CPL5_ARATH
ID CPL5_ARATH Reviewed; 601 AA.
AC F4JCB2; C0LW35; Q9LJN6; Q9LJN7;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=RNA polymerase II C-terminal domain phosphatase-like 5 {ECO:0000303|PubMed:21231936};
DE Short=FCP-like 5 {ECO:0000303|PubMed:21231936};
DE EC=3.1.3.16 {ECO:0000269|PubMed:21231936};
DE AltName: Full=Carboxyl-terminal phosphatase-like 5 {ECO:0000303|PubMed:21231936};
DE Short=AtCPL5 {ECO:0000303|PubMed:21231936};
DE Short=CTD phosphatase-like 5 {ECO:0000303|PubMed:21231936};
GN Name=CPL5 {ECO:0000303|PubMed:21231936};
GN OrderedLocusNames=At3g19600 {ECO:0000312|Araport:AT3G19600};
GN ORFNames=MMB12.6 {ECO:0000312|EMBL:BAB02544.1},
GN MMB12.7 {ECO:0000312|EMBL:BAB02545.1};
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, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION BY ABSCISIC ACID; SALT; COLD
RP AND DROUGHT, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=21231936; DOI=10.1111/j.1469-8137.2010.03601.x;
RA Jin Y.-M., Jung J., Jeon H., Won S.Y., Feng Y., Kang J.-S., Lee S.Y.,
RA Cheong J.-J., Koiwa H., Kim M.;
RT "AtCPL5, a novel Ser-2-specific RNA polymerase II C-terminal domain
RT phosphatase, positively regulates ABA and drought responses in
RT Arabidopsis.";
RL New Phytol. 190:57-74(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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).
CC -!- FUNCTION: Mediates the dephosphorylation of 'Ser-2' of the heptad
CC repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase
CC II subunit (RPB1). This promotes the activity of RNA polymerase II.
CC Regulates positively abscisic acid (ABA) and drought responses,
CC including the regulation of specific genes expression.
CC {ECO:0000269|PubMed:21231936}.
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 Evidence={ECO:0000269|PubMed:21231936};
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 Evidence={ECO:0000269|PubMed:21231936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21231936}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, hypocotyls,
CC cotyledons, leaves, siliques and flowers.
CC {ECO:0000269|PubMed:21231936}.
CC -!- DEVELOPMENTAL STAGE: In the vegetative stage, first detected in the
CC seed coat upon germination and in the hypocotyl of young seedlings. In
CC seedlings, expressed in roots (mostly in primary roots), hypocotyl,
CC rosette leaves and cotyledons. In rosette leaves, observed in the
CC vascular tissue of major veins, guard cells and trichomes. During the
CC reproductive stage, expressed in flower buds, stems, stamens, carpels
CC and funiculi of siliques. {ECO:0000269|PubMed:21231936}.
CC -!- INDUCTION: Induced transiently by abscisic acid (ABA), salt (NaCl),
CC cold and drought. {ECO:0000269|PubMed:21231936}.
CC -!- DISRUPTION PHENOTYPE: Weak abscisic acid (ABA) hyposensitivity during
CC the early stages of seedling development. Slighty decreased drought
CC stress tolerance. {ECO:0000269|PubMed:21231936}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE76264.1; Type=Erroneous gene model prediction; Note=The predicted split genes At3g19595 and At3g19600 have been merged into a single gene: At3g19600.; Evidence={ECO:0000305};
CC Sequence=BAB02544.1; Type=Erroneous gene model prediction; Note=The predicted split genes At3g19595 and At3g19600 have been merged into a single gene: At3g19600.; Evidence={ECO:0000305};
CC Sequence=BAB02545.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ773993; ACN81954.1; -; mRNA.
DR EMBL; AP000417; BAB02544.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP000417; BAB02545.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76264.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76265.2; -; Genomic_DNA.
DR PIR; T52387; T52387.
DR PIR; T52388; T52388.
DR RefSeq; NP_001118664.1; NM_001125192.1.
DR RefSeq; NP_001319592.1; NM_001338410.1.
DR AlphaFoldDB; F4JCB2; -.
DR SMR; F4JCB2; -.
DR STRING; 3702.AT3G19595.1; -.
DR PaxDb; F4JCB2; -.
DR PRIDE; F4JCB2; -.
DR DNASU; 6241385; -.
DR EnsemblPlants; AT3G19600.1; AT3G19600.1; AT3G19600.
DR GeneID; 6241385; -.
DR GeneID; 821497; -.
DR Gramene; AT3G19600.1; AT3G19600.1; AT3G19600.
DR KEGG; ath:AT3G19595; -.
DR KEGG; ath:AT3G19600; -.
DR Araport; AT3G19600; -.
DR TAIR; locus:2091221; AT3G19600.
DR TAIR; locus:4515103095; AT3G19595.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_023960_0_0_1; -.
DR InParanoid; F4JCB2; -.
DR OMA; GWASEME; -.
DR OrthoDB; 683531at2759; -.
DR PRO; PR:F4JCB2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JCB2; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR011947; FCP1_euk.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081; PTHR23081; 2.
DR Pfam; PF03031; NIF; 2.
DR SMART; SM00577; CPDc; 2.
DR SUPFAM; SSF56784; SSF56784; 2.
DR TIGRFAMs; TIGR02250; FCP1_euk; 2.
DR PROSITE; PS50969; FCP1; 2.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Activator; Hydrolase; Nucleus;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..601
FT /note="RNA polymerase II C-terminal domain phosphatase-like
FT 5"
FT /id="PRO_0000445685"
FT DOMAIN 84..259
FT /note="FCP1 homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT DOMAIN 381..553
FT /note="FCP1 homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 69150 MW; 4BC3976083AFD7CB CRC64;
MFVAKNLSPE RESKRQKKEP EIMEPSFPLL SPNNCGHWYI RYGFCIVCKS TVDKTIEGRV
FDGLHLSSEA LALTKRLITK FSCLNMKKLH LVLDLDLTLI HSVRVPCLSE AEKYLIEEAG
STTREDLWKM KVRGDPISIT IEHLVKLRPF LCEFLKEANE MFTMYVYTKG TRPYAEAILK
LIDPKKLYFG HRVITRNESP HTKTLDMVLA DERGVVIVDD TRKAWPNNKS NLVLIGRYNY
FRSQSRVLKP HSEEKTDESE NNGGLANVLK LLKGIHHKFF KVEEEVESQD VRLTMSVVEN
FSSEPKAKRR KIEPTINESS SSLSSSSSCG HWYICHGICI GCKSTVKKSQ GRAFDYIFDG
LQLSHEAVAL TKCFTTKLSC LNEKKLHLVL DLDHTLLHTV MVPSLSQAEK YLIEEAGSAT
RDDLWKIKAV GDPMEFLTKL RPFLRDFLKE ANEFFTMYVY TKGSRVYAKQ VLELIDPKKL
YFGDRVITKT ESPHMKTLDF VLAEERGVVI VDDTRNVWPD HKSNLVDISK YSYFRLKGQD
SMPYSEEKTD ESESEGGLAN VLKLLKEVHQ RFFRVEEELE SKDVRSLLQE IDFELNVESV
E
