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Protein

NADH-cytochrome b5 reductase 2

Gene

MCR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The outer membrane form may mediate the reduction of outer membrane cytochrome b5, and the soluble inter-membrane space form may transfer electrons from external NADH to cytochrome c, thereby mediating an antimycin-insensitive, energy-coupled oxidation of external NADH by yeast mitochondria. Involved in the reduction of D-erythroascorbyl free radicals.1 Publication

Catalytic activityi

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

Cofactori

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 19336FADBy similarityAdd
BLAST

GO - Molecular functioni

  • cytochrome-b5 reductase activity, acting on NAD(P)H Source: SGD
  • FAD binding Source: GO_Central

GO - Biological processi

  • cellular response to oxidative stress Source: SGD
  • ergosterol biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciYEAST:YKL150W-MONOMER.
ReactomeiR-SCE-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)
Alternative name(s):
Mitochondrial cytochrome b reductase
p34/p32
Cleaved into the following 2 chains:
Gene namesi
Name:MCR1
Ordered Locus Names:YKL150W
ORF Names:YKL605
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL150W.
SGDiS000001633. MCR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of mitochondrial outer membrane Source: SGD
  • mitochondrial intermembrane space Source: SGD
  • mitochondrial outer membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 242AA → QQ: Prevents insertion into the outer membrane and increases the efficiency of import into the intermembrane space. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302NADH-cytochrome b5 reductase p34 formPRO_0000019404Add
BLAST
Propeptidei1 – 4141Removed in p32 form2 PublicationsPRO_0000019405Add
BLAST
Chaini42 – 302261NADH-cytochrome b5 reductase p32 formPRO_0000019406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei278 – 2781PhosphoserineCombined sources

Post-translational modificationi

There are two isoforms of NADH-cytochrome b5 reductase, a 34 kDa form (p34) and a 32 kDa form (p32). The p34 form becomes firmly anchored to the outer mitochondrial membrane after an incomplete translocation arrest. The p32 form is formed after translocation of the p34 precursor to the inner mitochondrial membrane, where it is processed by mitochondrial inner membrane peptidase (IMP) complex and released to the intermembrane space.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei41 – 422Cleavage; by IMP1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36060.

2D gel databases

UCD-2DPAGEP36060.

PTM databases

iPTMnetiP36060.

Expressioni

Inductioni

By osmotic stress.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-10565,EBI-16219

Protein-protein interaction databases

BioGridi33987. 40 interactions.
DIPiDIP-5475N.
IntActiP36060. 16 interactions.
MINTiMINT-505396.

Structurei

3D structure databases

ProteinModelPortaliP36060.
SMRiP36060. Positions 65-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 155105FAD-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

GeneTreeiENSGT00830000128428.
HOGENOMiHOG000175005.
InParanoidiP36060.
KOiK00326.
OMAiNIKLFVC.
OrthoDBiEOG7N63XM.

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.

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

P36060-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSRLSRSHS KALPIALGTV AIAAATAFYF ANRNQHSFVF NESNKVFKGD
60 70 80 90 100
DKWIDLPISK IEEESHDTRR FTFKLPTEDS EMGLVLASAL FAKFVTPKGS
110 120 130 140 150
NVVRPYTPVS DLSQKGHFQL VVKHYEGGKM TSHLFGLKPN DTVSFKGPIM
160 170 180 190 200
KWKWQPNQFK SITLLGAGTG INPLYQLAHH IVENPNDKTK VNLLYGNKTP
210 220 230 240 250
QDILLRKELD ALKEKYPDKF NVTYFVDDKQ DDQDFDGEIS FISKDFIQEH
260 270 280 290 300
VPGPKESTHL FVCGPPPFMN AYSGEKKSPK DQGELIGILN NLGYSKDQVF

KF
Length:302
Mass (Da):34,138
Last modified:June 1, 1994 - v1
Checksum:iD3CB56356E8C572F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21Missing AA sequence (PubMed:16689936).Curated
Sequence conflicti101 – 1011N → L AA sequence (PubMed:8001120).Curated

Mass spectrometryi

Molecular mass is 34137 Da from positions 1 - 302. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81474 Genomic DNA. Translation: CAA57227.1.
Z26877 Genomic DNA. Translation: CAA81503.1.
Z28150 Genomic DNA. Translation: CAA81991.1.
EF123132 mRNA. Translation: ABM97476.1.
BK006944 Genomic DNA. Translation: DAA09013.1.
PIRiS37800.
RefSeqiNP_012772.1. NM_001179716.1.

Genome annotation databases

EnsemblFungiiYKL150W; YKL150W; YKL150W.
GeneIDi853707.
KEGGisce:YKL150W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81474 Genomic DNA. Translation: CAA57227.1.
Z26877 Genomic DNA. Translation: CAA81503.1.
Z28150 Genomic DNA. Translation: CAA81991.1.
EF123132 mRNA. Translation: ABM97476.1.
BK006944 Genomic DNA. Translation: DAA09013.1.
PIRiS37800.
RefSeqiNP_012772.1. NM_001179716.1.

3D structure databases

ProteinModelPortaliP36060.
SMRiP36060. Positions 65-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33987. 40 interactions.
DIPiDIP-5475N.
IntActiP36060. 16 interactions.
MINTiMINT-505396.

PTM databases

iPTMnetiP36060.

2D gel databases

UCD-2DPAGEP36060.

Proteomic databases

MaxQBiP36060.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL150W; YKL150W; YKL150W.
GeneIDi853707.
KEGGisce:YKL150W.

Organism-specific databases

EuPathDBiFungiDB:YKL150W.
SGDiS000001633. MCR1.

Phylogenomic databases

GeneTreeiENSGT00830000128428.
HOGENOMiHOG000175005.
InParanoidiP36060.
KOiK00326.
OMAiNIKLFVC.
OrthoDBiEOG7N63XM.

Enzyme and pathway databases

BioCyciYEAST:YKL150W-MONOMER.
ReactomeiR-SCE-1237044. Erythrocytes take up carbon dioxide and release oxygen.

Miscellaneous databases

PROiP36060.

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. "Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments."
    Hahne K., Haucke V., Ramage L., Schatz G.
    Cell 79:829-839(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 42-52; 70-89 AND 99-113.
  2. "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci of chromosome XI of Saccharomyces cerevisiae."
    Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.
    Yeast 10:S35-S40(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "High-density yeast-tiling array reveals previously undiscovered introns and extensive regulation of meiotic splicing."
    Juneau K., Palm C., Miranda M., Davis R.W.
    Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-41.
    Strain: ATCC 201390 / BY4743.
  6. "Integral membrane proteins in the mitochondrial outer membrane of Saccharomyces cerevisiae."
    Burri L., Vascotto K., Gentle I.E., Chan N.C., Beilharz T., Stapleton D.I., Ramage L., Lithgow T.
    FEBS J. 273:1507-1515(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    Strain: ATCC 24657 / D273-10B.
  7. "The yeast mitochondrial intermembrane space: purification and analysis of two distinct fractions."
    Martin H., Eckerskorn C., Gaertner F., Rassow J., Lottspeich F., Pfanner N.
    Anal. Biochem. 265:123-128(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 42-58.
  8. "Analysis of the sorting signals directing NADH-cytochrome b5 reductase to two locations within yeast mitochondria."
    Haucke V., Ocana C.S., Hoenlinger A., Tokatlidis K., Pfanner N., Schatz G.
    Mol. Cell. Biol. 17:4024-4032(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 23-ALA-ALA-24.
  9. "Mitochondrial NADH-cytochrome b(5) reductase plays a crucial role in the reduction of D-erythroascorbyl free radical in Saccharomyces cerevisiae."
    Lee J.-S., Huh W.-K., Lee B.-H., Baek Y.-U., Hwang C.-S., Kim S.-T., Kim Y.-R., Kang S.-O.
    Biochim. Biophys. Acta 1527:31-38(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "Anaerobicity prepares Saccharomyces cerevisiae cells for faster adaptation to osmotic shock."
    Krantz M., Nordlander B., Valadi H., Johansson M., Gustafsson L., Hohmann S.
    Eukaryot. Cell 3:1381-1390(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  13. "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins."
    Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.
    Mol. Biol. Cell 17:1436-1450(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.

Entry informationi

Entry nameiMCR1_YEAST
AccessioniPrimary (citable) accession number: P36060
Secondary accession number(s): A2TBM9, D6VX47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 6, 2016
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1920 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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.