Q5YDB5 (CPL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA polymerase II C-terminal domain phosphatase-like 2
Short name=FCP-like 2
EC=3.1.3.16

Alternative name(s):
Carboxyl-terminal phosphatase-like 2
Short name=AtCPL2
Short name=CTD phosphatase-like 2

Gene names

Name:	CPL2
Ordered Locus Names:	At5g01270
ORF Names:	F7J8.250

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	770 AA.
Sequence status	Complete.
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 CPL1, required for male gametes fertility. Multifunctional regulator that modulates plant growth, stress, and phytohormones responses. Positive transcription regulator of genes involved in high salinity resistance and auxin mediated signaling pathway. Ref.1 Ref.4
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds magnesium, cobalt or manganese ions. Ref.1
Subcellular location	Nucleus. Cytoplasm Ref.1.
Tissue specificity	Expressed in seedlings, particularly in tissues undergoing cell division and expansion, petioles, cotyledons vasculature, leaves, shoot and root meristems, and flowers, especially in buds and organs vasculatures. Ref.4
Disruption phenotype	Leaf expansion defects, early flowering, low fertility, and increased salt (NaCl) sensitivity. Produces shorter hypocotyls than wild-type plants in the light, but not in the dark. Ref.1 Ref.4
Sequence similarities	Contains 1 DRBM (double-stranded RNA-binding) domain. Contains 1 FCP1 homology domain.
Biophysicochemical properties	pH dependence: Optimum pH is 5.5-6.0. Ref.1
Sequence caution	The sequence CAB69855.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Auxin signaling pathway Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding RNA-binding
Molecular function	Activator Developmental protein Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	auxin mediated signaling pathway Inferred from mutant phenotype Ref.4. Source: UniProtKB multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.4. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	double-stranded RNA binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: EC phosphoserine phosphatase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q5YDB5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 770	770	RNA polymerase II C-terminal domain phosphatase-like 2		PRO_0000376084
Regions
	Domain	134 – 385	252	FCP1 homology
	Domain	656 – 722	67	DRBM

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 16, 2011. Version 3. Checksum: 7672B4F18397CB14	FASTA	770	85,953
	10 20 30 40 50 60 MNRLGHKSVV YHGDLRLGEL DVNHVSSSHE FRFPNDEIRI HHLSPAGERC PPLAILQTIA 70 80 90 100 110 120 SFAVRCKLES SAPVKSQELM HLHAVCFHEL KTAVVMLGDE EIHLVAMPSK EKKFPCFWCF 130 140 150 160 170 180 SVPSGLYDSC LRMLNTRCLS IVFDLDETLI VANTMKSFED RIEALKSWIS REMDPVRING 190 200 210 220 230 240 MSAELKRYMD DRMLLKQYID NDYAFDNGVL LKAQPEEVRP TSDGQEKVCR PVIRLPEKNT 250 260 270 280 290 300 VLTRIKPEIR DTSVLVKLRP AWEELRSYLT AKTRKRFEVY VCTMAERDYA LEMWRLLDPE 310 320 330 340 350 360 AHLISLKELR DRIVCVKPDA KKSLLSVFNG GICHPKMAMV IDDRMKVWED KDQPRVHVVS 370 380 390 400 410 420 AYLPYYAPQA ETALVVPHLC VARNVACNVR GYFFKEFDES LMSSISLVYY EDDVENLPPS 430 440 450 460 470 480 PDVSNYVVIE DPGFASNGNI NAPPINEGMC GGEVERRLNQ AAAADHSTLP ATSNAEQKPE 490 500 510 520 530 540 TPKPQIAVIP NNASTATAAA LLPSHKPSLL GAPRRDGFTF SDGGRPLMMR PGVDIRNQNF 550 560 570 580 590 600 NQPPILAKIP MQPPSSSMHS PGGWLVDDEN RPSFPGRPSG LYPSQFPHGT PGSAPVGPFA 610 620 630 640 650 660 HPSHLRSEEV AMDDDLKRQN PSRQTTEGGI SQNHLVSNGR EHHTDGGKSN GGQSHLFVSA 670 680 690 700 710 720 LQEIGRRCGS KVEFRTVIST NKELQFSVEV LFTGEKIGIG MAKTKKDAHQ QAAENALRSL 730 740 750 760 770 AEKYVAHVAP LARETEKGPE NDNGFLWESS EDVSNKGLEE EAPKENISEL

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, COFACTOR.
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[5]	"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] [Europe PMC] [Abstract] Cited for: GENE FAMILY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY557187 mRNA. Translation: AAT52023.1. AL137189 Genomic DNA. Translation: CAB69855.1. Sequence problems. CP002688 Genomic DNA. Translation: AED90320.1.
IPI	IPI00522259. IPI00991618.
PIR	T45967.
RefSeq	NP_195747.2. NM_120205.4.
UniGene	At.21936.
3D structure databases
ProteinModelPortal	Q5YDB5.
SMR	Q5YDB5. Positions 658-725.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G01270.1-P.
Proteomic databases
PaxDb	Q5YDB5.
PRIDE	Q5YDB5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	831743.
KEGG	ath:AT5G01270.
Organism-specific databases
TAIR	At5g01270.
Phylogenomic databases
eggNOG	NOG290259.
HOGENOM	HOG000078695.
InParanoid	Q5YDB5.
ProtClustDB	CLSN2918859.
Gene expression databases
ArrayExpress	Q5YDB5.
Genevestigator	Q5YDB5.
Family and domain databases
Gene3D	3.30.160.20. 1 hit. 3.40.50.1000. 3 hits.
InterPro	IPR001159. Ds-RNA-bd. IPR014720. dsRNA-bd-like_dom. IPR023214. HAD-like_dom. IPR004274. NIF. [Graphical view]
Pfam	PF00035. dsrm. 1 hit. PF03031. NIF. 1 hit. [Graphical view]
SMART	SM00577. CPDc. 1 hit. SM00358. DSRM. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
PROSITE	PS50137. DS_RBD. 1 hit. PS50969. FCP1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CPL2_ARATH

Accession

Primary (citable) accession number: Q5YDB5
Secondary accession number(s): F4K803, Q9LFA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 26, 2009
Last sequence update:	November 16, 2011
Last modified:	May 1, 2013
This is version 61 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program