RUP1_ARATH
ID RUP1_ARATH Reviewed; 385 AA.
AC Q9LTJ6; Q8LBH5;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=WD repeat-containing protein RUP1 {ECO:0000303|PubMed:21041653};
DE AltName: Full=Protein EARLY FLOWERING BY OVEREXPRESSION 1 {ECO:0000303|PubMed:21242318};
DE AltName: Full=Protein REPRESSOR OF UV-B PHOTOMORPHOGENESIS 1 {ECO:0000303|PubMed:21041653};
GN Name=RUP1 {ECO:0000303|PubMed:21041653};
GN Synonyms=EFO1 {ECO:0000303|PubMed:21242318};
GN OrderedLocusNames=At5g52250 {ECO:0000312|Araport:AT5G52250};
GN ORFNames=F17P19.15 {ECO:0000312|EMBL:BAA97468.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INTERACTION WITH UVR8, SUBCELLULAR LOCATION, AND INDUCTION BY
RP UV-B.
RC STRAIN=cv. Columbia;
RX PubMed=21041653; DOI=10.1073/pnas.0914532107;
RA Gruber H., Heijde M., Heller W., Albert A., Seidlitz H.K., Ulm R.;
RT "Negative feedback regulation of UV-B-induced photomorphogenesis and stress
RT acclimation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20132-20137(2010).
RN [7]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=21242318; DOI=10.1093/jxb/erq336;
RA Wang W., Yang D., Feldmann K.A.;
RT "EFO1 and EFO2, encoding putative WD-domain proteins, have overlapping and
RT distinct roles in the regulation of vegetative development and flowering of
RT Arabidopsis.";
RL J. Exp. Bot. 62:1077-1088(2011).
RN [8]
RP INTERACTION WITH UVR8.
RX PubMed=22988111; DOI=10.1073/pnas.1210898109;
RA Cloix C., Kaiserli E., Heilmann M., Baxter K.J., Brown B.A., O'Hara A.,
RA Smith B.O., Christie J.M., Jenkins G.I.;
RT "C-terminal region of the UV-B photoreceptor UVR8 initiates signaling
RT through interaction with the COP1 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16366-16370(2012).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH DHU1.
RC STRAIN=cv. Columbia;
RX PubMed=28735869; DOI=10.1016/j.bbrc.2017.07.110;
RA Kim S.-H., Kim H., Chung S., Lee J.-H.;
RT "DHU1 negatively regulates UV-B signaling via its direct interaction with
RT COP1 and RUP1.";
RL Biochem. Biophys. Res. Commun. 491:285-290(2017).
CC -!- FUNCTION: Functions in association with RUP2 as repressor of UV-B-
CC induced photomorphogenesis mediated by UVR8 and HY5, likely in
CC coordination with DHU1 (PubMed:28735869). Plays a crucial negative
CC feedback regulatory role downstream of UVR8-COP1 to inhibit UVR8
CC function, balance UV-B-specific responses and ensure normal plant
CC growth. Is involved in the regulation of photoperiodic flowering and
CC vegetative development. {ECO:0000269|PubMed:21041653,
CC ECO:0000269|PubMed:21242318, ECO:0000269|PubMed:28735869}.
CC -!- SUBUNIT: Interacts with UVR8 (PubMed:21041653, PubMed:22988111).
CC Interacts directly with DHU1 (PubMed:28735869).
CC {ECO:0000269|PubMed:21041653, ECO:0000269|PubMed:22988111,
CC ECO:0000269|PubMed:28735869}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21041653}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:21041653}.
CC -!- INDUCTION: Circadian-regulation. Expression increases during the dark
CC phase with a peak at the beginning of the light phase and then
CC decreases to reach the lowest expression at the end of the light phase.
CC Induced by UV-B. {ECO:0000269|PubMed:21041653,
CC ECO:0000269|PubMed:21242318}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:21242318). The UV-B responsiveness of the double
CC mutant dhu1-1 rup1-1 is similar to that of the single mutants dhu1-1
CC and rup1-1 (PubMed:28735869). {ECO:0000269|PubMed:21242318,
CC ECO:0000269|PubMed:28735869}.
CC -!- MISCELLANEOUS: Overexpression of RUP1 confers an early flowering
CC phenotype. {ECO:0000305|PubMed:21242318}.
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DR EMBL; AB025603; BAA97468.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96192.1; -; Genomic_DNA.
DR EMBL; BT003150; AAO24582.1; -; mRNA.
DR EMBL; AK228112; BAF00070.1; -; mRNA.
DR EMBL; AY087205; AAM64761.1; -; mRNA.
DR RefSeq; NP_200038.1; NM_124604.5.
DR AlphaFoldDB; Q9LTJ6; -.
DR SMR; Q9LTJ6; -.
DR BioGRID; 20546; 1.
DR DIP; DIP-60744N; -.
DR IntAct; Q9LTJ6; 1.
DR STRING; 3702.AT5G52250.1; -.
DR iPTMnet; Q9LTJ6; -.
DR PaxDb; Q9LTJ6; -.
DR PRIDE; Q9LTJ6; -.
DR ProteomicsDB; 228059; -.
DR EnsemblPlants; AT5G52250.1; AT5G52250.1; AT5G52250.
DR GeneID; 835301; -.
DR Gramene; AT5G52250.1; AT5G52250.1; AT5G52250.
DR KEGG; ath:AT5G52250; -.
DR Araport; AT5G52250; -.
DR TAIR; locus:2145111; AT5G52250.
DR eggNOG; ENOG502QVDX; Eukaryota.
DR HOGENOM; CLU_006994_0_2_1; -.
DR InParanoid; Q9LTJ6; -.
DR OMA; QVDEDWC; -.
DR OrthoDB; 857220at2759; -.
DR PhylomeDB; Q9LTJ6; -.
DR PRO; PR:Q9LTJ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTJ6; baseline and differential.
DR Genevisible; Q9LTJ6; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IDA:TAIR.
DR GO; GO:0010218; P:response to far red light; IEP:TAIR.
DR GO; GO:0010114; P:response to red light; IEP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IGI:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR044616; RUP1/2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR45389; PTHR45389; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Flowering; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..385
FT /note="WD repeat-containing protein RUP1"
FT /id="PRO_0000421720"
FT REPEAT 69..108
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 119..160
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 163..205
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 210..250
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 254..292
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 298..337
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 348..385
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT CONFLICT 117
FT /note="Y -> C (in Ref. 5; AAM64761)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="I -> L (in Ref. 5; AAM64761)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="R -> Q (in Ref. 5; AAM64761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 41997 MW; 6D2C3F5ED02164AC CRC64;
MEALFCSEIP NNNIRSSIND LSSSSSYTWP MIMTSSSSSS SSPTIMNIEN IPRCDWDLSL
SAVVSSASTG SDAIGAIEFD PTGEIIATGG IARKIRSYRL SSLLESRDDH VTASESYICT
PAKLSSLKWR PDFSGRVIGS GDYDGVVTEY DVEKQVPVSE RDEHGGRRIW SVDYTLYNGS
LIGASGSDDG TVQMWDPRNG GTLEETVRPG GGAAICSVEF DPFGGSSIAV GCADRNAYVY
DIRRLVDPLI VLDGHTKTVT YARFMDSHTI VTGSTDGSLK QWDIDNGRRV VRTYRGHVNS
RNFVGLSVWR HGGLVVSGSE NNQVFVYDKR WEEPVWVCGL GHTNRFGSDR RFVSSVCLRQ
VDEDWCTLVA GGSDGALEIF SGKQS
