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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

Miscellaneous

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

Catalytic activityi

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

Cofactori

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi158 – 193FADBy similarityAdd BLAST36

GO - Molecular functioni

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

GO - Biological processi

  • cellular response to oxidative stress Source: SGD
  • ergosterol biosynthetic process Source: SGD

Keywordsi

Molecular functionOxidoreductase
LigandFAD, 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei12 – 32HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23 – 24AA → QQ: Prevents insertion into the outer membrane and increases the efficiency of import into the intermembrane space. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000194041 – 302NADH-cytochrome b5 reductase p34 formAdd BLAST302
PropeptideiPRO_00000194051 – 41Removed in p32 form2 PublicationsAdd BLAST41
ChainiPRO_000001940642 – 302NADH-cytochrome b5 reductase p32 formAdd BLAST261

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei278PhosphoserineCombined sources1

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)DescriptionActionsGraphical viewLength
Sitei41 – 42Cleavage; by IMP12

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP36060.
PRIDEiP36060.

2D gel databases

UCD-2DPAGEiP36060.

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. 130 interactors.
DIPiDIP-5475N.
IntActiP36060. 17 interactors.
MINTiMINT-505396.
STRINGi4932.YKL150W.

Structurei

3D structure databases

ProteinModelPortaliP36060.
SMRiP36060.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 155FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST105

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00880000138068.
HOGENOMiHOG000175005.
InParanoidiP36060.
KOiK00326.
OMAiNGPMSTH.
OrthoDBiEOG092C43G8.

Family and domain databases

InterProiView protein in InterPro
IPR017927. 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.
PfamiView protein in Pfam
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PRINTSiPR00406. CYTB5RDTASE.
PR00371. FPNCR.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiView protein in PROSITE
PS51384. FAD_FR. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti2Missing AA sequence (PubMed:16689936).Curated1
Sequence conflicti101N → L AA sequence (PubMed:8001120).Curated1

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.

Similar proteinsi

Entry informationi

Entry nameiMCR1_YEAST
AccessioniPrimary (citable) accession number: P36060
Secondary accession number(s): A2TBM9, D6VX47
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 22, 2017
This is version 169 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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