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Protein

NADH-cytochrome b5 reductase 3

Gene

Cyb5r3

Organism
Rattus norvegicus (Rat)
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

FAD1 Publication

Regions

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

GO - Molecular functioni

  • ADP binding Source: RGD
  • AMP binding Source: RGD
  • cytochrome-b5 reductase activity, acting on NAD(P)H Source: RGD
  • FAD binding Source: GO_Central
  • flavin adenine dinucleotide binding Source: RGD
  • NAD binding Source: RGD

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

BRENDAi1.6.2.2. 5301.
ReactomeiR-RNO-196836. Vitamin C (ascorbate) metabolism.
SABIO-RKP20070.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi2502. Cyb5r3.

Subcellular locationi

Isoform 3 :
  • Cytoplasm

  • Note: Produces the soluble form found in erythrocytes.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 301300NADH-cytochrome b5 reductase 3 membrane-bound formPRO_0000019401Add
BLAST
Chaini27 – 301275NADH-cytochrome b5 reductase 3 soluble formPRO_0000019403Add
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

Post-translational modificationi

Only the isoform 1 is myristoyled.

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP20070.
PRIDEiP20070.

PTM databases

iPTMnetiP20070.
PhosphoSiteiP20070.
SwissPalmiP20070.

Expressioni

Tissue specificityi

Isoform 1 and isoform 3 are ubiquitously expressed. Isoform 2 is expressed only in erythroid tissues, reticulocytes and liver.1 Publication

Gene expression databases

GenevisibleiP20070. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP20070. 2 interactions.
MINTiMINT-4575419.
STRINGi10116.ENSRNOP00000012878.

Structurei

Secondary structure

1
301
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 5210Combined sources
Beta strandi54 – 6310Combined sources
Beta strandi78 – 858Combined sources
Beta strandi88 – 947Combined sources
Beta strandi104 – 1118Combined sources
Beta strandi115 – 1184Combined sources
Helixi126 – 1327Combined sources
Beta strandi139 – 1468Combined sources
Beta strandi148 – 1536Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi168 – 1714Combined sources
Beta strandi173 – 1808Combined sources
Helixi181 – 1833Combined sources
Helixi184 – 19613Combined sources
Beta strandi203 – 21210Combined sources
Helixi213 – 2153Combined sources
Helixi219 – 22810Combined sources
Turni230 – 2323Combined sources
Beta strandi233 – 2419Combined sources
Beta strandi247 – 2526Combined sources
Helixi255 – 2617Combined sources
Beta strandi269 – 2757Combined sources
Helixi277 – 2826Combined sources
Helixi285 – 2917Combined sources
Helixi295 – 2973Combined sources
Beta strandi298 – 3003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7PX-ray2.00A34-301[»]
1IB0X-ray2.30A34-301[»]
1QX4X-ray1.80A/B34-301[»]
ProteinModelPortaliP20070.
SMRiP20070. Positions 34-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20070.

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.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiP20070.
KOiK00326.
OMAiPVWFLYN.
OrthoDBiEOG7CZK69.
PhylomeDBiP20070.
TreeFamiTF314333.

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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative promoter usage and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P20070-1) [UniParc]FASTAAdd to basket

Also known as: L-form reticulocyte reductase

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.

« Hide

        10         20         30         40         50
MGAQLSTLSR VVLSPVWFVY SLFMKLFQRS SPAITLENPD IKYPLRLIDK
60 70 80 90 100
EIISHDTRRF RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD
110 120 130 140 150
DDKGFVDLVV KVYFKDTHPK FPAGGKMSQY LENMNIGDTI EFRGPNGLLV
160 170 180 190 200
YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG GTGITPMLQV IRAVLKDPND
210 220 230 240 250
HTVCYLLFAN QSEKDILLRP ELEELRNEHS SRFKLWYTVD KAPDAWDYSQ
260 270 280 290 300
GFVNEEMIRD HLPPPGEETL ILMCGPPPMI QFACLPNLER VGHPKERCFT

F
Note: Produced by alternative promoter usage.
Length:301
Mass (Da):34,175
Last modified:January 23, 2007 - v2
Checksum:i45431A644413905F
GO
Isoform 2 (identifier: P20070-2) [UniParc]FASTAAdd to basket

Also known as: R-form reticulocyte reductase

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MGAQLST → MLGPLLWTASLPV

Note: Produced by alternative promoter usage.
Show »
Length:307
Mass (Da):34,866
Checksum:iBEF7A5F4F12AC7C2
GO
Isoform 3 (identifier: P20070-3) [UniParc]FASTAAdd to basket

Also known as: Soluble form

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

Note: Produced by alternative initiation.
Show »
Length:278
Mass (Da):31,592
Checksum:i4FA80DCDADD24A1B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051F → L in AAA41008 (PubMed:3174630).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323Missing in isoform 3. 1 PublicationVSP_009660Add
BLAST
Alternative sequencei1 – 77MGAQLST → MLGPLLWTASLPV in isoform 2. 1 PublicationVSP_009661

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00636 mRNA. Translation: BAA00530.1.
J03867 mRNA. Translation: AAA41008.1.
BC062066 mRNA. Translation: AAH62066.1.
X65191 mRNA. Translation: CAA46308.1.
X65191 mRNA. Translation: CAA46309.1.
X65190 Genomic DNA. Translation: CAA46307.1.
X77117 Genomic DNA. No translation available.
PIRiA40495. RDRTB5.
S23641.
RefSeqiNP_620232.1. NM_138877.1. [P20070-1]
XP_006242127.1. XM_006242065.2. [P20070-2]
UniGeneiRn.35994.

Genome annotation databases

EnsembliENSRNOT00000064700; ENSRNOP00000061381; ENSRNOG00000009592. [P20070-1]
GeneIDi25035.
KEGGirno:25035.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00636 mRNA. Translation: BAA00530.1.
J03867 mRNA. Translation: AAA41008.1.
BC062066 mRNA. Translation: AAH62066.1.
X65191 mRNA. Translation: CAA46308.1.
X65191 mRNA. Translation: CAA46309.1.
X65190 Genomic DNA. Translation: CAA46307.1.
X77117 Genomic DNA. No translation available.
PIRiA40495. RDRTB5.
S23641.
RefSeqiNP_620232.1. NM_138877.1. [P20070-1]
XP_006242127.1. XM_006242065.2. [P20070-2]
UniGeneiRn.35994.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I7PX-ray2.00A34-301[»]
1IB0X-ray2.30A34-301[»]
1QX4X-ray1.80A/B34-301[»]
ProteinModelPortaliP20070.
SMRiP20070. Positions 34-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP20070. 2 interactions.
MINTiMINT-4575419.
STRINGi10116.ENSRNOP00000012878.

PTM databases

iPTMnetiP20070.
PhosphoSiteiP20070.
SwissPalmiP20070.

Proteomic databases

PaxDbiP20070.
PRIDEiP20070.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000064700; ENSRNOP00000061381; ENSRNOG00000009592. [P20070-1]
GeneIDi25035.
KEGGirno:25035.

Organism-specific databases

CTDi1727.
RGDi2502. Cyb5r3.

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiP20070.
KOiK00326.
OMAiPVWFLYN.
OrthoDBiEOG7CZK69.
PhylomeDBiP20070.
TreeFamiTF314333.

Enzyme and pathway databases

BRENDAi1.6.2.2. 5301.
ReactomeiR-RNO-196836. Vitamin C (ascorbate) metabolism.
SABIO-RKP20070.

Miscellaneous databases

EvolutionaryTraceiP20070.
PROiP20070.

Gene expression databases

GenevisibleiP20070. RN.

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. "Molecular cloning of a cDNA encoding rat NADH-cytochrome b5 reductase and the corresponding gene."
    Zenno S., Hattori M., Misumi Y., Yubisui T., Sakaki Y.
    J. Biochem. 107:810-816(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Sprague-Dawley.
    Tissue: Liver.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Prostate.
  4. "A single mRNA, transcribed from an alternative, erythroid-specific, promoter, codes for two non-myristylated forms of NADH-cytochrome b5 reductase."
    Pietrini G., Aggujaro D., Carrera P., Malyszko J., Vitale A., Borgese N.
    J. Cell Biol. 117:975-986(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-37 (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
    Strain: Sprague-Dawley and Wistar.
    Tissue: Liver and Reticulocyte.
  5. "The NH2-terminal structures of human and rat liver microsomal NADH-cytochrome b5 reductases."
    Murakami K., Yubisui T., Takeshita M., Miyata T.
    J. Biochem. 105:312-317(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-25, MYRISTOYLATION AT GLY-2.
    Tissue: Liver.
  6. "Heterogeneity of the rat NADH-cytochrome-b5-reductase transcripts resulting from multiple alternative first exons."
    Mota Vieira L., Kaplan J.-C., Kahn A., Leroux A.
    Eur. J. Biochem. 220:729-737(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  7. "A role for N-myristoylation in protein targeting: NADH-cytochrome b5 reductase requires myristic acid for association with outer mitochondrial but not ER membranes."
    Borgese N., Aggujaro D., Carrera P., Pietrini G., Bassetti M.
    J. Cell Biol. 135:1501-1513(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE OF MYRISTOYLATION.
  8. "High-level expression in Escherichia coli of the soluble, catalytic domain of rat hepatic cytochrome b5 reductase."
    Barber M.J., Quinn G.B.
    Protein Expr. Purif. 8:41-47(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FAD-BINDING.
  9. "The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent."
    Bewley M.C., Marohnic C.C., Barber M.J.
    Biochemistry 40:13574-13582(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-301.

Entry informationi

Entry nameiNB5R3_RAT
AccessioniPrimary (citable) accession number: P20070
Secondary accession number(s): Q64569, Q64720
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.