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 24-JAN-2024, entry version 160. 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}. 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; 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.Q9LKL2; -. DR PaxDb; 3702-AT5G61380-1; -. 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; AT5G61380; TOC1. DR eggNOG; KOG1601; Eukaryota. DR HOGENOM; CLU_041215_0_0_1; -. DR InParanoid; Q9LKL2; -. DR OMA; NGQDPPL; -. DR OrthoDB; 406014at2759; -. DR PhylomeDB; Q9LKL2; -. DR PRO; PR:Q9LKL2; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9LKL2; baseline and differential. 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:0006351; P:DNA-templated transcription; TAS:UniProtKB. 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:0006355; P:regulation of DNA-templated transcription; ISS:TAIR. DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR. DR CDD; cd17582; psREC_PRR; 1. DR Gene3D; 3.40.50.2300; -; 1. 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; TWO-COMPONENT RESPONSE REGULATOR; 1. DR PANTHER; PTHR43874:SF1; TWO-COMPONENT RESPONSE REGULATOR-LIKE APRR1; 1. DR Pfam; PF06203; CCT; 1. DR Pfam; PF00072; Response_reg; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR PROSITE; PS51017; CCT; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. DR Genevisible; Q9LKL2; AT. 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 //