NAKD2_RAT
ID NAKD2_RAT Reviewed; 425 AA.
AC Q1HCL7; Q3B8P3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Guo F., Zhang Z., Dai S., Wang X., Liu L., Liu C., Zhang H., Xiao X.,
RA He D.;
RT "A gene involved in the transition of the hepatocytes from quiescent to
RT proliferating stages.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-425.
RC TISSUE=Spleen;
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].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the NAD kinase 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; DQ504300; ABF56209.1; -; mRNA.
DR EMBL; BC105901; AAI05902.1; -; mRNA.
DR RefSeq; NP_001037717.1; NM_001044252.1.
DR AlphaFoldDB; Q1HCL7; -.
DR IntAct; Q1HCL7; 1.
DR MINT; Q1HCL7; -.
DR STRING; 10116.ENSRNOP00000022455; -.
DR iPTMnet; Q1HCL7; -.
DR PhosphoSitePlus; Q1HCL7; -.
DR PaxDb; Q1HCL7; -.
DR PRIDE; Q1HCL7; -.
DR Ensembl; ENSRNOT00000083799; ENSRNOP00000074419; ENSRNOG00000054157.
DR GeneID; 365699; -.
DR KEGG; rno:365699; -.
DR CTD; 133686; -.
DR RGD; 1306809; Nadk2.
DR eggNOG; KOG4180; Eukaryota.
DR GeneTree; ENSGT00390000006320; -.
DR InParanoid; Q1HCL7; -.
DR Reactome; R-RNO-196807; Nicotinate metabolism.
DR PRO; PR:Q1HCL7; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000054157; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; Q1HCL7; baseline and differential.
DR Genevisible; Q1HCL7; RN.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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; ATP-binding; Kinase; Mitochondrion; NAD; NADP;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..425
FT /note="NAD kinase 2, mitochondrial"
FT /id="PRO_0000296294"
FT REGION 20..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT MOD_RES 59
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0N4"
FT MOD_RES 285
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT MOD_RES 300
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT MOD_RES 300
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0N4"
FT MOD_RES 380
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8C5H8"
SQ SEQUENCE 425 AA; 48116 MW; DFAEBE23AC634BEA CRC64;
MDTSAIQQTL VKIYQRQAWQ PPRKASKNET TVGKPRELAG GGSPADGGFR PSRVVVVAKT
TRYEFEQQRY RYAELSEEDL KQLLALKGSS YSGLLERHHI HTKNVEHIID SLRDEGIEVR
LVKRREYDEE TVRWADAVIA AGGDGTMLLA ASKVLDRLKP VIGVNTDPER SEGHLCLPVR
YTHSFPEALQ KFSRGEFRWL WRQRIRLYLE GTGINPSPVD LHEQQLSLNQ HSRAFNIERV
DDERSEASGP QLLPVRALNE VFIGESLSSR ASYYEISVDD GPWEKQKSSG LNLCTGTGSK
AWSFNINRVA AQAVEDVLNI ARRQGNLTLP LNKELVEKVT NEYNESLLYS PEEPKILFSI
REPIANRVFS SSRQRCFSSK VCVRSRCWDA CMVVDGGTSF EFNDGAIASM MINKEDELRT
VILEQ
