CPL4_ARATH
ID CPL4_ARATH Reviewed; 440 AA.
AC Q00IB6; Q9FJL6;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=RNA polymerase II C-terminal domain phosphatase-like 4;
DE Short=FCP-like 4;
DE EC=3.1.3.16;
DE AltName: Full=Carboxyl-terminal phosphatase-like 4;
DE Short=AtCPL4;
DE Short=CTD phosphatase-like 4;
GN Name=CPL4; OrderedLocusNames=At5g58003; ORFNames=MTI20;
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, INTERACTION WITH RAP74, INDUCTION BY
RP NACL, BRCT DOMAIN, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16905668; DOI=10.1104/pp.106.084939;
RA Bang W., Kim S., Ueda A., Vikram M., Yun D., Bressan R.A., Hasegawa P.M.,
RA Bahk J., Koiwa H.;
RT "Arabidopsis carboxyl-terminal domain phosphatase-like isoforms share
RT common catalytic and interaction domains but have distinct in planta
RT functions.";
RL Plant Physiol. 142:586-594(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 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).
CC -!- FUNCTION: Processively dephosphorylates 'Ser-2' and/or 'Ser-5' 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 (By similarity). Required for normal plant growth.
CC {ECO:0000250, ECO:0000269|PubMed:16905668}.
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; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds Mg(2+), Co(2+) or Mn(2+). {ECO:0000250};
CC -!- SUBUNIT: Interacts with RAP74. {ECO:0000269|PubMed:16905668}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16905668}.
CC -!- INDUCTION: By NaCl. {ECO:0000269|PubMed:16905668}.
CC -!- DOMAIN: The BRCT domain is required for interaction with RAP74.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08870.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At5g58000 and At5g58003.; Evidence={ECO:0000305};
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DR EMBL; DQ503426; ABF55959.1; -; mRNA.
DR EMBL; AB013396; BAB08870.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96984.1; -; Genomic_DNA.
DR RefSeq; NP_001078764.1; NM_001085295.2.
DR AlphaFoldDB; Q00IB6; -.
DR SMR; Q00IB6; -.
DR BioGRID; 624522; 4.
DR STRING; 3702.AT5G58003.1; -.
DR PaxDb; Q00IB6; -.
DR PRIDE; Q00IB6; -.
DR ProteomicsDB; 220487; -.
DR EnsemblPlants; AT5G58003.1; AT5G58003.1; AT5G58003.
DR GeneID; 5008312; -.
DR Gramene; AT5G58003.1; AT5G58003.1; AT5G58003.
DR KEGG; ath:AT5G58003; -.
DR Araport; AT5G58003; -.
DR TAIR; locus:4010714056; AT5G58003.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_023960_1_0_1; -.
DR InParanoid; Q00IB6; -.
DR OrthoDB; 683531at2759; -.
DR PhylomeDB; Q00IB6; -.
DR PRO; PR:Q00IB6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q00IB6; baseline and differential.
DR Genevisible; Q00IB6; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0008022; F:protein C-terminus binding; IPI: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:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02250; FCP1_euk; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Nucleus; Reference proteome; Repressor;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..440
FT /note="RNA polymerase II C-terminal domain phosphatase-like
FT 4"
FT /id="PRO_0000376086"
FT DOMAIN 118..292
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT DOMAIN 337..429
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 50264 MW; 7712641DC888B82B CRC64;
MSVASDSPVH SSSSSDDLAA FLDAELDSAS DASSGPSEEE EAEDDVESGL KRQKLEHLEE
ASSSKGECEH PGSFGNMCFV CGQKLEETGV SFRYIHKEMR LNEDEISRLR DSDSRFLQRQ
RKLYLVLDLD HTLLNTTILR DLKPEEEYLK SHTHSLQDGC NVSGGSLFLL EFMQMMTKLR
PFVHSFLKEA SEMFVMYIYT MGDRNYARQM AKLLDPKGEY FGDRVISRDD GTVRHEKSLD
VVLGQESAVL ILDDTENAWP KHKDNLIVIE RYHFFSSSCR QFDHRYKSLS ELKSDESEPD
GALATVLKVL KQAHALFFEN VDEGISNRDV RLMLKQVRKE ILKGCKIVFS RVFPTKAKPE
DHPLWKMAEE LGATCATEVD ASVTHVVAMD VGTEKARWAV REKKYVVHRG WIDAANYLWM
KQPEENFGLE QLKKQLTEEE
