Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5YDB5 (CPL2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length770 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 770770RNA polymerase II C-terminal domain phosphatase-like 2
PRO_0000376084

Regions

Domain134 – 385252FCP1 homology
Domain656 – 72267DRBM

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 16, 2011. Version 3.
Checksum: 7672B4F18397CB14

FASTA77085,953
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
PIRT45967.
RefSeqNP_195747.2. NM_120205.4. [Q5YDB5-1]
UniGeneAt.21936.

3D structure databases

ProteinModelPortalQ5YDB5.
SMRQ5YDB5. Positions 655-725.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G01270.1-P.

Proteomic databases

PaxDbQ5YDB5.
PRIDEQ5YDB5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G01270.1; AT5G01270.1; AT5G01270. [Q5YDB5-1]
AT5G01270.2; AT5G01270.2; AT5G01270.
GeneID831743.
KEGGath:AT5G01270.

Organism-specific databases

TAIRAT5G01270.

Phylogenomic databases

eggNOGNOG290259.
HOGENOMHOG000078695.
InParanoidQ5YDB5.

Enzyme and pathway databases

BioCycARA:AT5G01270-MONOMER.
ARA:GQT-1723-MONOMER.

Gene expression databases

GenevestigatorQ5YDB5.

Family and domain databases

Gene3D3.30.160.20. 1 hit.
3.40.50.1000. 3 hits.
InterProIPR014720. dsRNA-bd_dom.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamPF00035. dsrm. 1 hit.
PF03031. NIF. 1 hit.
[Graphical view]
SMARTSM00577. CPDc. 1 hit.
SM00358. DSRM. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 2 hits.
PROSITEPS50137. DS_RBD. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPL2_ARATH
AccessionPrimary (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: June 11, 2014
This is version 71 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names