Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADH-cytochrome b5 reductase 3

Gene

Cyb5r3

Organism
Mus musculus (Mouse)
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.By similarity

Catalytic activityi

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

Cofactori

FADBy similarity

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

BioCyciMetaCyc:MONOMER-14527.
ReactomeiR-MMU-196836. Vitamin C (ascorbate) metabolism.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:94893. Cyb5r3.

Subcellular locationi

Isoform 1 :
  • Endoplasmic reticulum membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
  • Mitochondrion outer membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
Isoform 2 :
  • Cytoplasm

  • Note: Produces the soluble form found in erythrocytes.By similarity

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 methionineiRemovedBy similarity
Chaini2 – 301300NADH-cytochrome b5 reductase 3 membrane-bound formPRO_0000019398Add
BLAST
Chaini27 – 301275NADH-cytochrome b5 reductase 3 soluble formPRO_0000019400Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ9DCN2.
MaxQBiQ9DCN2.
PaxDbiQ9DCN2.
PeptideAtlasiQ9DCN2.
PRIDEiQ9DCN2.
TopDownProteomicsiQ9DCN2-1. [Q9DCN2-1]
Q9DCN2-2. [Q9DCN2-2]

PTM databases

iPTMnetiQ9DCN2.
PhosphoSiteiQ9DCN2.
SwissPalmiQ9DCN2.

Expressioni

Gene expression databases

BgeeiQ9DCN2.
CleanExiMM_CYB5R3.
ExpressionAtlasiQ9DCN2. baseline and differential.
GenevisibleiQ9DCN2. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-57517N.
IntActiQ9DCN2. 7 interactions.
MINTiMINT-1867235.
STRINGi10090.ENSMUSP00000018186.

Structurei

3D structure databases

ProteinModelPortaliQ9DCN2.
SMRiQ9DCN2. Positions 34-301.
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.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiQ9DCN2.
KOiK00326.
OMAiPVWFLYN.
OrthoDBiEOG7CZK69.
PhylomeDBiQ9DCN2.
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.

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

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

Isoform 1 (identifier: Q9DCN2-1) [UniParc]FASTAAdd to basket

Also known as: M

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
MGAQLSTLSH VVLSPVWFIY SLFMKLFQRS TPAITLENPD IKYPLRLIDK
60 70 80 90 100
EVISPDTRRF RFALPSPQHI LGLPIGQHIY LSTRIDGNLV IRPYTPVSSD
110 120 130 140 150
DDKGFVDLVV KVYFKDTHPK FPAGGKMSQY LENMKIGDTI EFRGPNGLLV
160 170 180 190 200
YQGKGKFAIR ADKKSNPVVR TVKSVGMIAG GTGITPMLQV IRAVLKDPND
210 220 230 240 250
HTVCYLLFAN QSEKDILLRP ELEELRNEHS ARFKLWYTVD KAPDAWDYSQ
260 270 280 290 300
GFVNEEMIRD HLPTPGEEPL ILMCGPPPMI QFACLPNLER VGHPKERCFT

F
Length:301
Mass (Da):34,128
Last modified:January 23, 2007 - v3
Checksum:i984D5B73430F725D
GO
Isoform 2 (identifier: Q9DCN2-2) [UniParc]FASTAAdd to basket

Also known as: S

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

Show »
Length:278
Mass (Da):31,550
Checksum:iE18DE5668ECD3939
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323Missing in isoform 2. CuratedVSP_012952Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332059 mRNA. Translation: AAK56088.1.
AF332060 mRNA. Translation: AAK56089.1.
AK002640 mRNA. Translation: BAB22252.1.
BC004760 mRNA. Translation: AAH04760.1.
BC032013 mRNA. Translation: AAH32013.1.
BC043074 mRNA. Translation: AAH43074.1.
CCDSiCCDS27698.1. [Q9DCN2-1]
RefSeqiNP_084063.1. NM_029787.2. [Q9DCN2-1]
XP_006520346.1. XM_006520283.2. [Q9DCN2-2]
UniGeneiMm.22560.

Genome annotation databases

EnsembliENSMUST00000018186; ENSMUSP00000018186; ENSMUSG00000018042. [Q9DCN2-1]
GeneIDi109754.
KEGGimmu:109754.
UCSCiuc007xac.2. mouse. [Q9DCN2-1]

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF332059 mRNA. Translation: AAK56088.1.
AF332060 mRNA. Translation: AAK56089.1.
AK002640 mRNA. Translation: BAB22252.1.
BC004760 mRNA. Translation: AAH04760.1.
BC032013 mRNA. Translation: AAH32013.1.
BC043074 mRNA. Translation: AAH43074.1.
CCDSiCCDS27698.1. [Q9DCN2-1]
RefSeqiNP_084063.1. NM_029787.2. [Q9DCN2-1]
XP_006520346.1. XM_006520283.2. [Q9DCN2-2]
UniGeneiMm.22560.

3D structure databases

ProteinModelPortaliQ9DCN2.
SMRiQ9DCN2. Positions 34-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-57517N.
IntActiQ9DCN2. 7 interactions.
MINTiMINT-1867235.
STRINGi10090.ENSMUSP00000018186.

PTM databases

iPTMnetiQ9DCN2.
PhosphoSiteiQ9DCN2.
SwissPalmiQ9DCN2.

Proteomic databases

EPDiQ9DCN2.
MaxQBiQ9DCN2.
PaxDbiQ9DCN2.
PeptideAtlasiQ9DCN2.
PRIDEiQ9DCN2.
TopDownProteomicsiQ9DCN2-1. [Q9DCN2-1]
Q9DCN2-2. [Q9DCN2-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018186; ENSMUSP00000018186; ENSMUSG00000018042. [Q9DCN2-1]
GeneIDi109754.
KEGGimmu:109754.
UCSCiuc007xac.2. mouse. [Q9DCN2-1]

Organism-specific databases

CTDi1727.
MGIiMGI:94893. Cyb5r3.

Phylogenomic databases

eggNOGiKOG0534. Eukaryota.
COG0543. LUCA.
GeneTreeiENSGT00390000008881.
HOGENOMiHOG000175005.
HOVERGENiHBG052580.
InParanoidiQ9DCN2.
KOiK00326.
OMAiPVWFLYN.
OrthoDBiEOG7CZK69.
PhylomeDBiQ9DCN2.
TreeFamiTF314333.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14527.
ReactomeiR-MMU-196836. Vitamin C (ascorbate) metabolism.

Miscellaneous databases

ChiTaRSiCyb5r3. mouse.
PROiQ9DCN2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCN2.
CleanExiMM_CYB5R3.
ExpressionAtlasiQ9DCN2. baseline and differential.
GenevisibleiQ9DCN2. 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

« Hide 'large scale' publications
  1. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ILS and ISS.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Kidney.
  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].
    Strain: 129, C57BL/6J and FVB/N.
    Tissue: Brain, Kidney and Mammary tumor.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 127-135, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
    Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
    Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42 AND LYS-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  8. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNB5R3_MOUSE
AccessioniPrimary (citable) accession number: Q9DCN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 131 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. 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.