Reviewed, UniProtKB/Swiss-Prot P36060 (MCR1_YEAST)

Names and origin

Protein names

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:
    1- Recommended name:
            NADH-cytochrome b5 reductase p34 form
    2- Recommended name:
            NADH-cytochrome b5 reductase p32 form

Gene names

Name:	MCR1
Ordered Locus Names:	YKL150W
ORF Names:	YKL605

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.8
Catalytic activity	NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5.
Cofactor	FAD.
Subcellular location	NADH-cytochrome b5 reductase p32 form: Mitochondrion intermembrane space. Ref.5 Ref.9 Ref.12 NADH-cytochrome b5 reductase p34 form: Mitochondrion outer membrane; Single-pass membrane protein. Ref.5 Ref.9 Ref.12
Induction	By osmotic stress. Ref.11
Post-translational modification	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.
Miscellaneous	Present with 1920 molecules/cell in log phase SD medium. Ref.10
Sequence similarities	Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain.
Mass spectrometry	Molecular mass is 34137 Da from positions 1 - 302. Ref.5

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ergosterol biosynthetic process Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Ref.8 Inferred from mutant phenotype. Source: SGD
Cellular component	integral to mitochondrial outer membrane Ref.5 Inferred from direct assay. Source: SGD mitochondrial intermembrane space Ref.1 Inferred from direct assay. Source: SGD
Molecular function	cytochrome-b5 reductase activity Ref.1 Inferred from direct assay. Source: SGD electron carrier activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALO1	P54783	1	EBI-10565,EBI-2519
PRP40	P33203	1	EBI-10565,EBI-701
RSP5	P39940	1	EBI-10565,EBI-16219

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	NADH-cytochrome b5 reductase p34 form		PRO_0000019404
	Propeptide	1 – 41	41	Removed in p32 form		PRO_0000019405
	Chain	42 – 302	261	NADH-cytochrome b5 reductase p32 form		PRO_0000019406
Regions
	Transmembrane	12 – 32	21	Potential
	Domain	51 – 155	105	FAD-binding FR-type
	Nucleotide binding	158 – 193	36	FAD By similarity
Sites
	Site	41 – 42	2	Cleavage; by IMP1
Amino acid modifications
	Modified residue	278	1	Phosphoserine Ref.13
Experimental info
	Mutagenesis	23 – 24	2	AA → QQ: Prevents insertion into the outer membrane and increases the efficiency of import into the intermembrane space. Ref.7
	Sequence conflict	2	1	Missing AA sequence Ref.5
	Sequence conflict	101	1	N → L AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P36060-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: D3CB56356E8C572F	FASTA	302	34,138
	10 20 30 40 50 60 MFSRLSRSHS KALPIALGTV AIAAATAFYF ANRNQHSFVF NESNKVFKGD DKWIDLPISK 70 80 90 100 110 120 IEEESHDTRR FTFKLPTEDS EMGLVLASAL FAKFVTPKGS NVVRPYTPVS DLSQKGHFQL 130 140 150 160 170 180 VVKHYEGGKM TSHLFGLKPN DTVSFKGPIM KWKWQPNQFK SITLLGAGTG INPLYQLAHH 190 200 210 220 230 240 IVENPNDKTK VNLLYGNKTP QDILLRKELD ALKEKYPDKF NVTYFVDDKQ DDQDFDGEIS 250 260 270 280 290 300 FISKDFIQEH VPGPKESTHL FVCGPPPFMN AYSGEKKSPK DQGELIGILN NLGYSKDQVF KF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8001120] [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: 8091859] [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: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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: 17244705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-41. Strain: ATCC 201390 / BY4743.
[5]	"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: 16689936] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20, MASS SPECTROMETRY, SUBCELLULAR LOCATION. Strain: ATCC 24657 / D273-10B.
[6]	"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: 9866716] [Abstract] Cited for: PROTEIN SEQUENCE OF 42-58.
[7]	"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: 9199337] [Abstract] Cited for: MUTAGENESIS OF 23-ALA-ALA-24.
[8]	"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: 11420140] [Abstract] Cited for: FUNCTION.
[9]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"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: 15590813] [Abstract] Cited for: INDUCTION.
[12]	"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: 16407407] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[13]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X81474 Genomic DNA. Translation: CAA57227.1. Z26877 Genomic DNA. Translation: CAA81503.1. Z28150 Genomic DNA. Translation: CAA81991.1. EF123132 mRNA. Translation: ABM97476.1.
PIR	S37800.
RefSeq	NP_012772.1.
3D structure databases
HSSP	HSSP built from PDB template 1I7P based on UniProtKB P20070.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5475N.
IntAct	P36060. 19 interactions.
STRING	P36060.
Proteomic databases
PeptideAtlas	P36060.
PRIDE	P36060.
Genome annotation databases
Ensembl	YKL150W; YKL150W; YKL150W; Saccharomyces cerevisiae. [Genome view]
GeneID	853707.
GenomeReviews	Gene locus YKL150W in contig Y13137_GR.
KEGG	sce:YKL150W.
NMPDR	fig|4932.3.peg.3751.
Organism-specific databases
CYGD	YKL150w.
SGD	S000001633. MCR1.
Phylogenomic databases
HOGENOM	P36060.
OMA	PVASCIT.
Enzyme and pathway databases
BRENDA	1.6.2.2. 250.
Gene expression databases
ArrayExpress	P36060.
Genevestigator	P36060.
GermOnline	YKL150W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view]
Pfam	PF00970. FAD_binding_6. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	974707.

Entry information

Entry name

MCR1_YEAST

Accession

Primary (citable) accession number: P36060
Secondary accession number(s): A2TBM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 3, 2009
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)