ID CPL1_ARATH Reviewed; 967 AA. AC Q5YDB6; Q0WNZ7; Q56WT8; Q9SVT0; DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 139. DE RecName: Full=RNA polymerase II C-terminal domain phosphatase-like 1 {ECO:0000305}; DE Short=FCP-like 1 {ECO:0000305}; DE EC=3.1.3.16 {ECO:0000269|PubMed:12149434}; DE AltName: Full=Carboxyl-terminal phosphatase-like 1; DE Short=AtCPL1 {ECO:0000303|PubMed:15388846}; DE Short=CTD phosphatase-like 1; DE AltName: Full=Protein FIERY 2 {ECO:0000303|PubMed:12149453}; DE AltName: Full=Protein JASMONATE OVEREXPRESSING 1 {ECO:0000303|PubMed:11874572}; DE AltName: Full=Protein SHINY 4 {ECO:0000303|PubMed:23874224}; GN Name=CPL1 {ECO:0000303|PubMed:15388846}; GN Synonyms=FRY2 {ECO:0000303|PubMed:12149453}, JOE1 {ECO:0000305}, SHI4 GN {ECO:0000303|PubMed:23874224}; GN OrderedLocusNames=At4g21670 {ECO:0000312|Araport:AT4G21670}; GN ORFNames=F17L22.130 {ECO:0000312|EMBL:CAB36811.1}; 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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND COFACTOR. RX PubMed=15388846; DOI=10.1073/pnas.0403174101; RA Koiwa H., Hausmann S., Bang W.Y., Ueda A., Kondo N., Hiraguri A., RA Fukuhara T., Bahk J.D., Yun D.-J., Bressan R.A., Hasegawa P.M., Shuman S.; RT "Arabidopsis C-terminal domain phosphatase-like 1 and 2 are essential Ser- RT 5-specific C-terminal domain phosphatases."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14539-14544(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). 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; 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 FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=11874572; DOI=10.1046/j.0960-7412.2001.01241.x; RA Jensen A.B., Raventos D., Mundy J.; RT "Fusion genetic analysis of jasmonate-signalling mutants in Arabidopsis."; RL Plant J. 29:595-606(2002). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE. RX PubMed=12149434; DOI=10.1073/pnas.112276199; RA Koiwa H., Barb A.W., Xiong L., Li F., McCully M.G., Lee B.-H., RA Sokolchik I., Zhu J., Gong Z., Reddy M., Sharkhuu A., Manabe Y., Yokoi S., RA Zhu J.-K., Bressan R.A., Hasegawa P.M.; RT "C-terminal domain phosphatase-like family members (AtCPLs) differentially RT regulate Arabidopsis thaliana abiotic stress signaling, growth, and RT development."; RL Proc. Natl. Acad. Sci. U.S.A. 99:10893-10898(2002). RN [7] RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=12149453; DOI=10.1073/pnas.162111599; RA Xiong L., Lee H., Ishitani M., Tanaka Y., Stevenson B., Koiwa H., RA Bressan R.A., Hasegawa P.M., Zhu J.-K.; RT "Repression of stress-responsive genes by FIERY2, a novel transcriptional RT regulator in Arabidopsis."; RL Proc. Natl. Acad. Sci. U.S.A. 99:10899-10904(2002). RN [8] RP INTERACTION WITH FREE1; ANAC019; DMS3; MYB3; MYB4 AND MYB32, SUBCELLULAR RP LOCATION, AND DRBM DOMAINS. RX PubMed=18541146; DOI=10.1016/j.bbrc.2008.05.161; RA Bang W.Y., Kim S.W., Jeong I.S., Koiwa H., Bahk J.D.; RT "The C-terminal region (640-967) of Arabidopsis CPL1 interacts with the RT abiotic stress- and ABA-responsive transcription factors."; RL Biochem. Biophys. Res. Commun. 372:907-912(2008). RN [9] RP FUNCTION. RX PubMed=18506580; DOI=10.1007/s11103-008-9348-y; RA Ueda A., Li P., Feng Y., Vikram M., Kim S., Kang C.H., Kang J.S., RA Bahk J.D., Lee S.Y., Fukuhara T., Staswick P.E., Pepper A.E., Koiwa H.; RT "The Arabidopsis thaliana carboxyl-terminal domain phosphatase-like 2 RT regulates plant growth, stress and auxin responses."; RL Plant Mol. Biol. 67:683-697(2008). RN [10] RP GENE FAMILY. RX PubMed=18156295; DOI=10.1104/pp.107.111393; RA Kerk D., Templeton G., Moorhead G.B.G.; RT "Evolutionary radiation pattern of novel protein phosphatases revealed by RT analysis of protein data from the completely sequenced genomes of humans, RT green algae, and higher plants."; RL Plant Physiol. 146:351-367(2008). RN [11] RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-116. RX PubMed=18764923; DOI=10.1111/j.1365-313x.2008.03663.x; RA Matsuda O., Sakamoto H., Nakao Y., Oda K., Iba K.; RT "CTD phosphatases in the attenuation of wound-induced transcription of RT jasmonic acid biosynthetic genes in Arabidopsis."; RL Plant J. 57:96-108(2009). RN [12] RP FUNCTION, INTERACTION WITH RCF3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP GLU-116. RX PubMed=23874224; DOI=10.1371/journal.pgen.1003625; RA Jiang J., Wang B., Shen Y., Wang H., Feng Q., Shi H.; RT "The arabidopsis RNA binding protein with K homology motifs, SHINY1, RT interacts with the C-terminal domain phosphatase-like 1 (CPL1) to repress RT stress-inducible gene expression."; RL PLoS Genet. 9:E1003625-E1003625(2013). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RCF3; RS40 AND RS41, RP AND SUBCELLULAR LOCATION. RX PubMed=24146632; DOI=10.1371/journal.pgen.1003875; RA Chen T., Cui P., Chen H., Ali S., Zhang S., Xiong L.; RT "A KH-domain RNA-binding protein interacts with FIERY2/CTD phosphatase-like RT 1 and splicing factors and is important for pre-mRNA splicing in RT Arabidopsis."; RL PLoS Genet. 9:E1003875-E1003875(2013). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RCF3, SUBCELLULAR RP LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF ASP-161. RX PubMed=24303021; DOI=10.1371/journal.pone.0080509; RA Jeong I.S., Fukudome A., Aksoy E., Bang W.Y., Kim S., Guan Q., Bahk J.D., RA May K.A., Russell W.K., Zhu J., Koiwa H.; RT "Regulation of abiotic stress signalling by Arabidopsis C-terminal domain RT phosphatase-like 1 requires interaction with a k-homology domain-containing RT protein."; RL PLoS ONE 8:E80509-E80509(2013). RN [15] RP FUNCTION. RX PubMed=26227967; DOI=10.1093/nar/gkv751; RA Chen T., Cui P., Xiong L.; RT "The RNA-binding protein HOS5 and serine/arginine-rich proteins RS40 and RT RS41 participate in miRNA biogenesis in Arabidopsis."; RL Nucleic Acids Res. 43:8283-8298(2015). RN [16] RP INTERACTION WITH RCF3. RX PubMed=26512101; DOI=10.1073/pnas.1512865112; RA Karlsson P., Christie M.D., Seymour D.K., Wang H., Wang X., Hagmann J., RA Kulcheski F., Manavella P.A.; RT "KH domain protein RCF3 is a tissue-biased regulator of the plant miRNA RT biogenesis cofactor HYL1."; RL Proc. Natl. Acad. Sci. U.S.A. 112:14096-14101(2015). RN [17] RP FUNCTION, INTERACTION WITH EIF4A3 AND UPF3, AND SUBCELLULAR LOCATION. RX PubMed=26887918; DOI=10.1105/tpc.15.00771; RA Cui P., Chen T., Qin T., Ding F., Wang Z., Chen H., Xiong L.; RT "The RNA polymerase II C-terminal domain phosphatase-like protein RT FIERY2/CPL1 interacts with eIF4AIII and is essential for nonsense-mediated RT mrna decay in Arabidopsis."; RL Plant Cell 28:770-785(2016). CC -!- FUNCTION: Processively dephosphorylates 'Ser-5' but not 'Ser-2' of the CC heptad repeats YSPTSPS in the C-terminal domain of the largest RNA CC polymerase II subunit (RPB1). This promotes the activity of RNA CC polymerase II. Together with CPL2, required for male gametes fertility. CC Multifunctional regulator that modulates plant growth, stress, and CC phytohormones responses. Negative regulator of stress gene CC transcription involved in abscisic acid (ABA) mediated and jasmonic CC acid (JA) mediated signaling pathways, NaCl, osmotic stress, wounding, CC and cold resistance. Negatively regulates the expression of jasmonic CC acid (JA) biosynthetic genes in response to wounding (PubMed:11874572, CC PubMed:12149434, PubMed:12149453, PubMed:15388846, PubMed:18506580, CC PubMed:18764923). Forms a complex with RCF3 that modulates co- CC transcriptional processes such as mRNA capping and polyadenylation, and CC functions to repress stress-inducible gene expression CC (PubMed:23874224). Dephosphorylates RCF3 (PubMed:26227967). Involved in CC the dephosphorylation of EIF4A3. This dephosphorylation retains EIF4A3 CC in the nucleus and limits its accumulation in the cytoplasm. Is CC essential for the degradation of the nonsense-mediated mRNA decay (NMD) CC transcripts (PubMed:26887918). {ECO:0000269|PubMed:11874572, CC ECO:0000269|PubMed:12149434, ECO:0000269|PubMed:12149453, CC ECO:0000269|PubMed:15388846, ECO:0000269|PubMed:18506580, CC ECO:0000269|PubMed:18764923, ECO:0000269|PubMed:23874224, CC ECO:0000269|PubMed:26227967, ECO:0000269|PubMed:26887918}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:12149434}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000269|PubMed:12149434}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:15388846}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:15388846}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:15388846}; CC Note=Binds Mg(2+), Co(2+) or Mn(2+). {ECO:0000269|PubMed:15388846}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:15388846}; CC -!- SUBUNIT: Interacts with FREE1, ANAC019, MYB3, MYB4 and MYB32. Binds to CC DMS3 (PubMed:18541146). Interacts with RCF3 (PubMed:23874224, CC PubMed:24146632, PubMed:24303021, PubMed:26512101). Interacts with RS40 CC and RS41 (PubMed:24146632). Interacts with EIF4A3 (PubMed:26887918). CC Interacts with UPF3 (PubMed:26887918). {ECO:0000269|PubMed:18541146, CC ECO:0000269|PubMed:23874224, ECO:0000269|PubMed:24146632, CC ECO:0000269|PubMed:24303021, ECO:0000269|PubMed:26512101, CC ECO:0000269|PubMed:26887918}. CC -!- INTERACTION: CC Q5YDB6; Q9ZVD0: SE; NbExp=7; IntAct=EBI-1786459, EBI-6553299; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15388846, CC ECO:0000269|PubMed:18541146, ECO:0000269|PubMed:23874224, CC ECO:0000269|PubMed:24146632, ECO:0000269|PubMed:24303021, CC ECO:0000269|PubMed:26887918}. Nucleus speckle CC {ECO:0000269|PubMed:24146632}. CC -!- TISSUE SPECIFICITY: Expressed at very low levels in roots, leaves, CC stems, flowers and siliques. {ECO:0000269|PubMed:12149453}. CC -!- INDUCTION: Slightly repressed by ABA. {ECO:0000269|PubMed:12149453}. CC -!- DOMAIN: DRBM domains are required for interactions with target CC transcription factors such as ANAC019 and MYB3. CC -!- DISRUPTION PHENOTYPE: Grows more rapidly and flower later than wild- CC type plants. Increased tolerance to salt stress and to ABA during seed CC germination but more sensitive to freezing damage at the seedling CC stage, by the enhanced expression of abiotic stress-induced genes. CC Hypersensitivity to MeJA, accumulates high levels of anthocyanin on CC medium containing MeJA. Confers wound hyperresponsiveness of JA- CC biosynthetic genes. {ECO:0000269|PubMed:11874572, CC ECO:0000269|PubMed:12149434, ECO:0000269|PubMed:12149453, CC ECO:0000269|PubMed:15388846, ECO:0000269|PubMed:18764923}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB36811.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB81274.1; Type=Erroneous gene model prediction; 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; AY557186; AAT52022.1; -; mRNA. DR EMBL; AL035527; CAB36811.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161555; CAB81274.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002687; AEE84488.1; -; Genomic_DNA. DR EMBL; AK221944; BAD94401.1; -; mRNA. DR EMBL; AK229289; BAF01152.1; -; mRNA. DR PIR; T05842; T05842. DR RefSeq; NP_193898.3; NM_118287.5. DR AlphaFoldDB; Q5YDB6; -. DR BioGRID; 13543; 13. DR IntAct; Q5YDB6; 12. DR STRING; 3702.Q5YDB6; -. DR iPTMnet; Q5YDB6; -. DR PaxDb; 3702-AT4G21670-1; -. DR ProteomicsDB; 224541; -. DR EnsemblPlants; AT4G21670.1; AT4G21670.1; AT4G21670. DR GeneID; 828254; -. DR Gramene; AT4G21670.1; AT4G21670.1; AT4G21670. DR KEGG; ath:AT4G21670; -. DR Araport; AT4G21670; -. DR TAIR; AT4G21670; CPL1. DR eggNOG; KOG0323; Eukaryota. DR HOGENOM; CLU_010333_0_0_1; -. DR InParanoid; Q5YDB6; -. DR OMA; GWFPAEE; -. DR OrthoDB; 1200617at2759; -. DR PhylomeDB; Q5YDB6; -. DR PRO; PR:Q5YDB6; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q5YDB6; baseline and differential. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0016791; F:phosphatase activity; IDA:TAIR. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:TAIR. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro. DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:TAIR. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW. DR GO; GO:0009651; P:response to salt stress; IMP:TAIR. DR GO; GO:0009611; P:response to wounding; IMP:UniProtKB. DR CDD; cd07521; HAD_FCP1-like; 1. DR Gene3D; 3.30.160.20; -; 2. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR039189; Fcp1. DR InterPro; IPR004274; FCP1_dom. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR PANTHER; PTHR23081:SF0; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 1; 1. DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1. DR Pfam; PF00035; dsrm; 2. DR Pfam; PF03031; NIF; 1. DR SMART; SM00577; CPDc; 1. DR SMART; SM00358; DSRM; 2. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2. DR SUPFAM; SSF56784; HAD-like; 1. DR PROSITE; PS50137; DS_RBD; 2. DR PROSITE; PS50969; FCP1; 1. PE 1: Evidence at protein level; KW Abscisic acid signaling pathway; Developmental protein; Hydrolase; KW Jasmonic acid signaling pathway; Metal-binding; KW Nonsense-mediated mRNA decay; Nucleus; Reference proteome; Repeat; KW Repressor; RNA-binding; Transcription; Transcription regulation. FT CHAIN 1..967 FT /note="RNA polymerase II C-terminal domain phosphatase-like FT 1" FT /id="PRO_0000376083" FT DOMAIN 151..401 FT /note="FCP1 homology" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336" FT DOMAIN 724..792 FT /note="DRBM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT DOMAIN 855..925 FT /note="DRBM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT REGION 548..611 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 643..712 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 928..967 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 945..967 FT /note="Required for nuclear localization (NLS)" FT /evidence="ECO:0000269|PubMed:15388846" FT MOTIF 38..41 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000269|PubMed:24303021" FT MOTIF 947..951 FT /note="Nuclear localization signal (NLS)" FT /evidence="ECO:0000269|PubMed:24303021" FT COMPBIAS 560..581 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 662..687 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 688..712 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 116 FT /note="E->K: In cpl1-3 and shi4; enhanced expression of FT abiotic stress-induced genes, and cold-sensitive FT phenotype." FT /evidence="ECO:0000269|PubMed:18764923, FT ECO:0000269|PubMed:23874224" FT MUTAGEN 161 FT /note="D->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:24303021" FT CONFLICT 446 FT /note="E -> V (in Ref. 4; BAF01152)" FT /evidence="ECO:0000305" FT CONFLICT 669 FT /note="E -> V (in Ref. 4; BAD94401)" FT /evidence="ECO:0000305" FT CONFLICT 797 FT /note="A -> T (in Ref. 4; BAD94401)" FT /evidence="ECO:0000305" SQ SEQUENCE 967 AA; 108421 MW; 3FD10F0F3A73154D CRC64; MYSNNRVEVF HGDGRLGELE IYPSRELNQQ QDDVMKQRKK KQREVMELAK MGIRISHFSQ SGERCPPLAI LTTISSCGLC FKLEASPSPA QESLSLFYSS CLRDNKTAVM LLGGEELHLV AMYSENIKND RPCFWAFSVA PGIYDSCLVM LNLRCLGIVF DLDETLVVAN TMRSFEDKID GFQRRINNEM DPQRLAVIVA EMKRYQDDKN LLKQYIESDQ VVENGEVIKV QSEIVPALSD NHQPLVRPLI RLQEKNIILT RINPMIRDTS VLVRMRPSWE ELRSYLTAKG RKRFEVYVCT MAERDYALEM WRLLDPEGNL INTNDLLARI VCVKSGFKKS LFNVFLDGTC HPKMALVIDD RLKVWDEKDQ PRVHVVPAFA PYYSPQAEAA ATPVLCVARN VACGVRGGFF RDFDDSLLPR IAEISYENDA EDIPSPPDVS HYLVSEDDTS GLNGNKDPLS FDGMADTEVE RRLKEAISAS SAVLPAANID PRIAAPVQFP MASASSVSVP VPVQVVQQAI QPSAMAFPSI PFQQPQQPTS IAKHLVPSEP SLQSSPAREE GEVPESELDP DTRRRLLILQ HGQDTRDPAP SEPSFPQRPP VQAPPSHVQS RNGWFPVEEE MDPAQIRRAV SKEYPLDSEM IHMEKHRPRH PSFFSKIDNS TQSDRMLHEN RRPPKESLRR DEQLRSNNNL PDSHPFYGED ASWNQSSSRN SDLDFLPERS VSATETSADV LHGIAIKCGA KVEYKPSLVS STDLRFSVEA WLSNQKIGEG IGKSRREALH KAAEASIQNL ADGYMRANGD PGPSHRDATP FTNENISMGN ANALNNQPFA RDETALPVSS RPTDPRLEGS MRHTGSITAL RELCASEGLE MAFQSQRQLP SDMVHRDELH AQVEIDGRVV GEGVGSTWDE ARMQAAERAL SSVRSMLGQP LHKRQGSPRS FGGMSNKRLK PDFQRSLQRM PSSGRYS //