Reviewed, UniProtKB/Swiss-Prot Q3KNK3 (NB5R2_MOUSE)

Names and origin

Protein names

Recommended name:
    NADH-cytochrome b5 reductase 2
      Short name=b5R.2
    EC=1.6.2.2

Gene names

Name:

Cyb5r2

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	276 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. Responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1) By similarity.
Catalytic activity	NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.
Cofactor	FAD By similarity.
Sequence similarities	Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Coding sequence diversity	Alternative splicing
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q3KNK3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q3KNK3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     130-130: G → GCQTRAAEVKNIFIFLG

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 276	276	NADH-cytochrome b5 reductase 2		PRO_0000287549
Regions
	Domain	15 – 127	113	FAD-binding FR-type
	Nucleotide binding	107 – 137	31	FAD By similarity
	Nucleotide binding	146 – 181	36	FAD By similarity
Amino acid modifications
	Modified residue	177	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	130	1	G → GCQTRAAEVKNIFIFLG in isoform 2.		VSP_025560
Experimental info
	Sequence conflict	132	1	L → I in AAI07239. Ref.2
	Sequence conflict	267	1	S → G in AAI07239. Ref.2
	Sequence conflict	275	1	I → T in AAI07239. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 15, 2007. Version 2. Checksum: 56596AF2F33F33E3	FASTA	276	31,360
	10 20 30 40 50 60 MSVKKKDLIT LQDPEAKYPL PLIEKEQISH NTRRFRFGLP SPDHVLGLPV GNYVHLLAQI 70 80 90 100 110 120 NNELVIRAYT PVSSDDDQGF VDLIIKIYFK NVHPKYPEGG KMTQYLENMK IGDTILFRGP 130 140 150 160 170 180 TGRLFYNEPG TLLIKANKTS EPEKKLVHHL GMIAGGTGIT PMLQLIRHIT KDTSDETRMS 190 200 210 220 230 240 LLFANQTEED ILLRKELEEV ATTHHKQFNL WYTLDRPPSD WKYSSGFVSA DMIKEHLPPP 250 260 270 GEDTLILVCG PPPLIQAAAH PSLEQLSYTK DMIFIY
	Isoform 2. Checksum: 1C4641E3F9297E31	FASTA	292	33,152
	10 20 30 40 50 60 MSVKKKDLIT LQDPEAKYPL PLIEKEQISH NTRRFRFGLP SPDHVLGLPV GNYVHLLAQI 70 80 90 100 110 120 NNELVIRAYT PVSSDDDQGF VDLIIKIYFK NVHPKYPEGG KMTQYLENMK IGDTILFRGP 130 140 150 160 170 180 TGRLFYNEPG CQTRAAEVKN IFIFLGTLLI KANKTSEPEK KLVHHLGMIA GGTGITPMLQ 190 200 210 220 230 240 LIRHITKDTS DETRMSLLFA NQTEEDILLR KELEEVATTH HKQFNLWYTL DRPPSDWKYS 250 260 270 280 290 SGFVSADMIK EHLPPPGEDT LILVCGPPPL IQAAAHPSLE QLSYTKDMIF IY

References

[1]	"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] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Kidney.
[2]	"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] (ISOFORM 1).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK085272 mRNA. Translation: BAC39408.1. AK147952 mRNA. Translation: BAE28247.1. BC107238 mRNA. Translation: AAI07239.1. BC107239 mRNA. Translation: AAI07240.1.
IPI	IPI00310925. IPI00845753.
RefSeq	NP_796190.1.
UniGene	Mm.132828
3D structure databases
SMR	Q3KNK3. Positions 8-276.
ModBase	Search...
Proteomic databases
PRIDE	Q3KNK3.
Genome annotation databases
Ensembl	ENSMUST00000052438; ENSMUSP00000050061; ENSMUSG00000048065; Mus musculus. [Genome view]
GeneID	320635.
KEGG	mmu:320635.
Organism-specific databases
CTD	320635.
MGI	MGI:2444415. Cyb5r2.
Phylogenomic databases
eggNOG	roNOG10122.
HOGENOM	HBG591994.
HOVERGEN	Q3KNK3.
InParanoid	Q3KNK3.
OMA	DDDQGFV.
PhylomeDB	Q3KNK3.
Enzyme and pathway databases
BRENDA	1.6.2.2. 244.
Gene expression databases
ArrayExpress	Q3KNK3.
Bgee	Q3KNK3.
CleanEx	MM_CYB5R2.
Genevestigator	Q3KNK3.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	397113.
SOURCE	Search...

Entry information

Entry name

NB5R2_MOUSE

Accession

Primary (citable) accession number: Q3KNK3
Secondary accession number(s): Q3UGG1, Q8BUG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	May 15, 2007
Last modified:	January 19, 2010
This is version 36 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)