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P53045 (MSMO_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylsterol monooxygenase

EC=1.14.13.72
Alternative name(s):
C-4 methylsterol oxidase
Gene names
Name:ERG25
Synonyms:FET6
Ordered Locus Names:YGR060W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.2

Catalytic activity

4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)+ + H2O.

4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O2 = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)+ + 2 H2O.

3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carbaldehyde + NAD(P)H + O2 = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha-carboxylate + NAD(P)+ + H2O.

Cofactor

Iron. Ref.2

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. Ref.7 Ref.10

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein Probable Ref.2 Ref.7 Ref.11.

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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Methylsterol monooxygenase
PRO_0000117039

Regions

Transmembrane56 – 7621Helical; Potential
Motif160 – 1645Histidine box-1
Motif173 – 1775Histidine box-2
Motif257 – 2637Histidine box-3

Amino acid modifications

Cross-link96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Experimental info

Sequence conflict3021N → K in AAS56153. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P53045 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E0422C416DD17794

FASTA30936,479
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"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] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH ERG27 AND ERG28, SUBCELLULAR LOCATION.
[8]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"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] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-96.
[10]"Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex."
Mo C., Bard M.
J. Lipid Res. 46:1991-1998(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERG28.
[11]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31885 Genomic DNA. Translation: AAC49139.1.
DQ115391 Genomic DNA. Translation: AAZ22473.1.
Z72845 Genomic DNA. Translation: CAA97062.1.
AY557827 Genomic DNA. Translation: AAS56153.1.
BK006941 Genomic DNA. Translation: DAA08156.1.
PIRS64354.
RefSeqNP_011574.3. NM_001181189.3.

3D structure databases

ProteinModelPortalP53045.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33305. 235 interactions.
DIPDIP-2799N.
IntActP53045. 60 interactions.
MINTMINT-536282.

Proteomic databases

PaxDbP53045.
PeptideAtlasP53045.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR060W; YGR060W; YGR060W.
GeneID852951.
KEGGsce:YGR060W.

Organism-specific databases

CYGDYGR060w.
SGDS000003292. ERG25.

Phylogenomic databases

eggNOGCOG3000.
GeneTreeENSGT00530000063017.
HOGENOMHOG000162289.
KOK07750.
OMADSQFIAY.
OrthoDBEOG7NW6M8.

Enzyme and pathway databases

BioCycMetaCyc:YGR060W-MONOMER.
YEAST:YGR060W-MONOMER.
UniPathwayUPA00770; UER00756.

Gene expression databases

GenevestigatorP53045.

Family and domain databases

InterProIPR006694. Fatty_acid_hydroxylase.
[Graphical view]
PfamPF04116. FA_hydroxylase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972708.
PROP53045.

Entry information

Entry nameMSMO_YEAST
AccessionPrimary (citable) accession number: P53045
Secondary accession number(s): D6VUJ5, E9P8T3, Q45U26
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways