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 03-AUG-2022, entry version 126.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Shuman S.;
RT "Arabidopsis C-terminal domain phosphatase-like 1 and 2 are essential Ser-
RT 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., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., 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., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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., 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 by
RT analysis of protein data from the completely sequenced genomes of humans,
RT 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., Hagmann J.,
RA Kulcheski F., Manavella P.A.;
RT "KH domain protein RCF3 is a tissue-biased regulator of the plant miRNA
RT 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 the
CC heptad repeats YSPTSPS in the C-terminal domain of the largest RNA
CC polymerase II subunit (RPB1). This promotes the activity of RNA
CC polymerase II. Together with CPL1, required for male gametes fertility.
CC Multifunctional regulator that modulates plant growth, stress, and
CC phytohormones responses. Positive transcription regulator of genes
CC involved in high salinity resistance and auxin mediated signaling
CC pathway. {ECO:0000269|PubMed:15388846, ECO:0000269|PubMed:18506580}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
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+). {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}. Cytoplasm
CC {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 tissues
CC undergoing cell division and expansion, petioles, cotyledons
CC vasculature, leaves, shoot and root meristems, and flowers, especially
CC in buds and organs vasculatures. {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 dark.
CC {ECO:0000269|PubMed:15388846, ECO:0000269|PubMed:18506580}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB69855.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q5YDB5; -.
DR STRING; 3702.AT5G01270.2; -.
DR PaxDb; Q5YDB5; -.
DR PRIDE; Q5YDB5; -.
DR ProteomicsDB; 222635; -. [Q5YDB5-1]
DR EnsemblPlants; AT5G01270.1; AT5G01270.1; AT5G01270. [Q5YDB5-1]
DR GeneID; 831743; -.
DR Gramene; AT5G01270.1; AT5G01270.1; AT5G01270. [Q5YDB5-1]
DR KEGG; ath:AT5G01270; -.
DR Araport; AT5G01270; -.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_010333_0_0_1; -.
DR InParanoid; Q5YDB5; -.
DR OMA; FWCYSVP; -.
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:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
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:0010468; P:regulation of gene expression; IMP:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081; PTHR23081; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00358; DSRM; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Auxin signaling pathway; Cytoplasm;
KW Developmental protein; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..770
FT /note="RNA polymerase II C-terminal domain phosphatase-like
FT 2"
FT /id="PRO_0000376084"
FT DOMAIN 134..385
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT DOMAIN 656..722
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 464..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
