CTDS1_MOUSE
ID CTDS1_MOUSE Reviewed; 261 AA.
AC P58466;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1;
DE EC=3.1.3.16;
DE AltName: Full=Golli-interacting protein;
DE Short=GIP;
DE AltName: Full=Nuclear LIM interactor-interacting factor 3;
DE Short=NLI-interacting factor 3;
DE AltName: Full=Small C-terminal domain phosphatase 1;
DE Short=SCP1;
DE Short=Small CTD phosphatase 1;
GN Name=Ctdsp1; Synonyms=Nif3, Nliif;
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 Fernandes A.O., Campagnoni C.W., Kampf K., Handley V.W., Schonmann V.,
RA Bongarzone E.R., Campagnoni A.T.;
RT "The golli products of the myelin basic protein gene are associated with
RT LIM-binding proteins in the brain.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-96 AND ASP-98.
RX PubMed=15681389; DOI=10.1126/science.1100801;
RA Yeo M., Lee S.-K., Lee B., Ruiz E.C., Pfaff S.L., Gill G.N.;
RT "Small CTD phosphatases function in silencing neuronal gene expression.";
RL Science 307:596-600(2005).
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 (By
CC similarity). Recruited by REST to neuronal genes that contain RE-1
CC elements, leading to neuronal gene silencing in non-neuronal cells.
CC {ECO:0000250, ECO:0000269|PubMed:15681389}.
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 -!- INTERACTION:
CC P58466; Q9GZU7: CTDSP1; Xeno; NbExp=2; IntAct=EBI-7091612, EBI-751587;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to non-neuronal tissues.
CC {ECO:0000269|PubMed:15681389}.
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DR EMBL; AY028804; AAK83555.1; -; mRNA.
DR EMBL; BC065158; AAH65158.1; -; mRNA.
DR EMBL; BC079638; AAH79638.1; -; mRNA.
DR CCDS; CCDS15048.1; -.
DR RefSeq; NP_694728.1; NM_153088.2.
DR AlphaFoldDB; P58466; -.
DR SMR; P58466; -.
DR BioGRID; 230610; 1.
DR IntAct; P58466; 2.
DR MINT; P58466; -.
DR STRING; 10090.ENSMUSP00000027367; -.
DR iPTMnet; P58466; -.
DR PhosphoSitePlus; P58466; -.
DR SwissPalm; P58466; -.
DR EPD; P58466; -.
DR jPOST; P58466; -.
DR PaxDb; P58466; -.
DR PeptideAtlas; P58466; -.
DR PRIDE; P58466; -.
DR ProteomicsDB; 283976; -.
DR Antibodypedia; 34272; 425 antibodies from 33 providers.
DR DNASU; 227292; -.
DR Ensembl; ENSMUST00000027367; ENSMUSP00000027367; ENSMUSG00000026176.
DR GeneID; 227292; -.
DR KEGG; mmu:227292; -.
DR UCSC; uc007blz.2; mouse.
DR CTD; 58190; -.
DR MGI; MGI:2654470; Ctdsp1.
DR VEuPathDB; HostDB:ENSMUSG00000026176; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240451; -.
DR HOGENOM; CLU_020262_4_0_1; -.
DR InParanoid; P58466; -.
DR OMA; CLCHDES; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; P58466; -.
DR TreeFam; TF313556; -.
DR BioGRID-ORCS; 227292; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ctdsp1; mouse.
DR PRO; PR:P58466; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P58466; protein.
DR Bgee; ENSMUSG00000026176; Expressed in granulocyte and 74 other tissues.
DR ExpressionAtlas; P58466; baseline and differential.
DR Genevisible; P58466; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IDA:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO: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 1: Evidence at protein level;
KW Acetylation; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..261
FT /note="Carboxy-terminal domain RNA polymerase II
FT polypeptide A small phosphatase 1"
FT /id="PRO_0000212573"
FT DOMAIN 86..244
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 152
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 190
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZU7"
FT MUTAGEN 96
FT /note="D->E: Leads to enhanced neuronal differentiation of
FT stem cells; when associated with N-98."
FT /evidence="ECO:0000269|PubMed:15681389"
FT MUTAGEN 98
FT /note="D->N: Leads to enhanced neuronal differentiation of
FT stem cells; when associated with E-96."
FT /evidence="ECO:0000269|PubMed:15681389"
SQ SEQUENCE 261 AA; 29266 MW; BFB4471390FE9091 CRC64;
MDSSAVITQI SKEEARGPLR GKGDQKSAVS QKPRSRGILH SLFCCVCRDD GEPLPAHSGA
PLLVEENGAI PKHTPVQYLL PEAKAQDSDK ICVVIDLDET LVHSSFKPVN NADFIIPVEI
DGVVHQVYVL KRPHVDEFLQ RMGELFECVL FTASLAKYAD PVADLLDKWG AFRARLFRES
CVFHRGNYVK DLSRLGRDLR RVLILDNSPA SYVFHPDNAV PVASWFDNMS DTELHDLLPF
FEQLSRVDDV YSVLRQPRPG S
