APRR5_ARATH
ID APRR5_ARATH Reviewed; 558 AA.
AC Q6LA42; F4KH52; Q9FGE3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Two-component response regulator-like APRR5;
DE AltName: Full=Pseudo-response regulator 5;
GN Name=APRR5; OrderedLocusNames=At5g24470; ORFNames=T31K7.5;
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 [MRNA], AND FUNCTION.
RX PubMed=11100772; DOI=10.1093/pcp/pcd043;
RA Matsushika A., Makino S., Kojima M., Mizuno T.;
RT "Circadian waves of expression of the APRR1/TOC1 family of pseudo-response
RT regulators in Arabidopsis thaliana: insight into the plant circadian
RT clock.";
RL Plant Cell Physiol. 41:1002-1012(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP GENE FAMILY.
RX PubMed=10945350; DOI=10.1093/pcp/41.6.791;
RA Makino S., Kiba T., Imamura A., Hanaki N., Nakamura A., Suzuki T.,
RA Taniguchi M., Ueguchi C., Sugiyama T., Mizuno T.;
RT "Genes encoding pseudo-response regulators: insight into His-to-Asp
RT phosphorelay and circadian rhythm in Arabidopsis thaliana.";
RL Plant Cell Physiol. 41:791-803(2000).
RN [6]
RP INTERACTION WITH ADO1 AND ADO2.
RX PubMed=15310821; DOI=10.1093/jxb/erh226;
RA Yasuhara M., Mitsui S., Hirano H., Takanabe R., Tokioka Y., Ihara N.,
RA Komatsu A., Seki M., Shinozaki K., Kiyosue T.;
RT "Identification of ASK and clock-associated proteins as molecular partners
RT of LKP2 (LOV kelch protein 2) in Arabidopsis.";
RL J. Exp. Bot. 55:2015-2027(2004).
RN [7]
RP INTERACTION WITH ADO1, AND PHOSPHORYLATION.
RX PubMed=18562312; DOI=10.1074/jbc.m803471200;
RA Fujiwara S., Wang L., Han L., Suh S.-S., Salome P.A., McClung C.R.,
RA Somers D.E.;
RT "Post-translational regulation of the Arabidopsis circadian clock through
RT selective proteolysis and phosphorylation of pseudo-response regulator
RT proteins.";
RL J. Biol. Chem. 283:23073-23083(2008).
RN [8]
RP FUNCTION.
RX PubMed=20233950; DOI=10.1105/tpc.109.072892;
RA Nakamichi N., Kiba T., Henriques R., Mizuno T., Chua N.H., Sakakibara H.;
RT "PSEUDO-RESPONSE REGULATORS 9, 7, and 5 are transcriptional repressors in
RT the Arabidopsis circadian clock.";
RL Plant Cell 22:594-605(2010).
RN [9]
RP FUNCTION.
RX PubMed=21357491; DOI=10.1105/tpc.110.081661;
RA Wang Y., Wu J.F., Nakamichi N., Sakakibara H., Nam H.G., Wu S.H.;
RT "LIGHT-REGULATED WD1 and PSEUDO-RESPONSE REGULATOR9 form a positive
RT feedback regulatory loop in the Arabidopsis circadian clock.";
RL Plant Cell 23:486-498(2011).
RN [10]
RP FUNCTION.
RX PubMed=21483796; DOI=10.1371/journal.pgen.1001350;
RA Rawat R., Takahashi N., Hsu P.Y., Jones M.A., Schwartz J., Salemi M.R.,
RA Phinney B.S., Harmer S.L.;
RT "REVEILLE8 and PSEUDO-RESPONSE REGULATOR5 form a negative feedback loop
RT within the Arabidopsis circadian clock.";
RL PLoS Genet. 7:E1001350-E1001350(2011).
RN [11]
RP FUNCTION.
RX PubMed=23027938; DOI=10.1073/pnas.1205156109;
RA Nakamichi N., Kiba T., Kamioka M., Suzuki T., Yamashino T., Higashiyama T.,
RA Sakakibara H., Mizuno T.;
RT "Transcriptional repressor PRR5 directly regulates clock-output pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17123-17128(2012).
RN [12]
RP FUNCTION.
RX PubMed=23333981; DOI=10.4161/psb.23534;
RA Takase M., Mizoguchi T., Kozuka T., Tsukaya H.;
RT "The unique function of the Arabidopsis circadian clock gene PRR5 in the
RT regulation of shade avoidance response.";
RL Plant Signal. Behav. 8:0-0(2013).
RN [13]
RP SUBCELLULAR LOCATION, INTERACTION WITH SPY, AND O-FUCOSYLATION.
RX PubMed=31899321; DOI=10.1016/j.molp.2019.12.013;
RA Wang Y., He Y., Su C., Zentella R., Sun T.P., Wang L.;
RT "Nuclear Localized O-Fucosyltransferase SPY Facilitates PRR5 Proteolysis to
RT Fine-Tune the Pace of Arabidopsis Circadian Clock.";
RL Mol. Plant 13:446-458(2020).
CC -!- FUNCTION: Transcriptional repressor of CCA1 and LHY, thereby
CC controlling photoperiodic flowering response. Involved in the positive
CC and negative feedback loops of the circadian clock. With RVE8, forms a
CC negative feedback loop of the circadian clock (PubMed:21483796).
CC Expression of several members of the ARR-like family is controlled by
CC circadian rhythm. Proteolytic substrate of the E3 ubiquitin ligase
CC SCF(ADO1) complex. APRR9, APRR7, and APRR5 coordinately act on the
CC upstream region of the target genes to repress their expression from
CC noon until midnight. The particular coordinated sequential expression
CC of APRR9, APRR7, APRR5, APRR3 and APPR1 result to circadian waves that
CC may be at the basis of the endogenous circadian clock. Negative
CC regulator of shade avoidance response. Involved in the inhibition of
CC leaf expansion in shade avoidance response.
CC {ECO:0000269|PubMed:11100772, ECO:0000269|PubMed:20233950,
CC ECO:0000269|PubMed:21357491, ECO:0000269|PubMed:21483796,
CC ECO:0000269|PubMed:23027938, ECO:0000269|PubMed:23333981}.
CC -!- SUBUNIT: Interacts with ADO1 and ADO2 (PubMed:15310821,
CC PubMed:18562312). Interacts with SPY (via N-terminus)
CC (PubMed:31899321). {ECO:0000269|PubMed:15310821,
CC ECO:0000269|PubMed:18562312, ECO:0000269|PubMed:31899321}.
CC -!- INTERACTION:
CC Q6LA42; Q9LKL2: APRR1; NbExp=5; IntAct=EBI-1536669, EBI-618423;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31899321}.
CC -!- PTM: Phosphorylation varies throughout the diurnal cycle and enhances
CC ADO1 binding. {ECO:0000269|PubMed:18562312}.
CC -!- PTM: O-fucosylated by SPY (PubMed:31899321). O-fucosylation promotes
CC APRR5 proteolysis (PubMed:31899321). {ECO:0000269|PubMed:31899321}.
CC -!- MISCELLANEOUS: The expression of APRR9, APRR7, and APRR5 requires the
CC presence of LWD1 and/or LWD2, indicating the existence of a positive
CC feedback loop within the circadian clock.
CC {ECO:0000305|PubMed:21357491}.
CC -!- SIMILARITY: Belongs to the ARR-like family. {ECO:0000305}.
CC -!- CAUTION: Lacks the phospho-accepting Asp (here Glu-102), present in the
CC receiver domain, which is one of the conserved features of two-
CC component response regulators (ARRs) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13743.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AB046955; BAB13743.1; ALT_INIT; mRNA.
DR EMBL; AB025641; BAB08930.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93314.2; -; Genomic_DNA.
DR EMBL; AY062114; AAL32986.1; -; mRNA.
DR EMBL; AY143934; AAN28873.1; -; mRNA.
DR RefSeq; NP_568446.2; NM_122355.4.
DR AlphaFoldDB; Q6LA42; -.
DR SMR; Q6LA42; -.
DR BioGRID; 17793; 28.
DR IntAct; Q6LA42; 3.
DR MINT; Q6LA42; -.
DR STRING; 3702.AT5G24470.1; -.
DR iPTMnet; Q6LA42; -.
DR PaxDb; Q6LA42; -.
DR PRIDE; Q6LA42; -.
DR ProteomicsDB; 244453; -.
DR EnsemblPlants; AT5G24470.1; AT5G24470.1; AT5G24470.
DR GeneID; 832518; -.
DR Gramene; AT5G24470.1; AT5G24470.1; AT5G24470.
DR KEGG; ath:AT5G24470; -.
DR Araport; AT5G24470; -.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_015512_2_0_1; -.
DR InParanoid; Q6LA42; -.
DR OMA; ERPTLWH; -.
DR OrthoDB; 926211at2759; -.
DR PhylomeDB; Q6LA42; -.
DR PRO; PR:Q6LA42; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6LA42; baseline and differential.
DR Genevisible; Q6LA42; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR045279; ARR-like.
DR InterPro; IPR010402; CCT_domain.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43874; PTHR43874; 2.
DR Pfam; PF06203; CCT; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51017; CCT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Biological rhythms; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..558
FT /note="Two-component response regulator-like APRR5"
FT /id="PRO_0000081437"
FT DOMAIN 51..169
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 509..551
FT /note="CCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00357"
FT REGION 180..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 240..260
FT /evidence="ECO:0000255"
FT COMPBIAS 180..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 62301 MW; 9813089FA9DC8CE9 CRC64;
MTSSEEVVEV TVVKAPEAGG GKLSRRKIRK KDAGVDGLVK WERFLPKIAL RVLLVEADDS
TRQIIAALLR KCSYRVAAVP DGLKAWEMLK GKPESVDLIL TEVDLPSISG YALLTLIMEH
DICKNIPVIM MSTQDSVNTV YKCMLKGAAD YLVKPLRRNE LRNLWQHVWR RQTSLAPDSF
PWNESVGQQK AEGASANNSN GKRDDHVVSG NGGDAQSSCT RPEMEGESAD VEVSARDAVQ
MECAKSQFNE TRLLANELQS KQAEAIDFMG ASFRRTGRRN REESVAQYES RIELDLSLRR
PNASENQSSG DRPSLHPSSA SAFTRYVHRP LQTQCSASPV VTDQRKNVAA SQDDNIVLMN
QYNTSEPPPN APRRNDTSFY TGADSPGPPF SNQLNSWPGQ SSYPTPTPIN NIQFRDPNTA
YTSAMAPASL SPSPSSVSPH EYSSMFHPFN SKPEGLQDRD CSMDVDERRY VSSATEHSAI
GNHIDQLIEK KNEDGYSLSV GKIQQSLQRE AALTKFRMKR KDRCYEKKVR YESRKKLAEQ
RPRIKGQFVR QVQSTQAP
