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Protein

NADH-cytochrome b5 reductase 2

Gene

Cyb5r2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. Responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1) (By similarity).By similarity

Catalytic activityi

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

Cofactori

FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 13731FADBy similarityAdd
BLAST
Nucleotide bindingi146 – 18136FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

ReactomeiR-RNO-1237044. Erythrocytes take up carbon dioxide and release oxygen.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-cytochrome b5 reductase 2 (EC:1.6.2.2)
Short name:
b5R.2
Gene namesi
Name:Cyb5r2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1308421. Cyb5r2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 276276NADH-cytochrome b5 reductase 2PRO_0000287550Add
BLAST

Proteomic databases

PaxDbiQ6AY12.

PTM databases

PhosphoSiteiQ6AY12.

Expressioni

Gene expression databases

ExpressionAtlasiQ6AY12. baseline and differential.
GenevisibleiQ6AY12. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026744.

Structurei

3D structure databases

ProteinModelPortaliQ6AY12.
SMRiQ6AY12. Positions 8-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 127113FAD-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.
InParanoidiQ6AY12.
KOiK00326.
OMAiHYPEGGK.
OrthoDBiEOG7CZK69.
PhylomeDBiQ6AY12.

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.

Q6AY12-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVKKKDLIT LQDPEAKYPL PLIEKEQINH NTRRFRFGLP SPDHVLGLPV
60 70 80 90 100
GNYVHLLAQI NNELVIRAYT PVSSDDDQGF VDLIIKIYFK NVHPKYPEGG
110 120 130 140 150
KMTQYLENMK IGDTILFRGP TGRLFYNEPG TLLIKTDKTS EPEKKLVHHL
160 170 180 190 200
GMIAGGTGIT PMLQLIRHIT KDTSDGTRMS LLFANQTEED ILLRKELEEV
210 220 230 240 250
ATTHQNQFSL WYTLDRPPSG WEYSSGFITA DMIKEHLPPP GEATLILVCG
260 270
PPPLIQEAAH PSLEQLGYTK DMIFTY
Length:276
Mass (Da):31,239
Last modified:September 13, 2004 - v1
Checksum:i2B44235766324E96
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079235 mRNA. Translation: AAH79235.1.
RefSeqiNP_001014266.1. NM_001014244.1.
UniGeneiRn.16198.

Genome annotation databases

EnsembliENSRNOT00000026744; ENSRNOP00000026744; ENSRNOG00000019751.
GeneIDi365345.
KEGGirno:365345.
UCSCiRGD:1308421. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079235 mRNA. Translation: AAH79235.1.
RefSeqiNP_001014266.1. NM_001014244.1.
UniGeneiRn.16198.

3D structure databases

ProteinModelPortaliQ6AY12.
SMRiQ6AY12. Positions 8-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026744.

PTM databases

PhosphoSiteiQ6AY12.

Proteomic databases

PaxDbiQ6AY12.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026744; ENSRNOP00000026744; ENSRNOG00000019751.
GeneIDi365345.
KEGGirno:365345.
UCSCiRGD:1308421. rat.

Organism-specific databases

CTDi51700.
RGDi1308421. Cyb5r2.

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiQ6AY12.
KOiK00326.
OMAiHYPEGGK.
OrthoDBiEOG7CZK69.
PhylomeDBiQ6AY12.

Enzyme and pathway databases

ReactomeiR-RNO-1237044. Erythrocytes take up carbon dioxide and release oxygen.

Miscellaneous databases

PROiQ6AY12.

Gene expression databases

ExpressionAtlasiQ6AY12. baseline and differential.
GenevisibleiQ6AY12. 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

  1. "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].
    Tissue: Testis.

Entry informationi

Entry nameiNB5R2_RAT
AccessioniPrimary (citable) accession number: Q6AY12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: September 13, 2004
Last modified: July 6, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.