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YEAST:MCR1
Contents
| Species (Taxon ID) | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292) | |
| Gene Name(s) | MCR1 | |
| Protein Name(s) | NADH-cytochrome b5 reductase 2
Mitochondrial cytochrome b reductase p34/p32 NADH-cytochrome b5 reductase p34 form NADH-cytochrome b5 reductase p32 form | |
| External Links | ||
| UniProt | P36060 | |
| EMBL | X81474 Z26877 Z28150 EF123132 BK006944 | |
| PIR | S37800 | |
| RefSeq | NP_012772.1 | |
| ProteinModelPortal | P36060 | |
| SMR | P36060 | |
| BioGrid | 33987 | |
| DIP | DIP-5475N | |
| IntAct | P36060 | |
| MINT | MINT-505396 | |
| iPTMnet | P36060 | |
| UCD-2DPAGE | P36060 | |
| MaxQB | P36060 | |
| PeptideAtlas | P36060 | |
| EnsemblFungi | YKL150W | |
| GeneID | 853707 | |
| KEGG | sce:YKL150W | |
| EuPathDB | FungiDB:YKL150W | |
| SGD | S000001633 | |
| GeneTree | ENSGT00830000128428 | |
| HOGENOM | HOG000175005 | |
| InParanoid | P36060 | |
| KO | K00326 | |
| OMA | NIKLFVC | |
| OrthoDB | EOG7N63XM | |
| BioCyc | YEAST:YKL150W-MONOMER | |
| Reactome | [www.reactome.org/content/detail/R-SCE-1237044 R-SCE-1237044] | |
| PRO | PR:P36060 | |
| Proteomes | UP000002311 | |
| GO | GO:0031307 GO:0005758 GO:0005741 GO:0004128 GO:0034599 GO:0006696 | |
| InterPro | IPR017927 IPR001709 IPR001834 IPR008333 IPR001433 IPR017938 | |
| Pfam | PF00970 PF00175 | |
| PRINTS | PR00406 PR00371 | |
| SUPFAM | SSF63380 | |
| PROSITE | PS51384 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0003954 |
NADH dehydrogenase activity |
ECO:0000314 |
F |
The author cloned and overexpressed Mcr1 and monitored the reduction of Dph3 by Dph3's absorbance at 488nm. The author found that Mcr1 reduced Dph3 after the addition of NADH to the reaction tube (Supplementary figure 5A). |
complete | |||||
|
part_of |
GO:0005741 |
mitochondrial outer membrane |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0034599 |
cellular response to oxidative stress |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0031307 |
integral component of mitochondrial outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006696 |
ergosterol biosynthetic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005758 |
mitochondrial intermembrane space |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005741 |
mitochondrial outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004128 |
cytochrome-b5 reductase activity, acting on NAD(P)H |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006696 |
ergosterol biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN001064729 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004128 |
cytochrome-b5 reductase activity, acting on NAD(P)H |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000452207 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR001433 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR001433 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004128 |
cytochrome-b5 reductase activity, acting on NAD(P)H |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005739 |
mitochondrion |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005741 |
mitochondrial outer membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005758 |
mitochondrial intermembrane space |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Lin, Z et al. (2016) Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification. Nat. Chem. Biol. PubMed GONUTS page
- ↑ Zahedi, RP et al. (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol. Biol. Cell 17 1436-50 PubMed GONUTS page
- ↑ Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
- ↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
- ↑ Lee, JS et al. (2001) Mitochondrial NADH-cytochrome b(5) reductase plays a crucial role in the reduction of D-erythroascorbyl free radical in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1527 31-8 PubMed GONUTS page
- ↑ Burri, L et al. (2006) Integral membrane proteins in the mitochondrial outer membrane of Saccharomyces cerevisiae. FEBS J. 273 1507-15 PubMed GONUTS page
- ↑ Lamb, DC et al. (1999) Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction. FEBS Lett. 462 283-8 PubMed GONUTS page
- ↑ 8.0 8.1 8.2 Hahne, K et al. (1994) Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments. Cell 79 829-39 PubMed GONUTS page
- ↑ 9.0 9.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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