CTDS2_MOUSE
ID CTDS2_MOUSE Reviewed; 270 AA.
AC Q8BX07;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2;
DE EC=3.1.3.16;
DE AltName: Full=Small C-terminal domain phosphatase 2;
DE AltName: Full=Small CTD phosphatase 2;
DE Short=SCP2;
GN Name=Ctdsp2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 TISSUE SPECIFICITY.
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. 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 -!- TISSUE SPECIFICITY: Expression is restricted to non-neuronal tissues.
CC {ECO:0000269|PubMed:15681389}.
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DR EMBL; AK049271; BAC33649.1; -; mRNA.
DR EMBL; BC085142; AAH85142.1; -; mRNA.
DR CCDS; CCDS48711.1; -.
DR RefSeq; NP_001106941.1; NM_001113470.1.
DR RefSeq; NP_666124.1; NM_146012.2.
DR AlphaFoldDB; Q8BX07; -.
DR SMR; Q8BX07; -.
DR STRING; 10090.ENSMUSP00000100891; -.
DR PhosphoSitePlus; Q8BX07; -.
DR SwissPalm; Q8BX07; -.
DR EPD; Q8BX07; -.
DR MaxQB; Q8BX07; -.
DR PaxDb; Q8BX07; -.
DR PRIDE; Q8BX07; -.
DR ProteomicsDB; 285216; -.
DR Antibodypedia; 8503; 298 antibodies from 28 providers.
DR Ensembl; ENSMUST00000105256; ENSMUSP00000100891; ENSMUSG00000078429.
DR GeneID; 52468; -.
DR KEGG; mmu:52468; -.
DR UCSC; uc007hhj.2; mouse.
DR CTD; 10106; -.
DR MGI; MGI:1098748; Ctdsp2.
DR VEuPathDB; HostDB:ENSMUSG00000078429; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240451; -.
DR HOGENOM; CLU_020262_4_0_1; -.
DR InParanoid; Q8BX07; -.
DR OMA; ANTIAKX; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q8BX07; -.
DR TreeFam; TF313556; -.
DR BioGRID-ORCS; 52468; 6 hits in 70 CRISPR screens.
DR ChiTaRS; Ctdsp2; mouse.
DR PRO; PR:Q8BX07; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BX07; protein.
DR Bgee; ENSMUSG00000078429; Expressed in ventricular zone and 70 other tissues.
DR ExpressionAtlas; Q8BX07; baseline and differential.
DR Genevisible; Q8BX07; 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; ISO:MGI.
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 GO; GO:0006470; P:protein dephosphorylation; 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 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Metal-binding; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..270
FT /note="Carboxy-terminal domain RNA polymerase II
FT polypeptide A small phosphatase 2"
FT /id="PRO_0000212575"
FT DOMAIN 96..254
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT ACT_SITE 106
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 162
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 200
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14595"
SQ SEQUENCE 270 AA; 30546 MW; 0098B97E0AEC1B1D CRC64;
MEHGSIITQA RREDALVLTK QGLVSKSSPK KPRGRSIFKA LLCCFHTQHV VQSSSSTELT
HKEEANTIAK SDLLQCLQYQ FYQIPGTCLL PEVTEQDQGR ICVVIDLDET LVHSSFKPIN
NADFIVPVEI EGTTHQVYVL KRPYVDEFLR RMGELFECVL FTASLAKYAD PVTDLLDRCG
VFRARLFREA CVFHQGCYVK DLSRLGRDLR KTVILDNSPA SYIFHPENAV PVQSWFDDMA
DTELLNLIPV FEELSGTDDV YTSLGQLRAP
