Reviewed, UniProtKB/Swiss-Prot Q9DCN2 (NB5R3_MOUSE)

Names and origin

Protein names

Recommended name:
    NADH-cytochrome b5 reductase 3
      Short name=Cytochrome b5 reductase
      Short name=B5R
    EC=1.6.2.2
Alternative name(s):
    Diaphorase-1
Cleaved into the following 2 chains:
    1- Recommended name:
            NADH-cytochrome b5 reductase 3 membrane-bound form
    2- Recommended name:
            NADH-cytochrome b5 reductase 3 soluble form

Gene names

Name:	Cyb5r3
Synonyms:	Dia1

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

General annotation (Comments)

Function	Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction By similarity.
Catalytic activity	NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.
Cofactor	FAD By similarity.
Subunit structure	Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2 By similarity.
Subcellular location	Isoform 1: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side By similarity. Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side By similarity. Isoform 2: Cytoplasm › cytosol By similarity. Note: Produces the soluble form found in erythrocytes By similarity.
Sequence similarities	Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative promoter usage
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Acetylation Lipoprotein Myristate Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell internal side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9DCN2-1)

Also known as: M;

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: Q9DCN2-2)

Also known as: S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Note: Produces the soluble form found in erythrocytes (By similarity).

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 301	300	NADH-cytochrome b5 reductase 3 membrane-bound form		PRO_0000019398
	Chain	27 – 301	275	NADH-cytochrome b5 reductase 3 soluble form		PRO_0000019400
Regions
	Domain	40 – 152	113	FAD-binding FR-type
	Nucleotide binding	132 – 147	16	FAD By similarity
	Nucleotide binding	171 – 206	36	FAD By similarity
Amino acid modifications
	Modified residue	42	1	N6-acetyllysine Ref.5
	Modified residue	43	1	Phosphotyrosine By similarity
	Modified residue	120	1	N6-acetyllysine Ref.5
	Modified residue	130	1	Phosphotyrosine Ref.6
	Lipidation	2	1	N-myristoyl glycine By similarity
Natural variations
	Alternative sequence	1 – 23	23	Missing in isoform 2.		VSP_012952

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (M) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 984D5B73430F725D	FASTA	301	34,128
	10 20 30 40 50 60 MGAQLSTLSH VVLSPVWFIY SLFMKLFQRS TPAITLENPD IKYPLRLIDK EVISPDTRRF 70 80 90 100 110 120 RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD DDKGFVDLVV KVYFKDTHPK 130 140 150 160 170 180 FPAGGKMSQY LENMKIGDTI EFRGPNGLLV YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG 190 200 210 220 230 240 GTGITPMLQV IRAVLKDPND HTVCYLLFAN QSEKDILLRP ELEELRNEHS ARFKLWYTVD 250 260 270 280 290 300 KAPDAWDYSQ GFVNEEMIRD HLPTPGEEPL ILMCGPPPMI QFACLPNLER VGHPKERCFT F
	Isoform 2 (S). Checksum: E18DE5668ECD3939	FASTA	278	31,550
	10 20 30 40 50 60 MKLFQRSTPA ITLENPDIKY PLRLIDKEVI SPDTRRFRFA LPSPQHILGL PIGQHIYLST 70 80 90 100 110 120 RIDGNLVIRP YTPVSSDDDK GFVDLVVKVY FKDTHPKFPA GGKMSQYLEN MKIGDTIEFR 130 140 150 160 170 180 GPNGLLVYQG KGKFAIRADK KSNPVVRTVK SVGMIAGGTG ITPMLQVIRA VLKDPNDHTV 190 200 210 220 230 240 CYLLFANQSE KDILLRPELE ELRNEHSARF KLWYTVDKAP DAWDYSQGFV NEEMIRDHLP 250 260 270 TPGEEPLILM CGPPPMIQFA CLPNLERVGH PKERCFTF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed: 11471062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ILS and ISS.
[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: Kidney.
[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]. Strain: 129, C57BL/6 and FVB/N. Tissue: Brain, Kidney and Mammary tumor.
[4]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 127-135, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[5]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42 AND LYS-120, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-130, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF332059 mRNA. Translation: AAK56088.1. AF332060 mRNA. Translation: AAK56089.1. AK002640 mRNA. Translation: BAB22252.1. BC004760 mRNA. Translation: AAH04760.1. BC032013 mRNA. Translation: AAH32013.1. BC043074 mRNA. Translation: AAH43074.1.
IPI	IPI00121079. IPI00759904.
RefSeq	NP_084063.1.
UniGene	Mm.22560
3D structure databases
HSSP	HSSP built from PDB template 1I7P based on UniProtKB P20070.
SMR	Q9DCN2. Positions 33-300, 34-301.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9DCN2.
PTM databases
PhosphoSite	Q9DCN2.
Proteomic databases
PRIDE	Q9DCN2.
Genome annotation databases
Ensembl	ENSMUST00000018186; ENSMUSP00000018186; ENSMUSG00000018042; Mus musculus. [Genome view] ENSMUST00000057383; ENSMUSP00000055473; ENSMUSG00000018042; Mus musculus. [Genome view]
GeneID	109754.
KEGG	mmu:109754.
UCSC	uc007xac.1. mouse.
Organism-specific databases
CTD	109754.
MGI	MGI:94893. Cyb5r3.
Phylogenomic databases
HOVERGEN	Q9DCN2.
OMA	ARFKFAL.
Enzyme and pathway databases
BRENDA	1.6.2.2. 244.
Gene expression databases
ArrayExpress	Q9DCN2.
Bgee	Q9DCN2.
CleanEx	MM_CYB5R3.
Genevestigator	Q9DCN2.
GermOnline	ENSMUSG00000018042. Mus musculus.
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. IPR001433. OxRdtase_FAD/NAD_bd. [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	362693.
SOURCE	Search...

Entry information

Entry name

NB5R3_MOUSE

Accession

Primary (citable) accession number: Q9DCN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)