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Protein

NADH-cytochrome b5 reductase 1

Gene

Cyb5r1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.By similarity

Catalytic activityi

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

Cofactori

FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi136 – 16631FADBy similarityAdd
BLAST
Nucleotide bindingi175 – 21036FADBy 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-MMU-114608. Platelet degranulation.
R-MMU-1237044. Erythrocytes take up carbon dioxide and release oxygen.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-cytochrome b5 reductase 1 (EC:1.6.2.2)
Short name:
b5R.1
Alternative name(s):
NAD(P)H:quinone oxidoreductase type 3 polypeptide A2
Gene namesi
Name:Cyb5r1
Synonyms:Nqo3a2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1919267. Cyb5r1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305NADH-cytochrome b5 reductase 1PRO_0000287546Add
BLAST

Proteomic databases

EPDiQ9DB73.
MaxQBiQ9DB73.
PaxDbiQ9DB73.
PRIDEiQ9DB73.

PTM databases

iPTMnetiQ9DB73.
PhosphoSiteiQ9DB73.

Expressioni

Gene expression databases

BgeeiQ9DB73.
CleanExiMM_CYB5R1.
ExpressionAtlasiQ9DB73. baseline and differential.
GenevisibleiQ9DB73. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027726.

Structurei

3D structure databases

ProteinModelPortaliQ9DB73.
SMRiQ9DB73. Positions 36-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 156113FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiQ9DB73.
KOiK00326.
OMAiMGIQPST.
PhylomeDBiQ9DB73.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9DB73-1) [UniParc]FASTAAdd to basket

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
MGIQPSPVLL ASLGVGLLTL LGLALGTYLV RRSRRPQVTL QDPDEKYLLR
60 70 80 90 100
LLDKTTVSHN TRRFRFALPT AHHILGLPVG KHVYLSARID GSLVIRPYTP
110 120 130 140 150
VTSDEDQGYV DLVIKVYLKG VHPKFPEGGK MSQYLDSLKI GDMVEFRGPS
160 170 180 190 200
GLLSYAGKGN FNIQPNKKSP PELRVAKKLG MIAGGTGITP MLQLIRAILK
210 220 230 240 250
VPEDPTQCFL LFANQTERDI ILREDLEELQ AQYPNRFKLW FTLDSPPEDW
260 270 280 290 300
TYSKGFVTAD MIQEHLPAPA EDVLLLLCGP PPMVQLACHP NLDKLGYSQK

MRFTY
Length:305
Mass (Da):34,135
Last modified:June 1, 2001 - v1
Checksum:i847B9AAFD99ED035
GO
Isoform 2 (identifier: Q9DB73-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     159-228: GNFNIQPNKK...DIILREDLEE → ESACVHGCTW...DDPSTVPCLW
     229-305: Missing.

Note: No experimental confirmation available.
Show »
Length:228
Mass (Da):25,305
Checksum:i85FCC210489EDD32
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei159 – 22870GNFNI…EDLEE → ESACVHGCTWAKSPEATMLY GKADFTLWRLPEETYASPSF TKDFPLAKDQKRKLFSSSHG DDPSTVPCLW in isoform 2. 1 PublicationVSP_025557Add
BLAST
Alternative sequencei229 – 30577Missing in isoform 2. 1 PublicationVSP_025558Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005159 mRNA. Translation: BAB23850.1.
AK159663 mRNA. Translation: BAE35270.1.
AK167178 mRNA. Translation: BAE39313.1.
BC016266 mRNA. Translation: AAH16266.1.
BC024618 mRNA. Translation: AAH24618.1.
CCDSiCCDS15308.1. [Q9DB73-1]
RefSeqiNP_082333.1. NM_028057.2. [Q9DB73-1]
UniGeneiMm.280230.
Mm.490981.

Genome annotation databases

EnsembliENSMUST00000027726; ENSMUSP00000027726; ENSMUSG00000026456. [Q9DB73-1]
ENSMUST00000154237; ENSMUSP00000133385; ENSMUSG00000026456. [Q9DB73-2]
GeneIDi72017.
KEGGimmu:72017.
UCSCiuc007cru.1. mouse. [Q9DB73-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005159 mRNA. Translation: BAB23850.1.
AK159663 mRNA. Translation: BAE35270.1.
AK167178 mRNA. Translation: BAE39313.1.
BC016266 mRNA. Translation: AAH16266.1.
BC024618 mRNA. Translation: AAH24618.1.
CCDSiCCDS15308.1. [Q9DB73-1]
RefSeqiNP_082333.1. NM_028057.2. [Q9DB73-1]
UniGeneiMm.280230.
Mm.490981.

3D structure databases

ProteinModelPortaliQ9DB73.
SMRiQ9DB73. Positions 36-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027726.

PTM databases

iPTMnetiQ9DB73.
PhosphoSiteiQ9DB73.

Proteomic databases

EPDiQ9DB73.
MaxQBiQ9DB73.
PaxDbiQ9DB73.
PRIDEiQ9DB73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027726; ENSMUSP00000027726; ENSMUSG00000026456. [Q9DB73-1]
ENSMUST00000154237; ENSMUSP00000133385; ENSMUSG00000026456. [Q9DB73-2]
GeneIDi72017.
KEGGimmu:72017.
UCSCiuc007cru.1. mouse. [Q9DB73-1]

Organism-specific databases

CTDi51706.
MGIiMGI:1919267. Cyb5r1.

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiQ9DB73.
KOiK00326.
OMAiMGIQPST.
PhylomeDBiQ9DB73.
TreeFamiTF314333.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-1237044. Erythrocytes take up carbon dioxide and release oxygen.

Miscellaneous databases

ChiTaRSiCyb5r1. mouse.
PROiQ9DB73.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DB73.
CleanExiMM_CYB5R1.
ExpressionAtlasiQ9DB73. baseline and differential.
GenevisibleiQ9DB73. MM.

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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: FVB/N.
    Tissue: Kidney and Salivary gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiNB5R1_MOUSE
AccessioniPrimary (citable) accession number: Q9DB73
Secondary accession number(s): Q91W81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 108 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.