NAKD2_MOUSE
ID NAKD2_MOUSE Reviewed; 452 AA.
AC Q8C5H8; Q3TRP5; Q3UEY1; Q9CTE4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=NAD kinase 2, mitochondrial;
DE EC=2.7.1.23;
DE AltName: Full=Mitochondrial NAD kinase;
DE AltName: Full=NAD kinase domain-containing protein 1, mitochondrial;
DE Flags: Precursor;
GN Name=Nadk2; Synonyms=Mnadk, Nadkd1;
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] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 63-452 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE
RP MRNA] OF 63-452 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF
RP 61-452 (ISOFORM 4).
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Cerebellum, Embryo, Olfactory bulb, and Retina;
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 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).
RN [3]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-64; LYS-312 AND LYS-327, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64; LYS-327 AND LYS-407, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to
CC yield NADP(+). Can use both ATP or inorganic polyphosphate as the
CC phosphoryl donor (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;
CC -!- ACTIVITY REGULATION: Inhibited by NADH, NADPH and NADP(+).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8C5H8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C5H8-2; Sequence=VSP_027195, VSP_027196;
CC Name=3;
CC IsoId=Q8C5H8-3; Sequence=VSP_027195;
CC Name=4;
CC IsoId=Q8C5H8-4; Sequence=VSP_027194, VSP_027195;
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23041.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE28780.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK003858; BAB23041.1; ALT_FRAME; mRNA.
DR EMBL; AK046666; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK078318; BAC37218.1; -; mRNA.
DR EMBL; AK149267; BAE28780.1; ALT_INIT; mRNA.
DR EMBL; AK162601; BAE36982.1; -; mRNA.
DR RefSeq; NP_001035485.2; NM_001040395.4. [Q8C5H8-3]
DR RefSeq; NP_001078879.1; NM_001085410.2. [Q8C5H8-1]
DR RefSeq; NP_001273184.1; NM_001286255.1. [Q8C5H8-4]
DR AlphaFoldDB; Q8C5H8; -.
DR BioGRID; 212970; 2.
DR STRING; 10090.ENSMUSP00000068318; -.
DR iPTMnet; Q8C5H8; -.
DR PhosphoSitePlus; Q8C5H8; -.
DR SwissPalm; Q8C5H8; -.
DR REPRODUCTION-2DPAGE; Q8C5H8; -.
DR REPRODUCTION-2DPAGE; Q9CTE4; -.
DR EPD; Q8C5H8; -.
DR jPOST; Q8C5H8; -.
DR MaxQB; Q8C5H8; -.
DR PaxDb; Q8C5H8; -.
DR PeptideAtlas; Q8C5H8; -.
DR PRIDE; Q8C5H8; -.
DR ProteomicsDB; 287347; -. [Q8C5H8-1]
DR ProteomicsDB; 287348; -. [Q8C5H8-2]
DR ProteomicsDB; 287349; -. [Q8C5H8-3]
DR ProteomicsDB; 287350; -. [Q8C5H8-4]
DR Antibodypedia; 50834; 158 antibodies from 20 providers.
DR DNASU; 68646; -.
DR Ensembl; ENSMUST00000190591; ENSMUSP00000159405; ENSMUSG00000022253. [Q8C5H8-1]
DR GeneID; 68646; -.
DR KEGG; mmu:68646; -.
DR UCSC; uc029sno.2; mouse. [Q8C5H8-1]
DR UCSC; uc029snp.2; mouse. [Q8C5H8-3]
DR UCSC; uc033gta.1; mouse. [Q8C5H8-2]
DR UCSC; uc033gtb.1; mouse. [Q8C5H8-4]
DR CTD; 133686; -.
DR MGI; MGI:1915896; Nadk2.
DR VEuPathDB; HostDB:ENSMUSG00000022253; -.
DR eggNOG; KOG4180; Eukaryota.
DR GeneTree; ENSGT00390000006320; -.
DR InParanoid; Q8C5H8; -.
DR OMA; QGSEGYM; -.
DR OrthoDB; 1416565at2759; -.
DR PhylomeDB; Q8C5H8; -.
DR TreeFam; TF314077; -.
DR Reactome; R-MMU-196807; Nicotinate metabolism.
DR BioGRID-ORCS; 68646; 8 hits in 45 CRISPR screens.
DR ChiTaRS; Nadk2; mouse.
DR PRO; PR:Q8C5H8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8C5H8; protein.
DR Bgee; ENSMUSG00000022253; Expressed in retinal neural layer and 225 other tissues.
DR ExpressionAtlas; Q8C5H8; baseline and differential.
DR Genevisible; Q8C5H8; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019674; P:NAD metabolic process; ISS:UniProtKB.
DR GO; GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002504; NADK.
DR InterPro; IPR012355; NADK2_mit.
DR Pfam; PF01513; NAD_kinase; 1.
DR PIRSF; PIRSF017565; Kin_ATP-NAD_euk; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Kinase; Mitochondrion; NAD;
KW NADP; Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..452
FT /note="NAD kinase 2, mitochondrial"
FT /id="PRO_0000296293"
FT REGION 23..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 64
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0N4"
FT MOD_RES 312
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 327
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 327
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0N4"
FT MOD_RES 407
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 175..202
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027194"
FT VAR_SEQ 276..297
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027195"
FT VAR_SEQ 408..452
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027196"
FT CONFLICT 62
FT /note="V -> G (in Ref. 1; BAB23041)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="S -> P (in Ref. 1; BAB23041)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="R -> S (in Ref. 1; BAB23041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 50859 MW; C0FC67A5BA762D1B CRC64;
MTCYRGFLLG SCRRVAGGRA ALRGSGSGAD GRRHLGHGQP RELAGGGSPA DGGFRPSRVV
VVAKTTRYEF EQQRYRYAEL SEEDLKQLLA LKGSSYSGLL ERHHIHTKNV EHIIDSLRDE
GIEVRLVKRR EYDEETVRWA DAVIAAGGDG TMLLAASKVL DRLKPVIGVN TDPERSEGHL
CLPVRYTHSF PEALRRFSRG EFRWLWRQRI RLYLEGTGIN PTPVDLHEQQ LSLNQHSRAF
NIERAHDERS EASGPQLLPV RALNEVFIGE SLSSRMPYCW AVAVDNLRRD IPNLKGLASY
YEISVDDGPW EKQKSSGLNL CTGTGSKAWS FNINRVAAQA VEDVLHIARR QGNLTLPLNK
DLVEKVTNEY NESLLYSPEE PKILFSIREP IANRVFSSSR QRCFSSKVCV RSRCWDACMV
VDGGTSFEFN DGAIASMMIN KEDELRTVIL EQ
