DCTP1_RAT
ID DCTP1_RAT Reviewed; 170 AA.
AC Q91VC0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=dCTP pyrophosphatase 1;
DE EC=3.6.1.12 {ECO:0000250|UniProtKB:Q9QY93};
DE AltName: Full=Deoxycytidine-triphosphatase 1;
DE Short=dCTPase 1;
DE AltName: Full=RS21-C6 {ECO:0000312|EMBL:AAK37408.1};
GN Name=Dctpp1 {ECO:0000312|RGD:620933};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Zhang J., Wang H., Chen W.-F.;
RT "Unknown protein homolog to murine RS21-C6.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the
CC corresponding nucleoside monophosphates. Has a strong preference for
CC dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which
CC it may even have a higher efficiency. May protect DNA or RNA against
CC the incorporation of these genotoxic nucleotide analogs through their
CC catabolism. {ECO:0000250|UniProtKB:Q9H773}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dCTP + H2O = dCMP + diphosphate + H(+); Xref=Rhea:RHEA:22636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57566, ChEBI:CHEBI:61481; EC=3.6.1.12;
CC Evidence={ECO:0000250|UniProtKB:Q9QY93};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9QY93};
CC Note=Probably binds two or three Mg(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q9QY93};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9QY93}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9H773}. Note=May also localize to mitochondrion
CC and nucleus. {ECO:0000250|UniProtKB:Q9H773}.
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; AY029335; AAK37408.1; -; mRNA.
DR EMBL; AF331839; AAK38638.1; -; mRNA.
DR RefSeq; NP_620247.1; NM_138892.1.
DR AlphaFoldDB; Q91VC0; -.
DR SMR; Q91VC0; -.
DR STRING; 10116.ENSRNOP00000024074; -.
DR jPOST; Q91VC0; -.
DR PaxDb; Q91VC0; -.
DR Ensembl; ENSRNOT00000024074; ENSRNOP00000024074; ENSRNOG00000017850.
DR GeneID; 192252; -.
DR KEGG; rno:192252; -.
DR UCSC; RGD:620933; rat.
DR CTD; 79077; -.
DR RGD; 620933; Dctpp1.
DR eggNOG; ENOG502S210; Eukaryota.
DR GeneTree; ENSGT00390000017709; -.
DR HOGENOM; CLU_110454_0_1_1; -.
DR InParanoid; Q91VC0; -.
DR OMA; KMDTNRQ; -.
DR OrthoDB; 1472354at2759; -.
DR PhylomeDB; Q91VC0; -.
DR TreeFam; TF300237; -.
DR PRO; PR:Q91VC0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017850; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q91VC0; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0047840; F:dCTP diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:UniProtKB.
DR GO; GO:0032556; F:pyrimidine deoxyribonucleotide binding; ISO:RGD.
DR GO; GO:0016462; F:pyrophosphatase activity; ISO:RGD.
DR GO; GO:0006253; P:dCTP catabolic process; ISS:UniProtKB.
DR GO; GO:0042262; P:DNA protection; ISS:UniProtKB.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; ISS:UniProtKB.
DR CDD; cd11537; NTP-PPase_RS21-C6_like; 1.
DR InterPro; IPR025984; DCTPP.
DR Pfam; PF12643; MazG-like; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H773"
FT CHAIN 2..170
FT /note="dCTP pyrophosphatase 1"
FT /id="PRO_0000291771"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT BINDING 47..51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT BINDING 63
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT BINDING 66
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H773"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H773"
SQ SEQUENCE 170 AA; 18474 MW; 2D344276C3A1228E CRC64;
MSQAGTGVCG NGGQEDSAAA GPFSFSPEPT LEDIRRLHAE FAAERDWEQF HQPRNLLLAL
VGEVGELAEL FQWKSDAEPG PQAWQPKERA ALQEELSDVL IYLVALAARC HVDLPRAVIS
KMDTNRQRYP VHLSRGSACK YTDLPRGTLS ENEAVGSGDP ASELGNQAST
