NDK3_MOUSE
ID NDK3_MOUSE Reviewed; 169 AA.
AC Q9WV85; Q9D931; Q9EPA2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Nucleoside diphosphate kinase 3;
DE Short=NDK 3;
DE Short=NDP kinase 3;
DE EC=2.7.4.6;
DE AltName: Full=DR-nm23;
DE AltName: Full=Nucleoside diphosphate kinase C;
DE Short=NDPKC;
DE AltName: Full=nm23-M3;
GN Name=Nme3;
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].
RA Mehus J.G., Lambeth D.O.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=12383506; DOI=10.1016/s0378-1119(02)00836-3;
RA Masse K., Dabernat S., Bourbon P.-M., Larou M., Amrein L., Barraud P.,
RA Perel Y., Camara M., Landry M., Lacombe M.L., Daniel J.-Y.;
RT "Characterization of the nm23-M2, nm23-M3 and nm23-M4 mouse genes:
RT comparison with their human orthologs.";
RL Gene 296:87-97(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Major role in the synthesis of nucleoside triphosphates other
CC than ATP. The ATP gamma phosphate is transferred to the NDP beta
CC phosphate via a ping-pong mechanism, using a phosphorylated active-site
CC intermediate. Probably has a role in normal hematopoiesis by inhibition
CC of granulocyte differentiation and induction of apoptosis (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; AF153449; AAD38976.1; -; mRNA.
DR EMBL; AF288689; AAG02199.1; -; mRNA.
DR EMBL; AF288691; AAG02201.1; -; Genomic_DNA.
DR EMBL; AK007399; BAB25013.1; -; mRNA.
DR EMBL; BC028503; AAH28503.1; -; mRNA.
DR CCDS; CCDS28503.1; -.
DR RefSeq; NP_062704.2; NM_019730.2.
DR AlphaFoldDB; Q9WV85; -.
DR SMR; Q9WV85; -.
DR BioGRID; 219731; 7.
DR STRING; 10090.ENSMUSP00000024978; -.
DR iPTMnet; Q9WV85; -.
DR PhosphoSitePlus; Q9WV85; -.
DR SwissPalm; Q9WV85; -.
DR EPD; Q9WV85; -.
DR jPOST; Q9WV85; -.
DR MaxQB; Q9WV85; -.
DR PaxDb; Q9WV85; -.
DR PeptideAtlas; Q9WV85; -.
DR PRIDE; Q9WV85; -.
DR ProteomicsDB; 293535; -.
DR Antibodypedia; 23225; 209 antibodies from 25 providers.
DR DNASU; 79059; -.
DR Ensembl; ENSMUST00000024978; ENSMUSP00000024978; ENSMUSG00000073435.
DR GeneID; 79059; -.
DR KEGG; mmu:79059; -.
DR UCSC; uc008ayz.2; mouse.
DR CTD; 4832; -.
DR MGI; MGI:1930182; Nme3.
DR VEuPathDB; HostDB:ENSMUSG00000073435; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000161283; -.
DR HOGENOM; CLU_060216_6_2_1; -.
DR InParanoid; Q9WV85; -.
DR OMA; WFRAEEL; -.
DR OrthoDB; 1334716at2759; -.
DR PhylomeDB; Q9WV85; -.
DR TreeFam; TF106373; -.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 79059; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Nme3; mouse.
DR PRO; PR:Q9WV85; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9WV85; protein.
DR Bgee; ENSMUSG00000073435; Expressed in bone marrow and 79 other tissues.
DR Genevisible; Q9WV85; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:MGI.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006231; P:dTMP biosynthetic process; NAS:MGI.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.141; -; 1.
DR HAMAP; MF_00451; NDP_kinase; 1.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00562; NDK; 1.
DR SUPFAM; SSF54919; SSF54919; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..169
FT /note="Nucleoside diphosphate kinase 3"
FT /id="PRO_0000137124"
FT ACT_SITE 135
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 97
FT /note="G -> W (in Ref. 1; AAD38976)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="M -> V (in Ref. 2; AAG02199/AAG02201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 19099 MW; 53223C0601A6467C CRC64;
MICLVLTIFA NLFPSAYSGV NERTFLAVKP DGVQRRLVGE IVRRFERKGF KLVALKLVQA
SEELLREHYV ELREKPFYSR LVKYMSSGPV VAMVWQGLDV VHASRALIGA TDPGDAMPGT
IRGDFCMEVG KNVIHGSDSV ESAHREIALW FREAELLCWE DSAGHWLYE
