Reviewed, UniProtKB/Swiss-Prot P07514 (NB5R3_BOVIN)

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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	300 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.
Catalytic activity	NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.
Cofactor	FAD.
Subunit structure	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. NADH-cytochrome b5 reductase 3 soluble form: Cytoplasm.
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
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	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytochrome-b5 reductase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 300	300	NADH-cytochrome b5 reductase 3 membrane-bound form Ref.1		PRO_0000019389
	Chain	26 – 300	275	NADH-cytochrome b5 reductase 3 soluble form		PRO_0000019391
Regions
	Domain	39 – 151	113	FAD-binding FR-type
	Nucleotide binding	131 – 146	16	FAD By similarity
	Nucleotide binding	170 – 205	36	FAD By similarity
Amino acid modifications
	Modified residue	41	1	N6-acetyllysine By similarity
	Modified residue	42	1	Phosphotyrosine By similarity
	Modified residue	119	1	N6-acetyllysine By similarity
	Modified residue	129	1	Phosphotyrosine By similarity
	Lipidation	1	1	N-myristoyl glycine Ref.4
Experimental info
	Mutagenesis	41	1	K → E: Decrease of activity.
	Mutagenesis	125	1	K → E: Decrease of activity.
	Mutagenesis	163	1	K → E: Decrease of activity.
	Sequence conflict	15	1	V → L AA sequence Ref.1
	Sequence conflict	15	1	V → L AA sequence Ref.4
	Sequence conflict	134	1	K → G AA sequence Ref.1
	Sequence conflict	162	1	K → S AA sequence Ref.1
	Sequence conflict	226	1	N → D AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P07514-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 11B29F57F9309F3E	FASTA	300	33,990
	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

References

[1]	"Complete amino acid sequence of steer liver microsomal NADH-cytochrome b5 reductase." Ozols J., Korza G., Heinemann F.S., Hediger M.A., Strittmatter P. J. Biol. Chem. 260:11953-11961(1985) [PubMed: 3900065] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: Black Angus. Tissue: Liver.
[2]	"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." Strittmatter P., Kittler J.M., Coghill J.E., Ozols J. J. Biol. Chem. 267:2519-2523(1992) [PubMed: 1370824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS.
[3]	"Structural comparison of bovine erythrocyte, brain, and liver NADH-cytochrome b5 reductase by HPLC mapping." Tamura M., Yubisui T., Takeshita M., Kawabata S., Miyata T., Iwanaga S. J. Biochem. 101:1147-1159(1987) [PubMed: 3654589] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-52.
[4]	"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." Ozols J., Carr S.A., Strittmatter P. J. Biol. Chem. 259:13349-13354(1984) [PubMed: 6436247] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-36, MYRISTOYLATION AT GLY-1.
[5]	"Isolation and partial characterization of the NH2-terminal membrane-binding domain of NADH-cytochrome b5 reductase." Kensil C.R., Hediger M.A., Ozols J., Strittmatter P. J. Biol. Chem. 258:14656-14663(1983) [PubMed: 6643503] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-43.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M83104 mRNA. Translation: AAA30483.1.
IPI	IPI00868665.
PIR	RDBOB5. A42328.
RefSeq	NP_001096720.1.
UniGene	Bt.4873
3D structure databases
HSSP	HSSP built from PDB template 1I7P based on UniProtKB P20070.
SMR	P07514. Positions 30-300.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000016516. Bos taurus. [Contig view]
GeneID	515773.
KEGG	bta:515773.
Phylogenomic databases
HOVERGEN	P07514.
Enzyme and pathway databases
BRENDA	1.6.2.2. 251.
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...

Entry information

Entry name

NB5R3_BOVIN

Accession

Primary (citable) accession number: P07514

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)