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Protein

NADH-cytochrome b5 reductase 3

Gene

CYB5R3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.

Catalytic activityi

NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.

Cofactori

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi132 – 14716FADBy similarityAdd
BLAST
Nucleotide bindingi171 – 20636FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

SABIO-RKP07514.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-cytochrome b5 reductase 3 (EC:1.6.2.2)
Short name:
B5R
Short name:
Cytochrome b5 reductase
Alternative name(s):
Diaphorase-1
Cleaved into the following 2 chains:
Gene namesi
Name:CYB5R3
Synonyms:DIA1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

NADH-cytochrome b5 reductase 3 membrane-bound form :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421K → E: Decrease of activity. 1 Publication
Mutagenesisi126 – 1261K → E: Decrease of activity. 1 Publication
Mutagenesisi164 – 1641K → E: Decrease of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 301300NADH-cytochrome b5 reductase 3 membrane-bound formPRO_0000019389Add
BLAST
Chaini27 – 301275NADH-cytochrome b5 reductase 3 soluble formPRO_0000019391Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei42 – 421N6-acetyllysineBy similarity
Modified residuei43 – 431PhosphotyrosineBy similarity
Modified residuei50 – 501N6-acetyllysineBy similarity
Modified residuei120 – 1201N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP07514.
PRIDEiP07514.

Interactioni

Subunit structurei

Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000040254.

Structurei

3D structure databases

ProteinModelPortaliP07514.
SMRiP07514. Positions 32-301.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 152113FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiP07514.
KOiK00326.

Family and domain databases

InterProiIPR017927. 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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07514-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQLSTLGH VVLSPVWFLY SLIMKLFQRS TPAITLENPD IKYPLRLIDK
60 70 80 90 100
EVISHDTRRF RFALPSPEHI LGLPVGQHIY LSARIDGNLV IRPYTPVSSD
110 120 130 140 150
DDKGFVDLVI KVYFKDTHPK FPAGGKMSQY LESMKIGDTI EFRGPNGLLV
160 170 180 190 200
YQGKGKFAIR PDKKSDPVIK TVKSVGMIAG GTGITPMLQV IRAIMKDPDD
210 220 230 240 250
HTVCHLLFAN QTEKDILLRP ELEELRNEHS ARFKLWYTVD KAPEAWDYSQ
260 270 280 290 300
GFVNEEMIRD HLPPPEEEPL VLMCGPPPMI QYACLPNLDR VGHPKERCFA

F
Length:301
Mass (Da):34,122
Last modified:May 3, 2011 - v3
Checksum:i435229B893B2A3DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161V → L AA sequence (PubMed:3900065).Curated
Sequence conflicti16 – 161V → L AA sequence (PubMed:6436247).Curated
Sequence conflicti135 – 1351K → G AA sequence (PubMed:3900065).Curated
Sequence conflicti163 – 1631K → S AA sequence (PubMed:3900065).Curated
Sequence conflicti227 – 2271N → D AA sequence (PubMed:3900065).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC146232 mRNA. Translation: AAI46233.1.
M83104 mRNA. Translation: AAA30483.1.
PIRiA42328. RDBOB5.
RefSeqiNP_001096720.1. NM_001103250.1.
UniGeneiBt.4873.

Genome annotation databases

GeneIDi515773.
KEGGibta:515773.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC146232 mRNA. Translation: AAI46233.1.
M83104 mRNA. Translation: AAA30483.1.
PIRiA42328. RDBOB5.
RefSeqiNP_001096720.1. NM_001103250.1.
UniGeneiBt.4873.

3D structure databases

ProteinModelPortaliP07514.
SMRiP07514. Positions 32-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000040254.

Proteomic databases

PaxDbiP07514.
PRIDEiP07514.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi515773.
KEGGibta:515773.

Organism-specific databases

CTDi1727.

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiP07514.
KOiK00326.

Enzyme and pathway databases

SABIO-RKP07514.

Family and domain databases

InterProiIPR017927. 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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Ascending colon.
  2. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-301.
    Strain: Black Angus.
    Tissue: Liver.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-301, MUTAGENESIS.
  4. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-53.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-37, MYRISTOYLATION AT GLY-2.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-44.

Entry informationi

Entry nameiNB5R3_BOVIN
AccessioniPrimary (citable) accession number: P07514
Secondary accession number(s): A6H7G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: May 3, 2011
Last modified: June 8, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.