATGG DGSSVEPIVI
     PPPRPKRKPA HPYPRKFGNE ADQTSRSVSP SERDTQSPTS VLSTVGSEAL CSLDSSSPNR
     SLSPVSSASP PAALTTTANA PEELETLKLE LFPSERLLNR ESSIKEPTKQ SLKLFGKTVL
     VSDSGMSSSL TTSTYCKSPI QPLPRKLSSS KTLPIIRNSQ EELLSCWIQV PLKQEDVENR
     CLDSGKAVQN EGSSTGSNTG SVDDTGHTEK TTEPETMLCQ WEFKPSERSA FSELRRTNSE
     SNSRGFGPYK KRKMVTEEEE HEIHLHL
 
 
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