(data stored in ACNUC13479 zone)

SWISSPROT: CPL2_ARATH

ID   CPL2_ARATH              Reviewed;         770 AA.
AC   Q5YDB5; F4K803; Q9LFA9;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   30-AUG-2017, entry version 99.
DE   RecName: Full=RNA polymerase II C-terminal domain phosphatase-like 2;
DE            Short=FCP-like 2;
DE            EC=3.1.3.16;
DE   AltName: Full=Carboxyl-terminal phosphatase-like 2;
DE            Short=AtCPL2;
DE            Short=CTD phosphatase-like 2;
GN   Name=CPL2; OrderedLocusNames=At5g01270; ORFNames=F7J8.250;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND COFACTOR.
RX   PubMed=15388846; DOI=10.1073/pnas.0403174101;
RA   Koiwa H., Hausmann S., Bang W.Y., Ueda A., Kondo N., Hiraguri A.,
RA   Fukuhara T., Bahk J.D., Yun D.-J., Bressan R.A., Hasegawa P.M.,
RA   Shuman S.;
RT   "Arabidopsis C-terminal domain phosphatase-like 1 and 2 are essential
RT   Ser-5-specific C-terminal domain phosphatases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14539-14544(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=18506580; DOI=10.1007/s11103-008-9348-y;
RA   Ueda A., Li P., Feng Y., Vikram M., Kim S., Kang C.H., Kang J.S.,
RA   Bahk J.D., Lee S.Y., Fukuhara T., Staswick P.E., Pepper A.E.,
RA   Koiwa H.;
RT   "The Arabidopsis thaliana carboxyl-terminal domain phosphatase-like 2
RT   regulates plant growth, stress and auxin responses.";
RL   Plant Mol. Biol. 67:683-697(2008).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=18156295; DOI=10.1104/pp.107.111393;
RA   Kerk D., Templeton G., Moorhead G.B.G.;
RT   "Evolutionary radiation pattern of novel protein phosphatases revealed
RT   by analysis of protein data from the completely sequenced genomes of
RT   humans, green algae, and higher plants.";
RL   Plant Physiol. 146:351-367(2008).
RN   [6]
RP   INTERACTION WITH RCF3.
RX   PubMed=26512101; DOI=10.1073/pnas.1512865112;
RA   Karlsson P., Christie M.D., Seymour D.K., Wang H., Wang X.,
RA   Hagmann J., Kulcheski F., Manavella P.A.;
RT   "KH domain protein RCF3 is a tissue-biased regulator of the plant
RT   miRNA biogenesis cofactor HYL1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:14096-14101(2015).
CC   -!- FUNCTION: Processively dephosphorylates 'Ser-5' but not 'Ser-2' of
CC       the heptad repeats YSPTSPS in the C-terminal domain of the largest
CC       RNA polymerase II subunit (RPB1). This promotes the activity of
CC       RNA polymerase II. Together with CPL1, required for male gametes
CC       fertility. Multifunctional regulator that modulates plant growth,
CC       stress, and phytohormones responses. Positive transcription
CC       regulator of genes involved in high salinity resistance and auxin
CC       mediated signaling pathway. {ECO:0000269|PubMed:15388846,
CC       ECO:0000269|PubMed:18506580}.
CC   -!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
CC       = [a protein]-serine/threonine + phosphate.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15388846};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:15388846};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:15388846};
CC       Note=Binds Mg(2+), Co(2+) or Mn(2+).
CC       {ECO:0000269|PubMed:15388846};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:15388846};
CC   -!- SUBUNIT: Interacts with RCF3. {ECO:0000269|PubMed:26512101}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15388846}.
CC       Cytoplasm {ECO:0000269|PubMed:15388846}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q5YDB5-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, particularly in
CC       tissues undergoing cell division and expansion, petioles,
CC       cotyledons vasculature, leaves, shoot and root meristems, and
CC       flowers, especially in buds and organs vasculatures.
CC       {ECO:0000269|PubMed:18506580}.
CC   -!- DISRUPTION PHENOTYPE: Leaf expansion defects, early flowering, low
CC       fertility, and increased salt (NaCl) sensitivity. Produces shorter
CC       hypocotyls than wild-type plants in the light, but not in the
CC       dark. {ECO:0000269|PubMed:15388846, ECO:0000269|PubMed:18506580}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB69855.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AY557187; AAT52023.1; -; mRNA.
DR   EMBL; AL137189; CAB69855.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90320.1; -; Genomic_DNA.
DR   PIR; T45967; T45967.
DR   RefSeq; NP_195747.2; NM_120205.5. [Q5YDB5-1]
DR   UniGene; At.21936; -.
DR   ProteinModelPortal; Q5YDB5; -.
DR   STRING; 3702.AT5G01270.2; -.
DR   PaxDb; Q5YDB5; -.
DR   PRIDE; Q5YDB5; -.
DR   EnsemblPlants; AT5G01270.1; AT5G01270.1; AT5G01270. [Q5YDB5-1]
DR   GeneID; 831743; -.
DR   Gramene; AT5G01270.1; AT5G01270.1; AT5G01270.
DR   KEGG; ath:AT5G01270; -.
DR   Araport; AT5G01270; -.
DR   eggNOG; KOG0323; Eukaryota.
DR   eggNOG; COG5190; LUCA.
DR   HOGENOM; HOG000078695; -.
DR   InParanoid; Q5YDB5; -.
DR   KO; K18998; -.
DR   PRO; PR:Q5YDB5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q5YDB5; baseline and differential.
DR   Genevisible; Q5YDB5; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008420; F:CTD phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004647; F:phosphoserine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SUPFAM; SSF56784; SSF56784; 2.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q5YDB5.
DR   SWISS-2DPAGE; Q5YDB5.
KW   Activator; Alternative splicing; Auxin signaling pathway;
KW   Complete proteome; Cytoplasm; Developmental protein; Hydrolase;
KW   Metal-binding; Nucleus; Reference proteome; RNA-binding;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    770       RNA polymerase II C-terminal domain
FT                                phosphatase-like 2.
FT                                /FTId=PRO_0000376084.
FT   DOMAIN      134    385       FCP1 homology. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00336}.
FT   DOMAIN      656    722       DRBM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00266}.
SQ   SEQUENCE   770 AA;  85953 MW;  7672B4F18397CB14 CRC64;
     MNRLGHKSVV YHGDLRLGEL DVNHVSSSHE FRFPNDEIRI HHLSPAGERC PPLAILQTIA
     SFAVRCKLES SAPVKSQELM HLHAVCFHEL KTAVVMLGDE EIHLVAMPSK EKKFPCFWCF
     SVPSGLYDSC LRMLNTRCLS IVFDLDETLI VANTMKSFED RIEALKSWIS REMDPVRING
     MSAELKRYMD DRMLLKQYID NDYAFDNGVL LKAQPEEVRP TSDGQEKVCR PVIRLPEKNT
     VLTRIKPEIR DTSVLVKLRP AWEELRSYLT AKTRKRFEVY VCTMAERDYA LEMWRLLDPE
     AHLISLKELR DRIVCVKPDA KKSLLSVFNG GICHPKMAMV IDDRMKVWED KDQPRVHVVS
     AYLPYYAPQA ETALVVPHLC VARNVACNVR GYFFKEFDES LMSSISLVYY EDDVENLPPS
     PDVSNYVVIE DPGFASNGNI NAPPINEGMC GGEVERRLNQ AAAADHSTLP ATSNAEQKPE
     TPKPQIAVIP NNASTATAAA LLPSHKPSLL GAPRRDGFTF SDGGRPLMMR PGVDIRNQNF
     NQPPILAKIP MQPPSSSMHS PGGWLVDDEN RPSFPGRPSG LYPSQFPHGT PGSAPVGPFA
     HPSHLRSEEV AMDDDLKRQN PSRQTTEGGI SQNHLVSNGR EHHTDGGKSN GGQSHLFVSA
     LQEIGRRCGS KVEFRTVIST NKELQFSVEV LFTGEKIGIG MAKTKKDAHQ QAAENALRSL
     AEKYVAHVAP LARETEKGPE NDNGFLWESS EDVSNKGLEE EAPKENISEL
//

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