Reviewed, UniProtKB/Swiss-Prot Q0X0E5 (NB5R3_CANFA)

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:	C5BR, DIA1

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

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	Endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side By similarity. Mitochondrion outer membrane; Lipid-anchor; Cytoplasmic side 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	Endoplasmic reticulum Membrane Mitochondrion Mitochondrion outer membrane
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Acetylation Lipoprotein Myristate Phosphoprotein
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 membrane Inferred from electronic annotation. Source: UniProtKB-SubCell 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 301	300	NADH-cytochrome b5 reductase 3 membrane-bound form		PRO_0000289590
	Chain	27 – 301	275	NADH-cytochrome b5 reductase 3 soluble form		PRO_0000289591
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 By similarity
	Modified residue	43	1	Phosphotyrosine By similarity
	Modified residue	120	1	N6-acetyllysine By similarity
	Modified residue	130	1	Phosphotyrosine By similarity
	Lipidation	2	1	N-myristoyl glycine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0X0E5-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 76FB38B457AFF841	FASTA	301	34,139
	10 20 30 40 50 60 MGAQLSTLGH VVLSPVWFLY NLLMKLFQRS TPAITLESPD IKYPLRLIDK EVINHDTRRF 70 80 90 100 110 120 RFALPSPQHI LGLPVGQHIY LSARIDGNLV IRPYTPVSSD DDKGFVDLVI KVYFKDTHPK 130 140 150 160 170 180 FPAGGKMSQY LESMKIGDTI EFRGPNGLLV YQGKGKFAIR PDKKSNPIIK TVKSVGMIAG 190 200 210 220 230 240 GTGITPMLQV IRAIIKDPHD PTVCHLLFAN QTEKDILLRP ELEELRNEHS ARFKLWYTVD 250 260 270 280 290 300 KAPEAWDYSQ GFVNEEMIRD HLPPPEEEPL ILMCGPPPMI QYACLPNLDR VGHPKERCFA F

References

[1]	"Cloning of canine NADH cytochrome b5 reductase mRNA." Ano H., Ebisu S., Kondoh S., Hagio M., Makimura S. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Expression and characterization of a functional canine variant of cytochrome b5 reductase." Roma G.W., Crowley L.J., Barber M.J. Arch. Biochem. Biophys. 452:69-82(2006) [PubMed: 16814740] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Trachea.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB185964 mRNA. Translation: BAF02366.1. DQ141222 mRNA. Translation: ABA12483.1.
RefSeq	NP_001041549.1.
UniGene	Cfa.15074
3D structure databases
SMR	Q0X0E5. Positions 31-301.
ModBase	Search...
Genome annotation databases
Ensembl	ENSCAFG00000000953. Canis familiaris. [Contig view]
GeneID	474479.
KEGG	cfa:474479.
Phylogenomic databases
HOVERGEN	Q0X0E5.
Enzyme and pathway databases
BRENDA	1.6.2.2. 463.
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_CANFA

Accession

Primary (citable) accession number: Q0X0E5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)