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Reviewed, UniProtKB/Swiss-Prot P25340 (ERG4_YEAST)

Last modified January 19, 2010. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Delta(24(24(1)))-sterol reductase
    EC=1.3.1.71
Alternative name(s):
    Sterol Delta(24(28))-reductase
    C-24(28) sterol reductase
Gene names
Name: ERG4
Ordered Locus Names: YGL012W
ORF Names: YGL022
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Ergosterol + NADP+ = ergosta-5,7,22,24(241)-tetraen-3-beta-ol + NADPH.

Pathway

Steroid metabolism; ergosterol biosynthesis; ergosterol from zymosterol: step 5/5.

Subcellular location

Membrane; Multi-pass membrane protein.

Miscellaneous

Present with 1640 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the ERG4/ERG24 family.

Caution

Was originally (Ref.1) thought to be a transport protein.

Ontologies

Keywords
   Biological processLipid synthesis
Steroid biosynthesis
Sterol biosynthesis
   Cellular componentMembrane
   DomainTransmembrane
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processergosterol biosynthetic process

Traceable author statement. Source: SGD

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from direct assay. Source: SGD

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondelta24(24-1) sterol reductase activity

Traceable author statement. Source: SGD

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Delta(24(24(1)))-sterol reductase
PRO_0000207491

Regions

Topological domain1 – 3939Lumenal Potential
Transmembrane40 – 6425 Potential
Topological domain65 – 10137Cytoplasmic Potential
Transmembrane102 – 12322 Potential
Topological domain124 – 13815Lumenal Potential
Transmembrane139 – 15719 Potential
Topological domain158 – 17417Cytoplasmic Potential
Transmembrane175 – 19723 Potential
Topological domain198 – 23235Lumenal Potential
Transmembrane233 – 24917 Potential
Topological domain250 – 32677Cytoplasmic Potential
Transmembrane327 – 34620 Potential
Topological domain347 – 41468Lumenal Potential
Transmembrane415 – 43925 Potential
Topological domain440 – 47334Cytoplasmic Potential

Experimental info

Sequence conflict3661G → V Ref.1
Sequence conflict3661G → V Ref.2

Sequences

Sequence LengthMass (Da)Tools
P25340-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: B4BFF14559272DD6

FASTA47356,040
        10         20         30         40         50         60 
MAKDNSEKLQ VQGEEKKSKQ PVNFLPQGKW LKPNEIEYEF GGTTGVIGML IGFPLLMYYM 

        70         80         90        100        110        120 
WICAEFYHGK VALPKAGESW MHFIKHLYQL VLENGIPEKY DWTIFLTFWV FQIIFYYTLP 

       130        140        150        160        170        180 
GIWTKGQPLS HLKGKQLPYF CNAMWTLYVT TTLVLVLHFT NLFRLYVIID RFGRIMTCAI 

       190        200        210        220        230        240 
ISGFAFSIIL YLWTLFISHD YHRMTGNHLY DFFMGAPLNP RWGILDLKMF FEVRLPWFTL 

       250        260        270        280        290        300 
YFITLGACLK QWETYGYVTP QLGVVMLAHW LYANACAKGE ELIVPTWDMA YEKFGFMLIF 

       310        320        330        340        350        360 
WNIAGVPYTY CHCTLYLYYH DPSEYHWSTL YNVSLYVVLL CAYYFFDTAN AQKNAFRKQM 

       370        380        390        400        410        420 
SGDKTGRKTF PFLPYQILKN PKYMVTSNGS YLLIDGWYTL ARKIHYTADW TQSLVWALSC 

       430        440        450        460        470 
GFNSVFPWFF PVFFLVVLIH RAFRDQAKCK RKYGKDWDEY CKHCPYVFIP YVF 

« Hide

References

« Hide 'large scale' references
[1]"The YGL022 gene encodes a putative transport protein."
Chen W., Capieaux E., Balzi E., Goffeau A.
Yeast 7:305-308(1991) [PubMed: 1882555] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 46191 / IL125-2B.
[2]"The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6 gene, a new member of the genetic network controlling pleiotropic drug resistance."
Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.
Yeast 7:287-299(1991) [PubMed: 1882553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 46191 / IL125-2B.
[3]"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: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]"The identification of a gene family in the Saccharomyces cerevisiae ergosterol biosynthesis pathway."
Lai M.H., Bard M., Pierson C.A., Alexander J.F., Goebl M., Carter G.T., Kirsch D.R.
Gene 140:41-49(1994) [PubMed: 8125337] [Abstract]
Cited for: CHARACTERIZATION.
[5]"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].
[6]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed: 16847258] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S58126 Genomic DNA. Translation: AAD13895.1.
S57891 Genomic DNA. Translation: AAB19615.1.
Z72534 Genomic DNA. Translation: CAA96712.1.
PIRS64014.
RefSeqNP_011503.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-7177N.
IntActP25340. 22 interactions.
STRINGP25340.

Proteomic databases

PeptideAtlasP25340.

Genome annotation databases

EnsemblYGL012W; YGL012W; YGL012W; Saccharomyces cerevisiae. [Genome view]
GeneID852872.
KEGGsce:YGL012W.
NMPDRfig|4932.3.peg.2611.

Organism-specific databases

CYGDYGL012w.
SGDS000002980. ERG4.

Phylogenomic databases

eggNOGfuNOG07477.
HOGENOMHBG592488.
OMADMAYEKF.
OrthoDBEOG9XPRZ1.
PhylomeDBP25340.

Enzyme and pathway databases

BioCycMetaCyc:YGL012W-MONOMER.
BRENDA1.3.1.71. 250.

Gene expression databases

ArrayExpressP25340.
GenevestigatorP25340.
GermOnlineYGL012W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio972502.

Entry information

Entry nameERG4_YEAST
AccessionPrimary (citable) accession number: P25340
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 1, 1996
Last modified: January 19, 2010
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VII

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents