Reviewed, UniProtKB/Swiss-Prot Q9JI75 (NQO2_MOUSE)

Names and origin

Protein names

Recommended name:
    Ribosyldihydronicotinamide dehydrogenase [quinone]
    EC=1.10.99.2
Alternative name(s):
    NRH dehydrogenase [quinone] 2
    NRH:quinone oxidoreductase 2
      Short name=Quinone reductase 2
      Short name=QR2

Gene names

Name:	Nqo2
Synonyms:	Nmor2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	231 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.
Catalytic activity	1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone.
Cofactor	Binds 1 zinc ion per subunit By similarity. FAD By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor.
Sequence similarities	Belongs to the NAD(P)H dehydrogenase (quinone) family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein Metal-binding Zinc
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	coenzyme binding Inferred from electronic annotation. Source: InterPro dihydronicotinamide riboside quinone reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 231	230	Ribosyldihydronicotinamide dehydrogenase [quinone]		PRO_0000071627
Regions
	Nucleotide binding	18 – 21	4	FAD By similarity
	Nucleotide binding	104 – 107	4	FAD By similarity
	Nucleotide binding	148 – 151	4	FAD By similarity
	Region	127 – 129	3	Substrate binding By similarity
Sites
	Metal binding	174	1	Zinc By similarity
	Metal binding	178	1	Zinc By similarity
	Metal binding	223	1	Zinc By similarity
	Binding site	12	1	FAD By similarity
	Binding site	156	1	FAD By similarity
	Binding site	194	1	FAD By similarity
	Binding site	201	1	FAD By similarity
Amino acid modifications
	Modified residue	31	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9JI75-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D5D9AB805C4AD9F5	FASTA	231	26,248
	10 20 30 40 50 60 MAGKKVLIVY AHQEPKSFNG SLKKVAVEEL SKQGCTVTVS DLYSMNFEPR ATRNDITGAP 70 80 90 100 110 120 SNPDVFSYGI ETHEAYKKKA LTSDIFEEQR KVQEADLVIF QFPLYWFSVP AILKGWMDRV 130 140 150 160 170 180 LCRGFAFDIP GFYDSGFLKG KLALLSLTTG GTAEMYTKDG VSGDFRYFLW PLQHGTLHFC 190 200 210 220 230 GFKVLAPQIS FGLDVSSEEE RKVMLASWAQ RLKSIWKEEP IHCTPPWYFQ E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse NRH:quinone oxidoreductase (NQO2): cloning of cDNA and gene- and tissue-specific expression." Long D.J. II, Jaiswal A.K. Gene 252:107-117(2000) [PubMed: 10903442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Kidney.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryonic liver.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF252260 mRNA. Translation: AAF97785.1. AF254081 , AF254076, AF254077, AF254078, AF254079, AF254080 Genomic DNA. Translation: AAF97789.1. AK010842 mRNA. Translation: BAB27217.1. BC027629 mRNA. Translation: AAH27629.1.
IPI	IPI00266614.
RefSeq	NP_064678.1.
UniGene	Mm.252210 Mm.264036
3D structure databases
HSSP	HSSP built from PDB template 1QR2 based on UniProtKB P16083.
SMR	Q9JI75. Positions 2-231.
ModBase	Search...
PTM databases
PhosphoSite	Q9JI75.
Genome annotation databases
Ensembl	ENSMUSG00000046949. Mus musculus. [Contig view]
GeneID	18105.
KEGG	mmu:18105.
NMPDR	fig|10090.3.peg.27682.
Organism-specific databases
MGI	MGI:104513. Nqo2.
Phylogenomic databases
HOVERGEN	Q9JI75.
Enzyme and pathway databases
BRENDA	1.10.99.2. 244.
Gene expression databases
ArrayExpress	Q9JI75.
Bgee	Q9JI75.
CleanEx	MM_NQO2.
GermOnline	ENSMUSG00000046949. Mus musculus.
Family and domain databases
InterPro	IPR003680. Flavodoxin_fold. [Graphical view]
Pfam	PF02525. Flavodoxin_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	293285.
SOURCE	Search...

Entry information

Entry name

NQO2_MOUSE

Accession

Primary (citable) accession number: Q9JI75

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 61 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)