Reviewed, UniProtKB/Swiss-Prot Q5YDB6 (CPL1_ARATH)

Names and origin

Protein names

Recommended name:
    RNA polymerase II C-terminal domain phosphatase-like 1
      Short name=FCP-like 1
    EC=3.1.3.16
Alternative name(s):
    Carboxyl-terminal phosphatase-like 1
      Short name=CTD phosphatase-like 1
      Short name=AtCPL1
    Protein JASMONATE OVEREXPRESSING 1
    Protein FIERY 2

Gene names

Name:	CPL1
Synonyms:	FRY2, JOE1
Ordered Locus Names:	At4g21670
ORF Names:	F17L22.130

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	967 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Processively dephosphorylates 'Ser-5' but not 'Ser-2' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). This promotes the activity of RNA polymerase II. Together with CPL2, required for male gametes fertility. Multifunctional regulator that modulates plant growth, stress, and phytohormones responses. Negative regulator of stress gene transcription involved in abscisic acid (ABA) mediated and jasmonic acid (JA) mediated signaling patways, NaCl, osmotic stress, wounding, and cold resistance. Regulates negatively the expression of jasmonic acid (JA) biosynthetic genes in response to wounding. Ref.1 Ref.4 Ref.5 Ref.6 Ref.8 Ref.10
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate. Ref.5
Cofactor	Binds magnesium, cobalt or manganese ions. Ref.1
Subunit structure	Interacts with the FYVE domain-containing protein At1g20110, ANAC019, MYB3, MYB4 and MYB32. Ref.7
Subcellular location	Nucleus. Ref.1 Ref.7
Tissue specificity	Expressed at very low levels in roots, leaves, stems, flowers and siliques. Ref.6
Induction	Slightly repressed by ABA. Ref.6
Domain	DRBM domains are required for interactions with target transcription factors such as ANAC019 and MYB3. Ref.7
Disruption phenotype	Grows more rapidly and flower later than wild-type plants. Increased tolerance to salt stress and to ABA during seed germination but more sensitive to freezing damage at the seedling stage, by the enhanced expression of abiotic stress-induced genes. Hypersentitivity to MeJA, accumulates high levels of anthocyanin on medium containing MeJA. Confers wound hyperresponsiveness of JA-biosynthetic genes. Ref.1 Ref.4 Ref.5 Ref.6 Ref.10
Sequence similarities	Contains 2 DRBM (double-stranded RNA-binding) domains. Contains 1 FCP1 homology domain.
Biophysicochemical properties	pH dependence: Optimum pH is 5.5-6.0.
Sequence caution	The sequence CAB36811.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB81274.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat
Ligand	Metal-binding RNA-binding
Molecular function	Developmental protein Hydrolase Repressor
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	abscisic acid mediated signaling pathway Ref.5 Inferred from mutant phenotype. Source: TAIR multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription Ref.5 Inferred from mutant phenotype. Source: TAIR response to abiotic stimulus Ref.5 Inferred from mutant phenotype. Source: TAIR response to wounding Ref.10 Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	double-stranded RNA binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide phosphatase activity Ref.5 Inferred from direct assay. Source: TAIR phosphoprotein phosphatase activity Inferred from electronic annotation. Source: EC phosphoserine phosphatase activity Ref.8 Inferred from direct assay. Source: UniProtKB protein binding Ref.7 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
At1g20110	Q9ASS2	2	EBI-1786459,EBI-1786536
At2g28840/F8N16.13	Q94B55	2	EBI-1786459,EBI-1786575
At3g26730	Q9LSE3	2	EBI-1786459,EBI-1786522
At3g49250	Q94A79	2	EBI-1786459,EBI-1786471
At3g54290	Q8RWC0	2	EBI-1786459,EBI-1786564
At4g28760	Q949M4	2	EBI-1786459,EBI-1786550
MYB3	Q9S9K9	2	EBI-1786459,EBI-1786591
NAC019	Q9C932	2	EBI-1786459,EBI-1786615

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 967	967	RNA polymerase II C-terminal domain phosphatase-like 1		PRO_0000376083
Regions
	Domain	151 – 401	251	FCP1 homology
	Domain	724 – 792	69	DRBM 1
	Domain	855 – 925	71	DRBM 2
	Region	945 – 967	23	Required for nuclear localization (NLS)
Experimental info
	Mutagenesis	116	1	E → K in cpl1-3; enhanced expression of abiotic stress-induced genes. Ref.10
	Sequence conflict	446	1	E → V in BAF01152. Ref.3
	Sequence conflict	669	1	E → V in BAD94401. Ref.3
	Sequence conflict	797	1	A → T in BAD94401. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q5YDB6-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 3FD10F0F3A73154D	FASTA	967	108,421
	10 20 30 40 50 60 MYSNNRVEVF HGDGRLGELE IYPSRELNQQ QDDVMKQRKK KQREVMELAK MGIRISHFSQ 70 80 90 100 110 120 SGERCPPLAI LTTISSCGLC FKLEASPSPA QESLSLFYSS CLRDNKTAVM LLGGEELHLV 130 140 150 160 170 180 AMYSENIKND RPCFWAFSVA PGIYDSCLVM LNLRCLGIVF DLDETLVVAN TMRSFEDKID 190 200 210 220 230 240 GFQRRINNEM DPQRLAVIVA EMKRYQDDKN LLKQYIESDQ VVENGEVIKV QSEIVPALSD 250 260 270 280 290 300 NHQPLVRPLI RLQEKNIILT RINPMIRDTS VLVRMRPSWE ELRSYLTAKG RKRFEVYVCT 310 320 330 340 350 360 MAERDYALEM WRLLDPEGNL INTNDLLARI VCVKSGFKKS LFNVFLDGTC HPKMALVIDD 370 380 390 400 410 420 RLKVWDEKDQ PRVHVVPAFA PYYSPQAEAA ATPVLCVARN VACGVRGGFF RDFDDSLLPR 430 440 450 460 470 480 IAEISYENDA EDIPSPPDVS HYLVSEDDTS GLNGNKDPLS FDGMADTEVE RRLKEAISAS 490 500 510 520 530 540 SAVLPAANID PRIAAPVQFP MASASSVSVP VPVQVVQQAI QPSAMAFPSI PFQQPQQPTS 550 560 570 580 590 600 IAKHLVPSEP SLQSSPAREE GEVPESELDP DTRRRLLILQ HGQDTRDPAP SEPSFPQRPP 610 620 630 640 650 660 VQAPPSHVQS RNGWFPVEEE MDPAQIRRAV SKEYPLDSEM IHMEKHRPRH PSFFSKIDNS 670 680 690 700 710 720 TQSDRMLHEN RRPPKESLRR DEQLRSNNNL PDSHPFYGED ASWNQSSSRN SDLDFLPERS 730 740 750 760 770 780 VSATETSADV LHGIAIKCGA KVEYKPSLVS STDLRFSVEA WLSNQKIGEG IGKSRREALH 790 800 810 820 830 840 KAAEASIQNL ADGYMRANGD PGPSHRDATP FTNENISMGN ANALNNQPFA RDETALPVSS 850 860 870 880 890 900 RPTDPRLEGS MRHTGSITAL RELCASEGLE MAFQSQRQLP SDMVHRDELH AQVEIDGRVV 910 920 930 940 950 960 GEGVGSTWDE ARMQAAERAL SSVRSMLGQP LHKRQGSPRS FGGMSNKRLK PDFQRSLQRM PSSGRYS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis C-terminal domain phosphatase-like 1 and 2 are essential Ser-5-specific C-terminal domain phosphatases." Koiwa H., Hausmann S., Bang W.Y., Ueda A., Kondo N., Hiraguri A., Fukuhara T., Bahk J.D., Yun D.-J., Bressan R.A., Hasegawa P.M., Shuman S. Proc. Natl. Acad. Sci. U.S.A. 101:14539-14544(2004) [PubMed: 15388846] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, COFACTOR.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Fusion genetic analysis of jasmonate-signalling mutants in Arabidopsis." Jensen A.B., Raventos D., Mundy J. Plant J. 29:595-606(2002) [PubMed: 11874572] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]	"C-terminal domain phosphatase-like family members (AtCPLs) differentially regulate Arabidopsis thaliana abiotic stress signaling, growth, and development." Koiwa H., Barb A.W., Xiong L., Li F., McCully M.G., Lee B.-H., Sokolchik I., Zhu J., Gong Z., Reddy M., Sharkhuu A., Manabe Y., Yokoi S., Zhu J.-K., Bressan R.A., Hasegawa P.M. Proc. Natl. Acad. Sci. U.S.A. 99:10893-10898(2002) [PubMed: 12149434] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
[6]	"Repression of stress-responsive genes by FIERY2, a novel transcriptional regulator in Arabidopsis." Xiong L., Lee H., Ishitani M., Tanaka Y., Stevenson B., Koiwa H., Bressan R.A., Hasegawa P.M., Zhu J.-K. Proc. Natl. Acad. Sci. U.S.A. 99:10899-10904(2002) [PubMed: 12149453] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
[7]	"The C-terminal region (640-967) of Arabidopsis CPL1 interacts with the abiotic stress- and ABA-responsive transcription factors." Bang W.Y., Kim S.W., Jeong I.S., Koiwa H., Bahk J.D. Biochem. Biophys. Res. Commun. 372:907-912(2008) [PubMed: 18541146] [Abstract] Cited for: INTERACTION WITH AT1G20110; ANAC019; MYB3; MYB4 AND MYB32, SUBCELLULAR LOCATION, DRBM DOMAINS.
[8]	"The Arabidopsis thaliana carboxyl-terminal domain phosphatase-like 2 regulates plant growth, stress and auxin responses." Ueda A., Li P., Feng Y., Vikram M., Kim S., Kang C.H., Kang J.S., Bahk J.D., Lee S.Y., Fukuhara T., Staswick P.E., Pepper A.E., Koiwa H. Plant Mol. Biol. 67:683-697(2008) [PubMed: 18506580] [Abstract] Cited for: FUNCTION.
[9]	"Evolutionary radiation pattern of novel protein phosphatases revealed by analysis of protein data from the completely sequenced genomes of humans, green algae, and higher plants." Kerk D., Templeton G., Moorhead G.B.G. Plant Physiol. 146:351-367(2008) [PubMed: 18156295] [Abstract] Cited for: GENE FAMILY.
[10]	"CTD phosphatases in the attenuation of wound-induced transcription of jasmonic acid biosynthetic genes in Arabidopsis." Matsuda O., Sakamoto H., Nakao Y., Oda K., Iba K. Plant J. 57:96-108(2009) [PubMed: 18764923] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-116.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY557186 mRNA. Translation: AAT52022.1. AL035527 Genomic DNA. Translation: CAB36811.1. Sequence problems. AL161555 Genomic DNA. Translation: CAB81274.1. Sequence problems. AK221944 mRNA. Translation: BAD94401.1. AK229289 mRNA. Translation: BAF01152.1.
IPI	IPI00518313.
PIR	T05842.
RefSeq	NP_193898.3.
UniGene	At.32611
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q5YDB6. 9 interactions.
STRING	Q5YDB6.
Proteomic databases
PRIDE	Q5YDB6.
Genome annotation databases
GeneID	828254.
GenomeReviews	Gene locus AT4G21670 in contig CT486007_GR.
KEGG	ath:AT4G21670.
Organism-specific databases
TAIR	At4g21670.
Phylogenomic databases
OMA	LSDNHQP.
Gene expression databases
Genevestigator	Q5YDB6.
Family and domain databases
InterPro	IPR001159. Ds-RNA_bd. IPR004274. NIF. [Graphical view]
Pfam	PF00035. dsrm. 2 hits. [Graphical view]
SMART	SM00577. CPDc. 1 hit. SM00358. DSRM. 2 hits. [Graphical view]
PROSITE	PS50137. DS_RBD. 2 hits. PS50969. FCP1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CPL1_ARATH

Accession

Primary (citable) accession number: Q5YDB6
Secondary accession number(s): Q0WNZ7, Q56WT8, Q9SVT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	November 23, 2004
Last modified:	November 3, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)