CPL1_ARATH
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 03-AUG-2022, entry version 131.
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},
GN SHI4 {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. Regulates negatively 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};
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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.AT4G21670.1; -.
DR iPTMnet; Q5YDB6; -.
DR PaxDb; Q5YDB6; -.
DR PRIDE; Q5YDB6; -.
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; locus:2119053; AT4G21670.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_010333_0_0_1; -.
DR InParanoid; Q5YDB6; -.
DR OMA; DIAFKCG; -.
DR OrthoDB; 131233at2759; -.
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; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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 Gene3D; 3.40.50.1000; -; 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; PTHR23081; 1.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SUPFAM; SSF56784; SSF56784; 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
