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 24-JAN-2024, entry version 134. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000072852; -. DR ProteomicsDB; 284140; -. DR Pumba; P58465; -. DR Antibodypedia; 28378; 228 antibodies from 22 providers. DR DNASU; 69274; -. DR Ensembl; ENSMUST00000073109.12; ENSMUSP00000072852.6; ENSMUSG00000047409.14. DR GeneID; 69274; -. DR KEGG; mmu:69274; -. DR UCSC; uc009rzz.2; mouse. DR AGR; MGI:1916524; -. DR CTD; 10217; -. DR MGI; MGI:1916524; Ctdspl. DR VEuPathDB; HostDB:ENSMUSG00000047409; -. DR eggNOG; KOG1605; Eukaryota. DR GeneTree; ENSGT01040000240451; -. DR InParanoid; P58465; -. DR OMA; SHKGNYV; -. DR OrthoDB; 5473812at2759; -. DR PhylomeDB; P58465; -. DR TreeFam; TF313556; -. DR BioGRID-ORCS; 69274; 2 hits in 79 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 213 other cell types or tissues. DR ExpressionAtlas; P58465; baseline and differential. 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: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 CDD; cd07521; HAD_FCP1-like; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR02251; HIF-SF_euk; 1. DR PANTHER; PTHR12210:SF43; CTD SMALL PHOSPHATASE-LIKE PROTEIN; 1. DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1. DR Pfam; PF03031; NIF; 1. DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SMART; SM00577; CPDc; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR PROSITE; PS50969; FCP1; 1. DR Genevisible; P58465; MM. 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 //