[1]	PROTEIN SEQUENCE. STRAIN=Black Angus; TISSUE=Liver; PubMed=3900065 [NCBI, ExPASy, EBI, Israel, Japan] Ozols J., Korza G., Heinemann F.S., Hediger M.A., Strittmatter P.; "Complete amino acid sequence of steer liver microsomal NADH-cytochrome b5 reductase."; J. Biol. Chem. 260:11953-11961(1985).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS. PubMed=1370824 [NCBI, ExPASy, EBI, Israel, Japan] Strittmatter P., Kittler J.M., Coghill J.E., Ozols J.; "Characterization of lysyl residues of NADH-cytochrome b5 reductase implicated in charge-pairing with active-site carboxyl residues of cytochrome b5 by site-directed mutagenesis of an expression vector for the flavoprotein."; J. Biol. Chem. 267:2519-2523(1992).
[3]	PROTEIN SEQUENCE OF 26-52. PubMed=3654589 [NCBI, ExPASy, EBI, Israel, Japan] Tamura M., Yubisui T., Takeshita M., Kawabata S., Miyata T., Iwanaga S.; "Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b5 reductase by HPLC mapping."; J. Biochem. 101:1147-1159(1987).
[4]	PROTEIN SEQUENCE OF 1-36, AND MYRISTOYLATION AT GLY-1. PubMed=6436247 [NCBI, ExPASy, EBI, Israel, Japan] Ozols J., Carr S.A., Strittmatter P.; "Identification of the NH2-terminal blocking group of NADH-cytochrome b5 reductase as myristic acid and the complete amino acid sequence of the membrane-binding domain."; J. Biol. Chem. 259:13349-13354(1984).
[5]	PROTEIN SEQUENCE OF 16-43. PubMed=6643503 [NCBI, ExPASy, EBI, Israel, Japan] Kensil C.R., Hediger M.A., Ozols J., Strittmatter P.; "Isolation and partial characterization of the NH2-terminal membrane-binding domain of NADH-cytochrome b5 reductase."; J. Biol. Chem. 258:14656-14663(1983).

Comments

FUNCTION: Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
CATALYTIC ACTIVITY: NADH + 2 ferricytochrome b5 = NAD⁺ + H⁺ + 2 ferrocytochrome b5.
COFACTOR: FAD.
SUBUNIT: Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity).
SUBCELLULAR LOCATION: NADH-cytochrome b5 reductase 3 membrane-bound form: Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side. Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side. Note=The enzyme exists in two forms, a membrane-bound form on the cytoplasmic side of the endoplasmic reticulum and also on the mitochondrial outer membrane and in soluble form in erythrocytes.
SUBCELLULAR LOCATION: NADH-cytochrome b5 reductase 3 soluble form: Cytoplasm.
SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M83104; AAA30483.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A42328; RDBOB5.

NP_001096720.1; -.

3D structure databases

HSSP

P20070; 1I7P. [HSSP ENTRY / PDB]

SMR

P07514; 30-300.

ModBase

P07514.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (inferred from electronic annotation from UniProtKB-KW).
GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004128;	Molecular function: cytochrome-b5 reductase activity (inferred from electronic annotation from EC).
GO:0006695;	Biological process: cholesterol biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001834; Cyt_B5_reductase.
IPR001709; FPN_cyt_redctse.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Pfam

PF00970; FAD_binding_6; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00406; CYTB5RDTASE.
PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSBTAG00000016516; Bos taurus. [Contig view]

GeneID

515773; -.

KEGG

bta:515773; -.

Phylogenomic databases

HOVERGEN

P07514; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Cholesterol biosynthesis; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; Lipid synthesis; Lipoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; Myristate; NAD; Oxidoreductase; Phosphoprotein; Steroid biosynthesis; Sterol biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 300`	`300`	`NADH-cytochrome b5 reductase 3 membrane-bound form.`	`PRO_0000019389`
`CHAIN`	`26 300`	`275`	`NADH-cytochrome b5 reductase 3 soluble form.`	`PRO_0000019391`
`DOMAIN`	`39 151`	`113`	`FAD-binding FR-type.`
`NP_BIND`	`131 146`	`16`	`FAD (By similarity).`
`NP_BIND`	`170 205`	`36`	`FAD (By similarity).`
`MOD_RES`	`41 41`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`119 119`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`129 129`		`Phosphotyrosine (By similarity).`
`LIPID`	`1 1`		`N-myristoyl glycine.`
`MUTAGEN`	`41 41`		`K->E: Decrease of activity.`
`MUTAGEN`	`125 125`		`K->E: Decrease of activity.`
`MUTAGEN`	`163 163`		`K->E: Decrease of activity.`
`CONFLICT`	`15 15`		`V -> L (in Ref. 1 and 4).`
`CONFLICT`	`134 134`		`K -> G (in Ref. 1; AA sequence).`
`CONFLICT`	`162 162`		`K -> S (in Ref. 1; AA sequence).`
`CONFLICT`	`226 226`		`N -> D (in Ref. 1; AA sequence).`

Sequence information

Length: 300 AA [This is the length of the unprocessed precursor]

Molecular weight: 33990 Da [This is the MW of the unprocessed precursor]

CRC64: 11B29F57F9309F3E [This is a checksum on the sequence]

        10         20         30         40         50         60 
GAQLSTLGHV VLSPVWFLYS LIMKLFQRST PAITLENPDI KYPLRLIDKE VISHDTRRFR 

        70         80         90        100        110        120 
FALPSPEHIL GLPVGQHIYL SARIDGNLVI RPYTPVSSDD DKGFVDLVIK VYFKDTHPKF 

       130        140        150        160        170        180 
PAGGKMSQYL ESMKIGDTIE FRGPNGLLVY QGKGKFAIRP DKKSDPVIKT VKSVGMIAGG 

       190        200        210        220        230        240 
TGITPMLQVI RAIMKDPDDH TVCHLLFANQ TEKDILLRPE LEELRNEHSA RFKLWYTVDK 

       250        260        270        280        290        300 
APEAWDYSQG FVNEEMIRDH LPPPEEEPLV LMCGPPPMIQ YACLPNLDRV GHPKERCFAF

P07514 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools