APRR1_ARATH
ID APRR1_ARATH Reviewed; 618 AA.
AC Q9LKL2; Q9M4B7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Two-component response regulator-like APRR1;
DE AltName: Full=ABI3-interacting protein 1;
DE AltName: Full=Pseudo-response regulator 1;
DE AltName: Full=Timing of CAB expression 1;
GN Name=APRR1; Synonyms=AIP1, TOC1; OrderedLocusNames=At5g61380;
GN ORFNames=MFB13.16;
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], CHARACTERIZATION, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF ALA-562.
RC STRAIN=cv. Columbia;
RX PubMed=10926537; DOI=10.1126/science.289.5480.768;
RA Strayer C., Oyama T., Schultz T.F., Raman R., Somers D.E., Mas P.,
RA Panda S., Kreps J.A., Kay S.A.;
RT "Cloning of the Arabidopsis clock gene TOC1, an autoregulatory response
RT regulator homolog.";
RL Science 289:768-771(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH ABI3.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10743655; DOI=10.1046/j.1365-313x.2000.00663.x;
RA Kurup S., Jones H.D., Holdsworth M.J.;
RT "Interactions of the developmental regulator ABI3 with proteins identified
RT from developing Arabidopsis seeds.";
RL Plant J. 21:143-155(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [5]
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 [6]
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 [7]
RP 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 [8]
RP INDUCTION.
RX PubMed=11486091; DOI=10.1126/science.1061320;
RA Alabadi D., Oyama T., Yanovsky M.J., Harmon F.G., Mas P., Kay S.A.;
RT "Reciprocal regulation between TOC1 and LHY/CCA1 within the Arabidopsis
RT circadian clock.";
RL Science 293:880-883(2001).
RN [9]
RP INTERACTION WITH PIF1.
RX PubMed=11828023; DOI=10.1093/pcp/pcf005;
RA Makino S., Matsushika A., Kojima M., Yamashino T., Mizuno T.;
RT "The APRR1/TOC1 quintet implicated in circadian rhythms of Arabidopsis
RT thaliana: I. Characterization with APRR1-overexpressing plants.";
RL Plant Cell Physiol. 43:58-69(2002).
RN [10]
RP INTERACTION WITH PIF1; PIL2; PIF3; PIF4; PIL5 AND PIL6.
RX PubMed=12826627; DOI=10.1093/pcp/pcg078;
RA Yamashino T., Matsushika A., Fujimori T., Sato S., Kato T., Tabata S.,
RA Mizuno T.;
RT "A link between circadian-controlled bHLH factors and the APRR1/TOC1
RT quintet in Arabidopsis thaliana.";
RL Plant Cell Physiol. 44:619-629(2003).
RN [11]
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 [12]
RP INTERACTION WITH ADO1.
RX PubMed=16428597; DOI=10.1104/pp.105.074864;
RA Kevei E., Gyula P., Hall A., Kozma-Bognar L., Kim W.Y., Eriksson M.E.,
RA Toth R., Hanano S., Feher B., Southern M.M., Bastow R.M., Viczian A.,
RA Hibberd V., Davis S.J., Somers D.E., Nagy F., Millar A.J.;
RT "Forward genetic analysis of the circadian clock separates the multiple
RT functions of ZEITLUPE.";
RL Plant Physiol. 140:933-945(2006).
RN [13]
RP TISSUE SPECIFICITY, AND INTERACTION WITH APRR3.
RX PubMed=18055606; DOI=10.1105/tpc.107.054775;
RA Para A., Farre E.M., Imaizumi T., Pruneda-Paz J.L., Harmon F.G., Kay S.A.;
RT "PRR3 Is a vascular regulator of TOC1 stability in the Arabidopsis
RT circadian clock.";
RL Plant Cell 19:3462-3473(2007).
RN [14]
RP PHOSPHORYLATION, INDUCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ADO1
RP AND APRR3.
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 [15]
RP ACTIVITY REGULATION.
RX PubMed=18433436; DOI=10.1111/j.1365-313x.2008.03527.x;
RA Harmon F., Imaizumi T., Gray W.M.;
RT "CUL1 regulates TOC1 protein stability in the Arabidopsis circadian
RT clock.";
RL Plant J. 55:568-579(2008).
RN [16]
RP FUNCTION, AND INTERACTION WITH TCP21.
RX PubMed=19286557; DOI=10.1126/science.1167206;
RA Pruneda-Paz J.L., Breton G., Para A., Kay S.A.;
RT "A functional genomics approach reveals CHE as a component of the
RT Arabidopsis circadian clock.";
RL Science 323:1481-1485(2009).
CC -!- FUNCTION: Controls photoperiodic flowering response. Component of the
CC circadian clock. Expression of several members of the ARR-like family
CC is controlled by circadian rhythm. The particular coordinated
CC sequential expression of APRR9, APRR7, APRR5, APRR3 and APPR1 result to
CC circadian waves that may be at the basis of the endogenous circadian
CC clock. Positive regulator of CCA1 and LHY expression.
CC {ECO:0000269|PubMed:11100772, ECO:0000269|PubMed:19286557}.
CC -!- SUBUNIT: Interacts with PIF1, PIL2, PIF3, PIF4, PIL5, PIL6, ABI3 (via
CC C-terminus), ADO1/ZTL, ADO2, APRR3 and TCP21/CHE. Both the
CC phosphorylated and the dephosphorylated forms interact with ADO1/ZLT.
CC {ECO:0000269|PubMed:10743655, ECO:0000269|PubMed:11828023,
CC ECO:0000269|PubMed:12826627, ECO:0000269|PubMed:15310821,
CC ECO:0000269|PubMed:16428597, ECO:0000269|PubMed:18055606,
CC ECO:0000269|PubMed:18562312, ECO:0000269|PubMed:19286557}.
CC -!- INTERACTION:
CC Q9LKL2; Q94BT6: ADO1; NbExp=7; IntAct=EBI-618423, EBI-300691;
CC Q9LKL2; Q9LVG4: APRR3; NbExp=3; IntAct=EBI-618423, EBI-1606968;
CC Q9LKL2; Q6LA42: APRR5; NbExp=5; IntAct=EBI-618423, EBI-1536669;
CC Q9LKL2; Q17TI5: BRX; NbExp=3; IntAct=EBI-618423, EBI-4426649;
CC Q9LKL2; Q9M1R4: IAA30; NbExp=3; IntAct=EBI-618423, EBI-3946710;
CC Q9LKL2; Q8L4B2: NFYC9; NbExp=3; IntAct=EBI-618423, EBI-2466050;
CC Q9LKL2; Q8L5W8: PIL1; NbExp=3; IntAct=EBI-618423, EBI-630752;
CC Q9LKL2; Q9XGN1: TTG1; NbExp=4; IntAct=EBI-618423, EBI-395803;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00357,
CC ECO:0000269|PubMed:18562312}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers and siliques.
CC Restricted to the vasculature. {ECO:0000269|PubMed:10743655,
CC ECO:0000269|PubMed:18055606}.
CC -!- INDUCTION: Expressed with a circadian rhythm showing a broad peak in
CC the late day and early night. Negatively regulated by LHY and CCA1.
CC {ECO:0000269|PubMed:11486091, ECO:0000269|PubMed:18562312}.
CC -!- DOMAIN: The N-terminus (1-243) is required for interactions with
CC ADO1/ZTL and APRR3.
CC -!- PTM: Phosphorylated; during the day. Phosphorylation is required for
CC optimal interaction with APRR3. {ECO:0000269|PubMed:18562312}.
CC -!- MISCELLANEOUS: Subject of targeted degradation by the 26S proteasome.
CC ZEITLUPE (ADO1/ZTL) is the F-box protein that associates with the SCF
CC (for Skp/Cullin/F-box) E3 ubiquitin ligase that is responsible for
CC marking APRR1/TOC1 for turnover. CUL1 is the functional cullin for the
CC SCF(ZTL) complex. APRR3 binding competitively inhibits the ADO1/ZTL
CC interaction.
CC -!- SIMILARITY: Belongs to the ARR-like family. {ECO:0000305}.
CC -!- CAUTION: Lacks the phospho-accepting Asp (here Glu-71), present in the
CC receiver domain, which is one of the conserved features of the two-
CC component response regulators (ARRs) family. {ECO:0000305}.
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DR EMBL; AB041530; BAA94547.1; -; mRNA.
DR EMBL; AF272039; AAF86252.1; -; mRNA.
DR EMBL; AJ251086; CAB75508.1; -; mRNA.
DR EMBL; AB010073; BAB08493.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97460.1; -; Genomic_DNA.
DR EMBL; AY094393; AAM19772.1; -; mRNA.
DR EMBL; BT005816; AAO64751.1; -; mRNA.
DR PIR; T52075; T52075.
DR PIR; T52076; T52076.
DR RefSeq; NP_200946.1; NM_125531.4.
DR AlphaFoldDB; Q9LKL2; -.
DR SMR; Q9LKL2; -.
DR BioGRID; 21503; 50.
DR DIP; DIP-33896N; -.
DR IntAct; Q9LKL2; 43.
DR MINT; Q9LKL2; -.
DR STRING; 3702.AT5G61380.1; -.
DR PaxDb; Q9LKL2; -.
DR PRIDE; Q9LKL2; -.
DR ProteomicsDB; 244410; -.
DR EnsemblPlants; AT5G61380.1; AT5G61380.1; AT5G61380.
DR GeneID; 836259; -.
DR Gramene; AT5G61380.1; AT5G61380.1; AT5G61380.
DR KEGG; ath:AT5G61380; -.
DR Araport; AT5G61380; -.
DR TAIR; locus:2163198; AT5G61380.
DR eggNOG; KOG1601; Eukaryota.
DR HOGENOM; CLU_041215_0_0_1; -.
DR InParanoid; Q9LKL2; -.
DR OMA; NGQDPPL; -.
DR OrthoDB; 952254at2759; -.
DR PhylomeDB; Q9LKL2; -.
DR PRO; PR:Q9LKL2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LKL2; baseline and differential.
DR Genevisible; Q9LKL2; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR GO; GO:0010031; P:circumnutation; IMP:TAIR.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; IEA:InterPro.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:TAIR.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:TAIR.
DR GO; GO:0006351; P:transcription, DNA-templated; TAS:UniProtKB.
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; 1.
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; Flowering; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Two-component regulatory system.
FT CHAIN 1..618
FT /note="Two-component response regulator-like APRR1"
FT /id="PRO_0000081435"
FT DOMAIN 20..138
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 533..575
FT /note="CCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00357"
FT REGION 161..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 588..610
FT /evidence="ECO:0000255"
FT COMPBIAS 161..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..609
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 562
FT /note="A->V: In toc1-1; causes shortened circadian rhythms
FT in light-grown plants."
FT /evidence="ECO:0000269|PubMed:10926537"
FT CONFLICT 126
FT /note="R -> L (in Ref. 2; CAB75508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 69195 MW; EDBE0AA0B7FAB61E CRC64;
MDLNGECKGG DGFIDRSRVR ILLCDNDSTS LGEVFTLLSE CSYQVTAVKS ARQVIDALNA
EGPDIDIILA EIDLPMAKGM KMLRYITRDK DLRRIPVIMM SRQDEVPVVV KCLKLGAADY
LVKPLRTNEL LNLWTHMWRR RRMLGLAEKN MLSYDFDLVG SDQSDPNTNS TNLFSDDTDD
RSLRSTNPQR GNLSHQENEW SVATAPVHAR DGGLGADGTA TSSLAVTAIE PPLDHLAGSH
HEPMKRNSNP AQFSSAPKKS RLKIGESSAF FTYVKSTVLR TNGQDPPLVD GNGSLHLHRG
LAEKFQVVAS EGINNTKQAR RATPKSTVLR TNGQDPPLVN GNGSHHLHRG AAEKFQVVAS
EGINNTKQAH RSRGTEQYHS QGETLQNGAS YPHSLERSRT LPTSMESHGR NYQEGNMNIP
QVAMNRSKDS SQVDGSGFSA PNAYPYYMHG VMNQVMMQSA AMMPQYGHQI PHCQPNHPNG
MTGYPYYHHP MNTSLQHSQM SLQNGQMSMV HHSWSPAGNP PSNEVRVNKL DRREEALLKF
RRKRNQRCFD KKIRYVNRKR LAERRPRVKG QFVRKMNGVN VDLNGQPDSA DYDDEEEEEE
EEEEENRDSS PQDDALGT
