Q12452 (ERG27_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-keto-steroid reductase
EC=1.1.1.270

Gene names

Name:	ERG27
Ordered Locus Names:	YLR100W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Responsible for the reduction of the keto group on the C-3 of sterols. Also facilitates the association of ERG7 with lipid particles preventing its digestion in the endoplasmic reticulum and the lipid particles. Ref.3 Ref.5
Catalytic activity	4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NADP+ = 4-alpha-methyl-5-alpha-cholest-7-en-3-one + NADPH.
Pathway	Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 5/6.
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 ERG25 and ERG28. Also interacts with ERG7, but only in lipid particles. Ref.4 Ref.5 Ref.6
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Lipid droplet Ref.4 Ref.5 Ref.7.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family. ERG27 subfamily.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis
Cellular component	Endoplasmic reticulum Lipid droplet Membrane
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ergosterol biosynthetic process Inferred from mutant phenotype Ref.3. Source: SGD
Cellular component	endoplasmic reticulum membrane Inferred from direct assay Ref.4. Source: SGD lipid particle Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from direct assay. Source: SGD
Molecular function	3-keto sterol reductase activity Inferred from mutant phenotype Ref.3. Source: SGD nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERG25	P53045	4	EBI-38132,EBI-6506
ERG28	P40030	6	EBI-38132,EBI-22518
ERG7	P38604	4	EBI-38132,EBI-6572

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 347	347	3-keto-steroid reductase		PRO_0000054595
Sites
	Active site	202	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	345	1	Phosphothreonine Ref.8 Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Q12452 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D9A0589C049D8C49	FASTA	347	39,725
	10 20 30 40 50 60 MNRKVAIVTG TNSNLGLNIV FRLIETEDTN VRLTIVVTSR TLPRVQEVIN QIKDFYNKSG 70 80 90 100 110 120 RVEDLEIDFD YLLVDFTNMV SVLNAYYDIN KKYRAINYLF VNAAQGIFDG IDWIGAVKEV 130 140 150 160 170 180 FTNPLEAVTN PTYKIQLVGV KSKDDMGLIF QANVFGPYYF ISKILPQLTR GKAYIVWISS 190 200 210 220 230 240 IMSDPKYLSL NDIELLKTNA SYEGSKRLVD LLHLATYKDL KKLGINQYVV QPGIFTSHSF 250 260 270 280 290 300 SEYLNFFTYF GMLCLFYLAR LLGSPWHNID GYKAANAPVY VTRLANPNFE KQDVKYGSAT 310 320 330 340 SRDGMPYIKT QEIDPTGMSD VFAYIQKKKL EWDEKLKDQI VETRTPI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Characterization of the Saccharomyces cerevisiae ERG27 gene encoding the 3-keto reductase involved in C-4 sterol demethylation." Gachotte D., Sen S.E., Eckstein J., Barbuch R., Krieger M., Ray B.D., Bard M. Proc. Natl. Acad. Sci. U.S.A. 96:12655-12660(1999) [PubMed: 10535978] [Abstract] Cited for: CHARACTERIZATION, FUNCTION.
[4]	"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 ERG25 AND ERG28, SUBCELLULAR LOCATION.
[5]	"In yeast sterol biosynthesis the 3-keto reductase protein (Erg27p) is required for oxidosqualene cyclase (Erg7p) activity." Mo C., Milla P., Athenstaedt K., Ott R., Balliano G., Daum G., Bard M. Biochim. Biophys. Acta 1633:68-74(2003) [PubMed: 12842197] [Abstract] Cited for: FUNCTION, INTERACTION WITH ERG7, SUBCELLULAR LOCATION.
[6]	"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.
[7]	"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.
[8]	"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 THR-345, MASS SPECTROMETRY. Strain: ADR376.
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-345, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U53876 Genomic DNA. Translation: AAB67544.1. Z73272 Genomic DNA. Translation: CAA97664.1. BK006945 Genomic DNA. Translation: DAA09417.1.
PIR	S64936.
RefSeq	NP_013201.1. NM_001181987.1.
3D structure databases
ProteinModelPortal	Q12452.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1237N.
IntAct	Q12452. 26 interactions.
MINT	MINT-387123.
STRING	Q12452.
Proteomic databases
PeptideAtlas	Q12452.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR100W; YLR100W; YLR100W.
GeneID	850790.
KEGG	sce:YLR100W.
NMPDR	fig|4932.3.peg.4193.
Organism-specific databases
CYGD	YLR100w.
SGD	S000004090. ERG27.
Phylogenomic databases
eggNOG	fuNOG05767.
GeneTree	EFGT00050000005048.
HOGENOM	HBG398311.
OMA	FLFYLAR.
OrthoDB	EOG4FBN2N.
Enzyme and pathway databases
BioCyc	MetaCyc:YLR100W-MONOMER.
Gene expression databases
ArrayExpress	Q12452.
Genevestigator	Q12452.
GermOnline	YLR100W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K09827.
ProtoNet	Search...
Other
NextBio	966996.

Entry information

Entry name

ERG27_YEAST

Accession

Primary (citable) accession number: Q12452
Secondary accession number(s): D6VYA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program