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Q5YDB5

- CPL2_ARATH

UniProt

Q5YDB5 - CPL2_ARATH

Protein

RNA polymerase II C-terminal domain phosphatase-like 2

Gene

CPL2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 3 (16 Nov 2011)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

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

    Cofactori

    Binds magnesium, cobalt or manganese ions.1 Publication

    pH dependencei

    Optimum pH is 5.5-6.0.1 Publication

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: UniProtKB-EC
    3. phosphoserine phosphatase activity Source: UniProtKB
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. auxin-activated signaling pathway Source: UniProtKB
    2. dephosphorylation Source: GOC
    3. multicellular organismal development Source: UniProtKB-KW
    4. positive regulation of transcription, DNA-templated Source: UniProtKB
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Developmental protein, Hydrolase

    Keywords - Biological processi

    Auxin signaling pathway, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, RNA-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase II C-terminal domain phosphatase-like 2 (EC:3.1.3.16)
    Short name:
    FCP-like 2
    Alternative name(s):
    Carboxyl-terminal phosphatase-like 2
    Short name:
    AtCPL2
    Short name:
    CTD phosphatase-like 2
    Gene namesi
    Name:CPL2
    Ordered Locus Names:At5g01270
    ORF Names:F7J8.250
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G01270.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 770770RNA polymerase II C-terminal domain phosphatase-like 2PRO_0000376084Add
    BLAST

    Proteomic databases

    PaxDbiQ5YDB5.
    PRIDEiQ5YDB5.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    GenevestigatoriQ5YDB5.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT5G01270.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5YDB5.
    SMRiQ5YDB5. Positions 655-725.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini134 – 385252FCP1 homologyPROSITE-ProRule annotationAdd
    BLAST
    Domaini656 – 72267DRBMPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 DRBM (double-stranded RNA-binding) domain.PROSITE-ProRule annotation
    Contains 1 FCP1 homology domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG290259.
    HOGENOMiHOG000078695.
    InParanoidiQ5YDB5.

    Family and domain databases

    Gene3Di3.30.160.20. 1 hit.
    3.40.50.1000. 3 hits.
    InterProiIPR014720. dsRNA-bd_dom.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view]
    PfamiPF00035. dsrm. 1 hit.
    PF03031. NIF. 1 hit.
    [Graphical view]
    SMARTiSM00577. CPDc. 1 hit.
    SM00358. DSRM. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 2 hits.
    PROSITEiPS50137. DS_RBD. 1 hit.
    PS50969. FCP1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. Align

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

    Isoform 1 (identifier: Q5YDB5-1) [UniParc]FASTAAdd to Basket

    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.

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    MNRLGHKSVV YHGDLRLGEL DVNHVSSSHE FRFPNDEIRI HHLSPAGERC    50
    PPLAILQTIA SFAVRCKLES SAPVKSQELM HLHAVCFHEL KTAVVMLGDE 100
    EIHLVAMPSK EKKFPCFWCF SVPSGLYDSC LRMLNTRCLS IVFDLDETLI 150
    VANTMKSFED RIEALKSWIS REMDPVRING MSAELKRYMD DRMLLKQYID 200
    NDYAFDNGVL LKAQPEEVRP TSDGQEKVCR PVIRLPEKNT VLTRIKPEIR 250
    DTSVLVKLRP AWEELRSYLT AKTRKRFEVY VCTMAERDYA LEMWRLLDPE 300
    AHLISLKELR DRIVCVKPDA KKSLLSVFNG GICHPKMAMV IDDRMKVWED 350
    KDQPRVHVVS AYLPYYAPQA ETALVVPHLC VARNVACNVR GYFFKEFDES 400
    LMSSISLVYY EDDVENLPPS PDVSNYVVIE DPGFASNGNI NAPPINEGMC 450
    GGEVERRLNQ AAAADHSTLP ATSNAEQKPE TPKPQIAVIP NNASTATAAA 500
    LLPSHKPSLL GAPRRDGFTF SDGGRPLMMR PGVDIRNQNF NQPPILAKIP 550
    MQPPSSSMHS PGGWLVDDEN RPSFPGRPSG LYPSQFPHGT PGSAPVGPFA 600
    HPSHLRSEEV AMDDDLKRQN PSRQTTEGGI SQNHLVSNGR EHHTDGGKSN 650
    GGQSHLFVSA LQEIGRRCGS KVEFRTVIST NKELQFSVEV LFTGEKIGIG 700
    MAKTKKDAHQ QAAENALRSL AEKYVAHVAP LARETEKGPE NDNGFLWESS 750
    EDVSNKGLEE EAPKENISEL 770
    Length:770
    Mass (Da):85,953
    Last modified:November 16, 2011 - v3
    Checksum:i7672B4F18397CB14
    GO

    Sequence cautioni

    The sequence CAB69855.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY557187 mRNA. Translation: AAT52023.1.
    AL137189 Genomic DNA. Translation: CAB69855.1. Sequence problems.
    CP002688 Genomic DNA. Translation: AED90320.1.
    PIRiT45967.
    RefSeqiNP_195747.2. NM_120205.4. [Q5YDB5-1]
    UniGeneiAt.21936.

    Genome annotation databases

    EnsemblPlantsiAT5G01270.1; AT5G01270.1; AT5G01270. [Q5YDB5-1]
    AT5G01270.2; AT5G01270.2; AT5G01270.
    GeneIDi831743.
    KEGGiath:AT5G01270.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY557187 mRNA. Translation: AAT52023.1 .
    AL137189 Genomic DNA. Translation: CAB69855.1 . Sequence problems.
    CP002688 Genomic DNA. Translation: AED90320.1 .
    PIRi T45967.
    RefSeqi NP_195747.2. NM_120205.4. [Q5YDB5-1 ]
    UniGenei At.21936.

    3D structure databases

    ProteinModelPortali Q5YDB5.
    SMRi Q5YDB5. Positions 655-725.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT5G01270.1-P.

    Proteomic databases

    PaxDbi Q5YDB5.
    PRIDEi Q5YDB5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G01270.1 ; AT5G01270.1 ; AT5G01270 . [Q5YDB5-1 ]
    AT5G01270.2 ; AT5G01270.2 ; AT5G01270 .
    GeneIDi 831743.
    KEGGi ath:AT5G01270.

    Organism-specific databases

    TAIRi AT5G01270.

    Phylogenomic databases

    eggNOGi NOG290259.
    HOGENOMi HOG000078695.
    InParanoidi Q5YDB5.

    Enzyme and pathway databases

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

    Gene expression databases

    Genevestigatori Q5YDB5.

    Family and domain databases

    Gene3Di 3.30.160.20. 1 hit.
    3.40.50.1000. 3 hits.
    InterProi IPR014720. dsRNA-bd_dom.
    IPR023214. HAD-like_dom.
    IPR004274. NIF.
    [Graphical view ]
    Pfami PF00035. dsrm. 1 hit.
    PF03031. NIF. 1 hit.
    [Graphical view ]
    SMARTi SM00577. CPDc. 1 hit.
    SM00358. DSRM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 2 hits.
    PROSITEi PS50137. DS_RBD. 1 hit.
    PS50969. FCP1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiCPL2_ARATH
    AccessioniPrimary (citable) accession number: Q5YDB5
    Secondary accession number(s): F4K803, Q9LFA9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 26, 2009
    Last sequence update: November 16, 2011
    Last modified: October 1, 2014
    This is version 72 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3