NTPCR_MOUSE
ID NTPCR_MOUSE Reviewed; 190 AA.
AC Q9CQA9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Cancer-related nucleoside-triphosphatase homolog;
DE Short=NTPase;
DE EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9BSD7};
DE AltName: Full=Nucleoside triphosphate phosphohydrolase;
GN Name=Ntpcr {ECO:0000312|MGI:MGI:1913816};
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; TISSUE=Hippocampus, Testis, and Tongue;
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=FVB/N; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.
CC {ECO:0000250|UniProtKB:Q9BSD7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + TTP = H(+) + phosphate + TDP; Xref=Rhea:RHEA:65580,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61417, ChEBI:CHEBI:63527;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65581;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58069;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9BSD7}.
CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000305}.
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DR EMBL; AK006433; BAB24586.1; -; mRNA.
DR EMBL; AK010229; BAB26783.1; -; mRNA.
DR EMBL; AK010823; BAB27206.1; -; mRNA.
DR EMBL; AK019321; BAB31665.1; -; mRNA.
DR EMBL; BC025168; AAH25168.1; -; mRNA.
DR CCDS; CCDS22781.1; -.
DR RefSeq; NP_001297617.1; NM_001310688.1.
DR RefSeq; NP_079912.1; NM_025636.5.
DR AlphaFoldDB; Q9CQA9; -.
DR SMR; Q9CQA9; -.
DR BioGRID; 211557; 4.
DR STRING; 10090.ENSMUSP00000034313; -.
DR PhosphoSitePlus; Q9CQA9; -.
DR EPD; Q9CQA9; -.
DR MaxQB; Q9CQA9; -.
DR PaxDb; Q9CQA9; -.
DR PeptideAtlas; Q9CQA9; -.
DR PRIDE; Q9CQA9; -.
DR ProteomicsDB; 291918; -.
DR Antibodypedia; 34690; 155 antibodies from 27 providers.
DR DNASU; 66566; -.
DR Ensembl; ENSMUST00000034313; ENSMUSP00000034313; ENSMUSG00000031851.
DR GeneID; 66566; -.
DR KEGG; mmu:66566; -.
DR UCSC; uc009nyk.2; mouse.
DR CTD; 84284; -.
DR MGI; MGI:1913816; Ntpcr.
DR VEuPathDB; HostDB:ENSMUSG00000031851; -.
DR eggNOG; ENOG502QVJ8; Eukaryota.
DR GeneTree; ENSGT00390000018683; -.
DR HOGENOM; CLU_103145_1_0_1; -.
DR InParanoid; Q9CQA9; -.
DR OMA; GAMEFKC; -.
DR OrthoDB; 1401569at2759; -.
DR PhylomeDB; Q9CQA9; -.
DR TreeFam; TF323592; -.
DR BioGRID-ORCS; 66566; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ntpcr; mouse.
DR PRO; PR:Q9CQA9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CQA9; protein.
DR Bgee; ENSMUSG00000031851; Expressed in spermatocyte and 240 other tissues.
DR ExpressionAtlas; Q9CQA9; baseline and differential.
DR Genevisible; Q9CQA9; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00796; NTPase_1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004948; Nuc-triphosphatase_THEP1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43146; PTHR43146; 1.
DR Pfam; PF03266; NTPase_1; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..190
FT /note="Cancer-related nucleoside-triphosphatase homolog"
FT /id="PRO_0000146712"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSD7"
SQ SEQUENCE 190 AA; 20667 MW; A6B9C6DFDFB06813 CRC64;
MSRHVFLTGP PGVGKTTLIQ KAIEVLQSSG LPVDGFYTQE VRQEGKRIGF DVVTLSGAQG
PLSRVGSQPL PGKPECRVGQ YVVNLDSFEQ LALPVLRNAG SSCGPKHRVC IIDEIGKMEL
FSQPFIQAVR QMLSTPGIIV VGTIPVPKGK PLALVEEIRK RRDVKVFNVT RDNRNSLLPD
IVAVVQSSRT
