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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi132 – 147FADAdd BLAST16
Nucleotide bindingi171 – 206FADAdd BLAST36

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.
R-RNO-6798695. Neutrophil degranulation.
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000194012 – 301NADH-cytochrome b5 reductase 3 membrane-bound formAdd BLAST300
ChainiPRO_000001940327 – 301NADH-cytochrome b5 reductase 3 soluble formAdd BLAST275

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Modified residuei42N6-acetyllysineBy similarity1
Modified residuei43PhosphotyrosineBy similarity1
Modified residuei50N6-acetyllysineBy similarity1
Modified residuei120N6-acetyllysineBy similarity1

Post-translational modificationi

Only the isoform 1 is myristoyled.

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiP20070.
PRIDEiP20070.

PTM databases

iPTMnetiP20070.
PhosphoSitePlusiP20070.
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

BgeeiENSRNOG00000009592.
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 interactors.
MINTiMINT-4575419.
STRINGi10116.ENSRNOP00000012878.

Structurei

Secondary structure

1301
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 52Combined sources10
Beta strandi54 – 63Combined sources10
Beta strandi78 – 85Combined sources8
Beta strandi88 – 94Combined sources7
Beta strandi104 – 111Combined sources8
Beta strandi115 – 118Combined sources4
Helixi126 – 132Combined sources7
Beta strandi139 – 146Combined sources8
Beta strandi148 – 153Combined sources6
Beta strandi156 – 159Combined sources4
Beta strandi168 – 171Combined sources4
Beta strandi173 – 180Combined sources8
Helixi181 – 183Combined sources3
Helixi184 – 196Combined sources13
Beta strandi203 – 212Combined sources10
Helixi213 – 215Combined sources3
Helixi219 – 228Combined sources10
Turni230 – 232Combined sources3
Beta strandi233 – 241Combined sources9
Beta strandi247 – 252Combined sources6
Helixi255 – 261Combined sources7
Beta strandi269 – 275Combined sources7
Helixi277 – 282Combined sources6
Helixi285 – 291Combined sources7
Helixi295 – 297Combined sources3
Beta strandi298 – 300Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP20070.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 152FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiP20070.
KOiK00326.
OMAiPVWFLYN.
OrthoDBiEOG091G0EIS.
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)DescriptionActionsGraphical viewLength
Sequence conflicti105F → L in AAA41008 (PubMed:3174630).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0096601 – 23Missing in isoform 3. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_0096611 – 7MGAQLST → MLGPLLWTASLPV in isoform 2. 1 Publication7

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_006242065.3. [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_006242065.3. [P20070-2]
UniGeneiRn.35994.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

iPTMnetiP20070.
PhosphoSitePlusiP20070.
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.
OrthoDBiEOG091G0EIS.
PhylomeDBiP20070.
TreeFamiTF314333.

Enzyme and pathway databases

BRENDAi1.6.2.2. 5301.
ReactomeiR-RNO-196836. Vitamin C (ascorbate) metabolism.
R-RNO-6798695. Neutrophil degranulation.
SABIO-RKP20070.

Miscellaneous databases

EvolutionaryTraceiP20070.
PROiP20070.

Gene expression databases

BgeeiENSRNOG00000009592.
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...

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: November 30, 2016
This is version 163 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.