Reviewed, UniProtKB/Swiss-Prot P53045 (ERG25_YEAST)

Names and origin

Protein names

Recommended name:
    C-4 methylsterol oxidase
    EC=1.14.13.72
Alternative name(s):
    Methylsterol monooxygenase

Gene names

Name:	ERG25
Synonyms:	FET6
Ordered Locus Names:	YGR060W

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	309 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol.
Catalytic activity	4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O(2) = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)(+) + H(2)O. 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O(2) = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)(+) + 2 H(2)O. 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)H + O(2) = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)(+) + H(2)O.
Cofactor	Iron.
Pathway	Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 3/6.
Subunit structure	Heterotetramer of ERG25, ERG26, ERG27 and ERG28. ERG28 acts as a scaffold to tether ERG27 and other 4,4-demethylation-related enzymes, forming a demethylation enzyme complex, in the endoplasmic reticulum. Interacts with ERG27 and ERG28.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane proteinProbable.
Domain	The histidine box domains may contain the active site and/or be involved in metal ion binding.
Miscellaneous	Present with 77100 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the sterol desaturase family.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	Iron NAD
Molecular function	Oxidoreductase
PTM	Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ergosterol biosynthetic process Ref.2 Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Ref.2 Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Ref.2 Inferred from direct assay. Source: SGD
Molecular function	C-4 methylsterol oxidase activity Ref.2 Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.5 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERG27	Q12452	1	EBI-6506,EBI-38132
ERG28	P40030	1	EBI-6506,EBI-22518

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 309	309	C-4 methylsterol oxidase		PRO_0000117039
Regions
	Transmembrane	56 – 76	21	Potential
	Motif	160 – 164	5	Histidine box-1
	Motif	173 – 177	5	Histidine box-2
	Motif	257 – 263	7	Histidine box-3
Amino acid modifications
	Cross-link	96		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Sequences

	Sequence		Length	Mass (Da)
	P53045-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E0422C416DD17794	FASTA	309	36,479
	10 20 30 40 50 60 MSAVFNNATL SGLVQASTYS QTLQNVAHYQ PQLNFMEKYW AAWYSYMNND VLATGLMFFL 70 80 90 100 110 120 LHEFMYFFRC LPWFIIDQIP YFRRWKLQPT KIPSAKEQLY CLKSVLLSHF LVEAIPIWTF 130 140 150 160 170 180 HPMCEKLGIT VEVPFPSLKT MALEIGLFFV LEDTWHYWAH RLFHYGVFYK YIHKQHHRYA 190 200 210 220 230 240 APFGLSAEYA HPAETLSLGF GTVGMPILYV MYTGKLHLFT LCVWITLRLF QAVDSHSGYD 250 260 270 280 290 300 FPWSLNKIMP FWAGAEHHDL HHHYFIGNYA SSFRWWDYCL DTESGPEAKA SREERMKKRA ENNAQKKTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of ERG25, the Saccharomyces cerevisiae gene encoding C-4 sterol methyl oxidase." Bard M., Bruner D.A., Pierson C.A., Lees N.D., Biermann B., Frye L., Koegel C., Barbuch R. Proc. Natl. Acad. Sci. U.S.A. 93:186-190(1996) [PubMed: 8552601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue." Li L., Kaplan J. J. Biol. Chem. 271:16927-16933(1996) [PubMed: 8663358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, SUBCELLULAR LOCATION.
[3]	"Quantitative trait loci mapped to single-nucleotide resolution in yeast." Deutschbauer A.M., Davis R.W. Nat. Genet. 37:1333-1340(2005) [PubMed: 16273108] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SK1.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Protein-protein interactions among C-4 demethylation enzymes involved in yeast sterol biosynthesis." Mo C., Valachovic M., Randall S.K., Nickels J.T., Bard M. Proc. Natl. Acad. Sci. U.S.A. 99:9739-9744(2002) [PubMed: 12119386] [Abstract] Cited for: SUBUNIT, INTERACTION WITH ERG27 AND ERG28, SUBCELLULAR LOCATION.
[6]	"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].
[7]	"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery." Hitchcock A.L., Auld K., Gygi S.P., Silver P.A. Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed: 14557538] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-96, MASS SPECTROMETRY.
[8]	"Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex." Mo C., Bard M. J. Lipid Res. 46:1991-1998(2005) [PubMed: 15995173] [Abstract] Cited for: INTERACTION WITH ERG28.
[9]	"The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy." Natter K., Leitner P., Faschinger A., Wolinski H., McCraith S., Fields S., Kohlwein S.D. Mol. Cell. Proteomics 4:662-672(2005) [PubMed: 15716577] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U31885 Genomic DNA. Translation: AAC49139.1. DQ115391 Genomic DNA. Translation: AAZ22473.1. Z72845 Genomic DNA. Translation: CAA97062.1.
PIR	S64354.
RefSeq	NP_011574.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2799N.
IntAct	P53045.
Proteomic databases
PeptideAtlas	P53045.
Genome annotation databases
Ensembl	YGR060W. Saccharomyces cerevisiae. [Contig view]
GeneID	852951.
GenomeReviews	Gene locus YGR060W in contig Y13135_GR.
KEGG	sce:YGR060W.
NMPDR	fig|4932.3.peg.2690.
Organism-specific databases
CYGD	YGR060w.
SGD	S000003292. ERG25.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P53045.
Gene expression databases
GermOnline	YGR060W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006088. Sterol_desatur. [Graphical view]
Pfam	PF01598. Sterol_desat. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	P53045.
NextBio	972708.

Entry information

Entry name

ERG25_YEAST

Accession

Primary (citable) accession number: P53045
Secondary accession number(s): Q45U26

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)