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P32462 (ERG24_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 93. Feed History...

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

Names and origin

Protein namesRecommended name:
Delta(14)-sterol reductase
EC=1.3.1.70
Alternative name(s):
C-14 sterol reductase
Sterol C14-reductase
Gene names
Name:ERG24
Ordered Locus Names:YNL280C
ORF Names:N0593
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol.

Catalytic activity

4,4-dimethyl-5-alpha-cholesta-8,24-dien-3-beta-ol + NADP+ = 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3-beta-ol + NADPH.

Enzyme regulation

Inhibited by the morpholine antifungal drug fenpropimorph.

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 2/6.

Subcellular location

Membrane; Multi-pass membrane protein.

Miscellaneous

Present with 1600 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the ERG4/ERG24 family.

Ontologies

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

Inferred from mutant phenotype Ref.1. Source: SGD

   Cellular componentendoplasmic reticulum

Inferred from direct assay. Source: SGD

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiondelta14-sterol reductase activity

Inferred from direct assay. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Delta(14)-sterol reductase
PRO_0000207494

Regions

Topological domain1 – 1313Lumenal Potential
Transmembrane14 – 3421Helical; Potential
Topological domain35 – 7137Cytoplasmic Potential
Transmembrane72 – 9019Helical; Potential
Topological domain91 – 10919Lumenal Potential
Transmembrane110 – 12718Helical; Potential
Topological domain128 – 14720Cytoplasmic Potential
Transmembrane148 – 17225Helical; Potential
Topological domain173 – 24270Lumenal Potential
Transmembrane243 – 26321Helical; Potential
Topological domain264 – 30845Cytoplasmic Potential
Transmembrane309 – 32820Helical; Potential
Topological domain329 – 36840Lumenal Potential
Transmembrane369 – 38719Helical; Potential
Topological domain388 – 43851Cytoplasmic Potential

Experimental info

Sequence conflict2531L → S in AAB30203. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32462 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: B9368B004506C0F3

FASTA43850,615
        10         20         30         40         50         60 
MVSALNPRTT EFEFGGLIGA LGISIGLPVF TIILNQMIRP DYFIKGFFQN FDIVELWNGI 

        70         80         90        100        110        120 
KPLRYYLGNR ELWTVYCLWY GILAVLDVIL PGRVMKGVQL RDGSKLSYKI NGIAMSTTLV 

       130        140        150        160        170        180 
LVLAIRWKLT DGQLPELQYL YENHVSLCII SILFSFFLAT YCYVASFIPL IFKKNGNGKR 

       190        200        210        220        230        240 
EKILALGGNS GNIIYDWFIG RELNPRLGPL DIKMFSELRP GMLLWLLINL SCLHHHYLKT 

       250        260        270        280        290        300 
GKINDALVLV NFLQGFYIFD GVLNEEGVLT MMDITTDGFG FMLAFGDLSL VPFTYSLQAR 

       310        320        330        340        350        360 
YLSVSPVELG WVKVVGILAI MFLGFHIFHS ANKQKSEFRQ GKLENLKSIQ TKRGTKLLCD 

       370        380        390        400        410        420 
GWWAKSQHIN YFGDWLISLS WCLATWFQTP LTYYYSLYFA TLLLHRQQRD EHKCRLKYGE 

       430 
NWEEYERKVP YKIIPYVY

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and disruption of the gene encoding sterol C-14 reductase in Saccharomyces cerevisiae."
Lorenz R.T., Parks L.W.
DNA Cell Biol. 11:685-692(1992) [PubMed: 1418625] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed: 9169873] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[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].
Strain: ATCC 208353 / W303-1A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M99419 Genomic DNA. Translation: AAA18256.1.
S69420 Genomic DNA. Translation: AAB30203.1.
Z71556 Genomic DNA. Translation: CAA96192.1.
BK006947 Genomic DNA. Translation: DAA10280.1.
PIRS30769.
RefSeqNP_014119.1. NM_001183118.1.

3D structure databases

ProteinModelPortalP32462.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5155N.
IntActP32462. 25 interactions.
MINTMINT-507875.
STRINGP32462.

Proteomic databases

PeptideAtlasP32462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL280C; YNL280C; YNL280C.
GeneID855441.
KEGGsce:YNL280C.
NMPDRfig|4932.3.peg.5183.

Organism-specific databases

CYGDYNL280c.
SGDS000005224. ERG24.

Phylogenomic databases

eggNOGfuNOG04486.
GeneTreeEFGT00050000001699.
HOGENOMHBG592488.
OMATMFHLLL.
OrthoDBEOG4R273N.

Enzyme and pathway databases

BioCycMetaCyc:YNL280C-MONOMER.

Gene expression databases

ArrayExpressP32462.
GenevestigatorP32462.
GermOnlineYNL280C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
KOK00222.
PfamPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979334.

Entry information

Entry nameERG24_YEAST
AccessionPrimary (citable) accession number: P32462
Secondary accession number(s): D6W0R4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: December 14, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIV

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents