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Q8LL04 (CPL3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA polymerase II C-terminal domain phosphatase-like 3

Short name=FCP-like 3
EC=3.1.3.16
Alternative name(s):
Carboxyl-terminal phosphatase-like 3
Short name=AtCPL3
Short name=CTD phosphatase-like 3
Gene names
Name:CPL3
Ordered Locus Names:At2g33540
ORF Names:F4P9.31
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1241 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Processively dephosphorylates 'Ser-2' and/or 'Ser-5' 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 By similarity. Negative regulator of stress gene transcription involved in abscisic acid (ABA) mediated signaling pathway and cold resistance. Ref.1 Ref.4

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate. Ref.1

Cofactor

Binds magnesium, cobalt or manganese ions By similarity.

Subunit structure

Interacts with RAP74. Ref.4

Subcellular location

Nucleus Ref.4.

Induction

By NaCl. Ref.4

Domain

The BRCT domain is required for interaction with RAP74. Ref.4

Disruption phenotype

Grows more slowly and flower earlier than wild-type plants. ABA hyperactivation of stress-inducible genes. Ref.1 Ref.4

Sequence similarities

Contains 1 BRCT domain.

Contains 1 FCP1 homology domain.

Sequence caution

The sequence AAB80671.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12411241RNA polymerase II C-terminal domain phosphatase-like 3
PRO_0000376085

Regions

Domain923 – 1103181FCP1 homology
Domain1146 – 123994BRCT
Compositional bias64 – 729Poly-Gly

Experimental info

Sequence conflict10101A → V in AAM94371. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8LL04 [UniParc].

Last modified May 26, 2009. Version 2.
Checksum: CEFFBD725719D404

FASTA1,241136,479
        10         20         30         40         50         60 
MLVARSGCSR TLIRMGNDEN LMVMVDVEEG EIPDSVNTEI EVKHKSTTTT ADVGGDVDVG 

        70         80         90        100        110        120 
VVAGGRGGGG GGSNGNSRVW TMEELISQYP AYRPYANSGL SNLAWARAVQ NKPFNEGLVM 

       130        140        150        160        170        180 
DYEPRESDKI VIEDSDDEKE EGELEEGEID LVDNASDDNL VEKDTESVVL ISADKVEDDR 

       190        200        210        220        230        240 
ILKERDLEKK VKLIRGVLES TSLVEAQTGF EGVCSRILGA LESLRELVSD NDDFPKRDTL 

       250        260        270        280        290        300 
VQLSFASLQT INYVFCSMNN ISKERNKETM SRLLTLVNDH FSQFLSFNQK NEIETMNQDL 

       310        320        330        340        350        360 
SRSAIAVFAG TSSEENVNQM TQPSNGDSFL AKKLTSESTH RGAAYLRSRL PMLPLLDLHK 

       370        380        390        400        410        420 
DHDADSLPSP TRETTPSLPV NGRHTMVRPG FPVGRESQTT EGAKVYSYES DARKAVSTYQ 

       430        440        450        460        470        480 
QKFGLNSVFK TDDLPSPTPS GEPNDGNGDV GGEVSSSVVK SSNPGSHLIY GQDVPLPSNF 

       490        500        510        520        530        540 
NSRSMPVANS VSSTVPPHHL SIHAISAPTA SDQTVKPSAK SRDPRLRLAK PDAANVTIYS 

       550        560        570        580        590        600 
YSSGDARNLS KVELSADLVN PRKQKAADEF LIDGPAWKRQ KSDTDAPKAA GTGGWLEDTE 

       610        620        630        640        650        660 
SSGLLKLESK PRLIENGVTS MTSSVMPTSA VSVSQKVRTA STDTASLQSL LKDIAVNPTM 

       670        680        690        700        710        720 
LLNLLKMGER QKVPEKAIQK PMDPRRAAQL PGSSVQPGVS TPLSIPASNA LAANSLNSGV 

       730        740        750        760        770        780 
LQDSSQNAPA AESGSIRMKP RDPRRILHGS TLQRTDSSME KQTKVNDPST LGTLTMKGKA 

       790        800        810        820        830        840 
EDLETPPQLD PRQNISQNGT SKMKISGELL SGKTPDFSTQ FTKNLKSIAD MVVVSQQLGN 

       850        860        870        880        890        900 
PPASMHSVQL KTERDVKHNP SNPNAQDEDV SVSAASVTAA AGPTRSMNSW GDVEHLFEGY 

       910        920        930        940        950        960 
DDIQRVAIQR ERVRRLEEQN KMFASQKLSL VLDIDHTLLN SAKFNEVESR HEEILRKKEE 

       970        980        990       1000       1010       1020 
QDREKPYRHL FRFLHMGMWT KLRPGIWNFL EKASKLYELH LYTMGNKLYA TEMAKLLDPK 

      1030       1040       1050       1060       1070       1080 
GVLFNGRVIS KGDDGDPLDG DERVPKSKDL EGVMGMESSV VIIDDSVRVW PQHKMNLIAV 

      1090       1100       1110       1120       1130       1140 
ERYLYFPCSR RQFGLLGPSL LELDRDEVPE EGTLASSLAV IEKIHQNFFS HTSLDEVDVR 

      1150       1160       1170       1180       1190       1200 
NILASEQRKI LAGCRIVFSR IIPVGEAKPH LHPLWQTAEQ FGAVCTTQVD EHVTHVVTNS 

      1210       1220       1230       1240 
LGTDKVNWAL TRGRFVVHPG WVEASAFLYQ RANENLYAIN P 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [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]"Arabidopsis carboxyl-terminal domain phosphatase-like isoforms share common catalytic and interaction domains but have distinct in planta functions."
Bang W., Kim S., Ueda A., Vikram M., Yun D., Bressan R.A., Hasegawa P.M., Bahk J., Koiwa H.
Plant Physiol. 142:586-594(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAP74, DISRUPTION PHENOTYPE, INDUCTION BY NACL, BRCT DOMAIN, SUBCELLULAR LOCATION.
[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.
[6]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF486633 mRNA. Translation: AAM94371.1.
AC002332 Genomic DNA. Translation: AAB80671.1. Sequence problems.
CP002685 Genomic DNA. Translation: AEC08850.1.
PIRG84746.
RefSeqNP_180912.2. NM_128914.2.
UniGeneAt.43643.

3D structure databases

ProteinModelPortalQ8LL04.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid3266. 1 interaction.

Proteomic databases

PaxDbQ8LL04.
PRIDEQ8LL04.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G33540.1; AT2G33540.1; AT2G33540.
GeneID817919.
KEGGath:AT2G33540.

Organism-specific databases

TAIRAT2G33540.

Phylogenomic databases

eggNOGCOG5190.
HOGENOMHOG000085035.
InParanoidQ8LL04.
OMAHPLWQTA.
PhylomeDBQ8LL04.
ProtClustDBCLSN2680006.

Enzyme and pathway databases

BioCycARA:AT2G33540-MONOMER.

Gene expression databases

GenevestigatorQ8LL04.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
IPR011947. FCP1_euk.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamPF00533. BRCT. 1 hit.
PF03031. NIF. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
SM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMSSF52113. SSF52113. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR02250. FCP1_euk. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPL3_ARATH
AccessionPrimary (citable) accession number: Q8LL04
Secondary accession number(s): O22804
Entry history
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: May 26, 2009
Last modified: March 19, 2014
This is version 71 of the entry and version 2 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