NDKM_HUMAN
ID NDKM_HUMAN Reviewed; 187 AA.
AC O00746; A2IDD0; Q5U0M9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Nucleoside diphosphate kinase, mitochondrial {ECO:0000305};
DE Short=NDK;
DE Short=NDP kinase, mitochondrial;
DE EC=2.7.4.6 {ECO:0000269|PubMed:10799505};
DE AltName: Full=Nucleoside diphosphate kinase D;
DE Short=NDPKD;
DE AltName: Full=nm23-H4;
DE Flags: Precursor;
GN Name=NME4 {ECO:0000312|HGNC:HGNC:7852}; Synonyms=NM23D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Stomach;
RX PubMed=9099850; DOI=10.1007/s004390050405;
RA Milon L., Rousseau-Merck M.-F., Munier A., Erent M., Lascu I., Capeau J.,
RA Lacombe M.-L.;
RT "nm23-H4, a new member of the family of human nm23/nucleoside diphosphate
RT kinase genes localised on chromosome 16p13.";
RL Hum. Genet. 99:550-557(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and Uterus;
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 [7]
RP FUNCTION.
RX PubMed=17028143; DOI=10.1529/biophysj.106.092353;
RA Epand R.F., Schlattner U., Wallimann T., Lacombe M.L., Epand R.M.;
RT "Novel lipid transfer property of two mitochondrial proteins that bridge
RT the inner and outer membranes.";
RL Biophys. J. 92:126-137(2007).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, PHOSPHOLIPID-BINDING, MUTAGENESIS OF
RP ARG-90, AND ACTIVITY REGULATION.
RX PubMed=18635542; DOI=10.1074/jbc.m803132200;
RA Tokarska-Schlattner M., Boissan M., Munier A., Borot C., Mailleau C.,
RA Speer O., Schlattner U., Lacombe M.L.;
RT "The nucleoside diphosphate kinase D (NM23-H4) binds the inner
RT mitochondrial membrane with high affinity to cardiolipin and couples
RT nucleotide transfer with respiration.";
RL J. Biol. Chem. 283:26198-26207(2008).
RN [9]
RP FUNCTION, MUTAGENESIS OF ARG-90, INTERACTION WITH OPA1, CATALYTIC ACTIVITY,
RP AND ACTIVITY REGULATION.
RX PubMed=23150663; DOI=10.1074/jbc.m112.408633;
RA Schlattner U., Tokarska-Schlattner M., Ramirez S., Tyurina Y.Y.,
RA Amoscato A.A., Mohammadyani D., Huang Z., Jiang J., Yanamala N.,
RA Seffouh A., Boissan M., Epand R.F., Epand R.M., Klein-Seetharaman J.,
RA Lacombe M.L., Kagan V.E.;
RT "Dual function of mitochondrial Nm23-H4 protein in phosphotransfer and
RT intermembrane lipid transfer: a cardiolipin-dependent switch.";
RL J. Biol. Chem. 288:111-121(2013).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24970086; DOI=10.1126/science.1253768;
RA Boissan M., Montagnac G., Shen Q., Griparic L., Guitton J., Romao M.,
RA Sauvonnet N., Lagache T., Lascu I., Raposo G., Desbourdes C.,
RA Schlattner U., Lacombe M.L., Polo S., van der Bliek A.M., Roux A.,
RA Chavrier P.;
RT "Membrane trafficking. Nucleoside diphosphate kinases fuel dynamin
RT superfamily proteins with GTP for membrane remodeling.";
RL Science 344:1510-1515(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), CHARACTERIZATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10799505; DOI=10.1074/jbc.275.19.14264;
RA Milon L., Meyer P., Chiadmi M., Munier A., Johansson M., Karlsson A.,
RA Lascu I., Capeau J., Janin J., Lacombe M.-L.;
RT "The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate
RT kinase.";
RL J. Biol. Chem. 275:14264-14272(2000).
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. Through the catalyzed exchange of gamma-phosphate between
CC di- and triphosphonucleosides participates in regulation of
CC intracellular nucleotide homeostasis (PubMed:10799505). Binds to
CC anionic phospholipids, predominantly to cardiolipin; the binding
CC inhibits its phosphotransfer activity (PubMed:18635542,
CC PubMed:23150663). Acts as mitochondria-specific NDK; its association
CC with cardiolipin-containing mitochondrial inner membrane is coupled to
CC respiration suggesting that ADP locally regenerated in the
CC mitochondrion innermembrane space by its activity is directly taken up
CC via ANT ADP/ATP translocase into the matrix space to stimulate
CC respiratory ATP regeneration (PubMed:18635542). Proposed to increase
CC GTP-loading on dynamin-related GTPase OPA1 in mitochondria
CC (PubMed:24970086). In vitro can induce liposome cross-linking
CC suggesting that it can cross-link inner and outer membranes to form
CC contact sites, and promotes intermembrane migration of anionic
CC phosphoplipids. Promotes the redistribution of cardiolipin between the
CC mitochondrial inner membrane and outer membrane which is implicated in
CC pro-apoptotic signaling (PubMed:18635542, PubMed:17028143,
CC PubMed:23150663). {ECO:0000269|PubMed:10799505,
CC ECO:0000269|PubMed:17028143, ECO:0000269|PubMed:18635542,
CC ECO:0000269|PubMed:23150663, ECO:0000305, ECO:0000305|PubMed:24970086}.
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 Evidence={ECO:0000269|PubMed:10799505};
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 Evidence={ECO:0000269|PubMed:10799505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cardiolipin(in) = a cardiolipin(out); Xref=Rhea:RHEA:38695,
CC ChEBI:CHEBI:62237; Evidence={ECO:0000269|PubMed:23150663};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38696;
CC Evidence={ECO:0000305|PubMed:23150663};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Binding to anionic phospholipids, predominantly to
CC cardiolipin inhibits its phosphotransfer activity.
CC {ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:23150663}.
CC -!- SUBUNIT: Homohexamer (PubMed:10799505). Interacts with OPA1
CC (PubMed:23150663). Interacts with CAPN8 (By similarity).
CC {ECO:0000250|UniProtKB:Q9WV84, ECO:0000269|PubMed:10799505,
CC ECO:0000269|PubMed:23150663}.
CC -!- INTERACTION:
CC O00746; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-744871, EBI-11096309;
CC O00746; P01019: AGT; NbExp=3; IntAct=EBI-744871, EBI-751728;
CC O00746; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-744871, EBI-742909;
CC O00746; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-744871, EBI-1166928;
CC O00746; P54253: ATXN1; NbExp=6; IntAct=EBI-744871, EBI-930964;
CC O00746; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-744871, EBI-2837444;
CC O00746; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-744871, EBI-725606;
CC O00746; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-744871, EBI-8643161;
CC O00746; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-744871, EBI-12011224;
CC O00746; Q9NP86: CABP5; NbExp=3; IntAct=EBI-744871, EBI-10311131;
CC O00746; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-744871, EBI-10171570;
CC O00746; Q2TAC2-2: CCDC57; NbExp=5; IntAct=EBI-744871, EBI-10961624;
CC O00746; P55273: CDKN2D; NbExp=3; IntAct=EBI-744871, EBI-745859;
CC O00746; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-744871, EBI-749051;
CC O00746; Q99828: CIB1; NbExp=3; IntAct=EBI-744871, EBI-372594;
CC O00746; Q96Q77: CIB3; NbExp=3; IntAct=EBI-744871, EBI-10292696;
CC O00746; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-744871, EBI-7062247;
CC O00746; Q86UW9: DTX2; NbExp=3; IntAct=EBI-744871, EBI-740376;
CC O00746; P02042: HBD; NbExp=3; IntAct=EBI-744871, EBI-6152722;
CC O00746; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-744871, EBI-12094670;
CC O00746; O75031: HSF2BP; NbExp=3; IntAct=EBI-744871, EBI-7116203;
CC O00746; P42858: HTT; NbExp=20; IntAct=EBI-744871, EBI-466029;
CC O00746; P03952: KLKB1; NbExp=3; IntAct=EBI-744871, EBI-10087153;
CC O00746; P61968: LMO4; NbExp=3; IntAct=EBI-744871, EBI-2798728;
CC O00746; P06858: LPL; NbExp=3; IntAct=EBI-744871, EBI-715909;
CC O00746; Q13064: MKRN3; NbExp=3; IntAct=EBI-744871, EBI-2340269;
CC O00746; P40692: MLH1; NbExp=3; IntAct=EBI-744871, EBI-744248;
CC O00746; P15531: NME1; NbExp=11; IntAct=EBI-744871, EBI-741141;
CC O00746; P22392: NME2; NbExp=5; IntAct=EBI-744871, EBI-713693;
CC O00746; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-744871, EBI-744782;
CC O00746; P61970: NUTF2; NbExp=3; IntAct=EBI-744871, EBI-591778;
CC O00746; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-744871, EBI-398874;
CC O00746; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-744871, EBI-721769;
CC O00746; O15160: POLR1C; NbExp=5; IntAct=EBI-744871, EBI-1055079;
CC O00746; P20618: PSMB1; NbExp=3; IntAct=EBI-744871, EBI-372273;
CC O00746; P37840: SNCA; NbExp=3; IntAct=EBI-744871, EBI-985879;
CC O00746; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-744871, EBI-742688;
CC O00746; Q9UMX1: SUFU; NbExp=3; IntAct=EBI-744871, EBI-740595;
CC O00746; Q13148: TARDBP; NbExp=6; IntAct=EBI-744871, EBI-372899;
CC O00746; O14656-2: TOR1A; NbExp=3; IntAct=EBI-744871, EBI-25847109;
CC O00746; P0DI81-3: TRAPPC2; NbExp=3; IntAct=EBI-744871, EBI-11961968;
CC O00746; Q15645: TRIP13; NbExp=4; IntAct=EBI-744871, EBI-358993;
CC O00746; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-744871, EBI-3918381;
CC O00746; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-744871, EBI-948354;
CC O00746; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-744871, EBI-607755;
CC O00746; P40337-2: VHL; NbExp=3; IntAct=EBI-744871, EBI-12157263;
CC O00746; Q05516: ZBTB16; NbExp=3; IntAct=EBI-744871, EBI-711925;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:18635542}; Peripheral membrane protein.
CC Mitochondrion matrix {ECO:0000305|PubMed:18635542}. Note=Predominantly
CC localized in the mitochondrion intermembrane space (PubMed:18635542).
CC Colocalizes with OPA1 in mitochondria (PubMed:24970086).
CC {ECO:0000269|PubMed:18635542, ECO:0000269|PubMed:24970086}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00746-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00746-2; Sequence=VSP_054743;
CC -!- TISSUE SPECIFICITY: Widely distributed. Found at very high levels in
CC prostate, heart, liver, small intestine, and skeletal muscle tissues,
CC and in low amounts in the brain and in blood leukocytes.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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; Y07604; CAA68877.1; -; mRNA.
DR EMBL; BT019438; AAV38245.1; -; mRNA.
DR EMBL; AE006463; AAK61230.1; -; Genomic_DNA.
DR EMBL; Z97634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85818.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85819.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85820.1; -; Genomic_DNA.
DR EMBL; BC004880; AAH04880.1; -; mRNA.
DR EMBL; BC017067; AAH17067.1; -; mRNA.
DR CCDS; CCDS10408.1; -. [O00746-1]
DR CCDS; CCDS66886.1; -. [O00746-2]
DR RefSeq; NP_001273362.1; NM_001286433.1.
DR RefSeq; NP_001273364.1; NM_001286435.1.
DR RefSeq; NP_001273365.1; NM_001286436.1. [O00746-2]
DR RefSeq; NP_001273367.1; NM_001286438.1. [O00746-2]
DR RefSeq; NP_001273368.1; NM_001286439.1. [O00746-2]
DR RefSeq; NP_001273369.1; NM_001286440.1. [O00746-2]
DR RefSeq; NP_005000.1; NM_005009.2. [O00746-1]
DR PDB; 1EHW; X-ray; 2.40 A; A/B=33-175.
DR PDBsum; 1EHW; -.
DR AlphaFoldDB; O00746; -.
DR SMR; O00746; -.
DR BioGRID; 110897; 183.
DR IntAct; O00746; 120.
DR MINT; O00746; -.
DR STRING; 9606.ENSP00000219479; -.
DR SwissLipids; SLP:000000360; -.
DR iPTMnet; O00746; -.
DR PhosphoSitePlus; O00746; -.
DR BioMuta; NME4; -.
DR EPD; O00746; -.
DR jPOST; O00746; -.
DR MassIVE; O00746; -.
DR MaxQB; O00746; -.
DR PaxDb; O00746; -.
DR PeptideAtlas; O00746; -.
DR PRIDE; O00746; -.
DR ProteomicsDB; 449; -.
DR ProteomicsDB; 48013; -. [O00746-1]
DR Antibodypedia; 34896; 405 antibodies from 26 providers.
DR DNASU; 4833; -.
DR Ensembl; ENST00000219479.7; ENSP00000219479.2; ENSG00000103202.13. [O00746-1]
DR Ensembl; ENST00000397722.5; ENSP00000380834.1; ENSG00000103202.13. [O00746-2]
DR Ensembl; ENST00000450036.1; ENSP00000389048.1; ENSG00000103202.13. [O00746-2]
DR Ensembl; ENST00000620944.4; ENSP00000479996.1; ENSG00000103202.13. [O00746-2]
DR GeneID; 4833; -.
DR KEGG; hsa:4833; -.
DR MANE-Select; ENST00000219479.7; ENSP00000219479.2; NM_005009.3; NP_005000.1.
DR UCSC; uc002cgz.4; human. [O00746-1]
DR CTD; 4833; -.
DR DisGeNET; 4833; -.
DR GeneCards; NME4; -.
DR HGNC; HGNC:7852; NME4.
DR HPA; ENSG00000103202; Low tissue specificity.
DR MIM; 601818; gene.
DR neXtProt; NX_O00746; -.
DR OpenTargets; ENSG00000103202; -.
DR PharmGKB; PA31657; -.
DR VEuPathDB; HostDB:ENSG00000103202; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000160286; -.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; O00746; -.
DR OMA; LLNWECC; -.
DR OrthoDB; 1334716at2759; -.
DR PhylomeDB; O00746; -.
DR TreeFam; TF106373; -.
DR BRENDA; 2.7.4.6; 2681.
DR PathwayCommons; O00746; -.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR SignaLink; O00746; -.
DR BioGRID-ORCS; 4833; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; NME4; human.
DR EvolutionaryTrace; O00746; -.
DR GeneWiki; NME4; -.
DR GenomeRNAi; 4833; -.
DR Pharos; O00746; Tbio.
DR PRO; PR:O00746; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O00746; protein.
DR Bgee; ENSG00000103202; Expressed in stromal cell of endometrium and 200 other tissues.
DR ExpressionAtlas; O00746; baseline and differential.
DR Genevisible; O00746; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:BHF-UCL.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1901612; F:cardiolipin binding; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IDA:BHF-UCL.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0009116; P:nucleoside metabolic process; TAS:ProtInc.
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 3D-structure; Alternative splicing; ATP-binding; Direct protein sequencing;
KW Kinase; Lipid transport; Lipid-binding; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Nucleotide metabolism; Nucleotide-binding;
KW Reference proteome; Transferase; Transit peptide; Transport.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..187
FT /note="Nucleoside diphosphate kinase, mitochondrial"
FT /id="PRO_0000019432"
FT ACT_SITE 151
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054743"
FT MUTAGEN 90
FT /note="R->D: Abolishes cardiolipin-containing membrane
FT binding; decreases lipid transfer and pro-apoptotic
FT activity; does not change phosphotransfer activity."
FT /evidence="ECO:0000269|PubMed:18635542,
FT ECO:0000269|PubMed:23150663"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1EHW"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:1EHW"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:1EHW"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:1EHW"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:1EHW"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1EHW"
SQ SEQUENCE 187 AA; 20659 MW; A56FEF18A7D712D4 CRC64;
MGGLFWRSAL RGLRCGPRAP GPSLLVRHGS GGPSWTRERT LVAVKPDGVQ RRLVGDVIQR
FERRGFTLVG MKMLQAPESV LAEHYQDLRR KPFYPALIRY MSSGPVVAMV WEGYNVVRAS
RAMIGHTDSA EAAPGTIRGD FSVHISRNVI HASDSVEGAQ REIQLWFQSS ELVSWADGGQ
HSSIHPA
