CTDSL_MOUSE
ID CTDSL_MOUSE Reviewed; 276 AA.
AC P58465; Q52KL5;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=CTD small phosphatase-like protein;
DE Short=CTDSP-like;
DE EC=3.1.3.16;
DE AltName: Full=Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 3;
DE AltName: Full=NIF-like protein;
DE AltName: Full=Nuclear LIM interactor-interacting factor 1;
DE Short=NLI-interacting factor 1;
DE AltName: Full=Small C-terminal domain phosphatase 3;
DE Short=SCP3;
DE Short=Small CTD phosphatase 3;
GN Name=Ctdspl; Synonyms=Nif1, Nifl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Protopopov A., Kashuba V., Zabarovsky E.;
RT "Refined physical mapping and genomic structure of a 4-Mb region (AP-20) on
RT human chromosome 3p22-p21.33 implicated in lung and kidney
RT cancerogenesis.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Preferentially catalyzes the dephosphorylation of 'Ser-5'
CC within the tandem 7 residue repeats in the C-terminal domain (CTD) of
CC the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA
CC polymerase II transcription, possibly by controlling the transition
CC from initiation/capping to processive transcript elongation. Recruited
CC by REST to neuronal genes that contain RE-1 elements, leading to
CC neuronal gene silencing in non-neuronal cells (By similarity).
CC {ECO:0000250}.
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 Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250};
CC -!- SUBUNIT: Monomer. Interacts with REST. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AJ344340; CAC69078.2; -; mRNA.
DR EMBL; AC055818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094289; AAH94289.1; -; mRNA.
DR CCDS; CCDS23605.1; -.
DR RefSeq; NP_598471.3; NM_133710.3.
DR AlphaFoldDB; P58465; -.
DR SMR; P58465; -.
DR STRING; 10090.ENSMUSP00000072852; -.
DR iPTMnet; P58465; -.
DR PhosphoSitePlus; P58465; -.
DR SwissPalm; P58465; -.
DR jPOST; P58465; -.
DR PaxDb; P58465; -.
DR PRIDE; P58465; -.
DR ProteomicsDB; 284140; -.
DR Antibodypedia; 28378; 184 antibodies from 22 providers.
DR DNASU; 69274; -.
DR Ensembl; ENSMUST00000073109; ENSMUSP00000072852; ENSMUSG00000047409.
DR GeneID; 69274; -.
DR KEGG; mmu:69274; -.
DR UCSC; uc009rzz.2; mouse.
DR CTD; 10217; -.
DR MGI; MGI:1916524; Ctdspl.
DR VEuPathDB; HostDB:ENSMUSG00000047409; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240451; -.
DR InParanoid; P58465; -.
DR OMA; SMRAYCD; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; P58465; -.
DR TreeFam; TF313556; -.
DR BioGRID-ORCS; 69274; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ctdspl; mouse.
DR PRO; PR:P58465; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P58465; protein.
DR Bgee; ENSMUSG00000047409; Expressed in humerus cartilage element and 210 other tissues.
DR ExpressionAtlas; P58465; baseline and differential.
DR Genevisible; P58465; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:MGI.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
DR Pfam; PF03031; NIF; 1.
DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Metal-binding; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..276
FT /note="CTD small phosphatase-like protein"
FT /id="PRO_0000212570"
FT DOMAIN 102..260
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 168
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 206
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 37
FT /note="Q -> E (in Ref. 1; CAC69078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 31156 MW; 3989E5B2E57EEC75 CRC64;
MDGPAIITQV TNPKEDEARS PVAGEKASQR NISLKKQRGR SILSSFFCCF RDYNVEAPPA
NSPSVLPPLV EENGGLQKGD QRQVIPVPSP PAKYLLPEVT VLDYGKKCVV IDLDETLVHS
SFKPISNADF IVPVEIDGTI HQVYVLKRPH VDEFLQRMGQ LFECVLFTAS LAKYADPVAD
LLDRWGVFRA RLFRESCVFH RGNYVKDLSR LGRELSKVII VDNSPASYIF HPENAVPVQS
WFDDMTDTEL LDLIPFFEGL SREDDVYSML HRLCSR
