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Protein

Delta(14)-sterol reductase

Gene

ERG24

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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 regulationi

Inhibited by the morpholine antifungal drug fenpropimorph.

Pathwayi: zymosterol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes zymosterol from lanosterol.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Lanosterol 14-alpha demethylase (ERG11)
  2. Delta(14)-sterol reductase (ERG24)
  3. Methylsterol monooxygenase (ERG25)
  4. Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (ERG26)
  5. 3-keto-steroid reductase (ERG27)
  6. no protein annotated in this organism
This subpathway is part of the pathway zymosterol biosynthesis, which is itself part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes zymosterol from lanosterol, the pathway zymosterol biosynthesis and in Steroid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei335 – 3351NADPBy similarity
Binding sitei339 – 3391NADPBy similarity
Binding sitei358 – 3581NADP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei363 – 3631NADPBy similarity
Binding sitei410 – 4101NADPBy similarity
Binding sitei425 – 4251NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi370 – 3712NADPBy similarity
Nucleotide bindingi414 – 4185NADPBy similarity

GO - Molecular functioni

  • delta14-sterol reductase activity Source: SGD

GO - Biological processi

  • ergosterol biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:YNL280C-MONOMER.
YEAST:YNL280C-MONOMER.
ReactomeiR-SCE-191273. Cholesterol biosynthesis.
R-SCE-2426168. Activation of gene expression by SREBF (SREBP).
R-SCE-6807047. Cholesterol biosynthesis via desmosterol.
R-SCE-6807062. Cholesterol biosynthesis via lathosterol.
UniPathwayiUPA00770; UER00755.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta(14)-sterol reductase (EC:1.3.1.70)
Alternative name(s):
C-14 sterol reductase
Sterol C14-reductase
Gene namesi
Name:ERG24
Ordered Locus Names:YNL280C
ORF Names:N0593
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL280C.
SGDiS000005224. ERG24.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313LumenalSequence analysisAdd
BLAST
Transmembranei14 – 3421HelicalSequence analysisAdd
BLAST
Topological domaini35 – 7137CytoplasmicSequence analysisAdd
BLAST
Transmembranei72 – 9019HelicalSequence analysisAdd
BLAST
Topological domaini91 – 10919LumenalSequence analysisAdd
BLAST
Transmembranei110 – 12718HelicalSequence analysisAdd
BLAST
Topological domaini128 – 14720CytoplasmicSequence analysisAdd
BLAST
Transmembranei148 – 17225HelicalSequence analysisAdd
BLAST
Topological domaini173 – 24270LumenalSequence analysisAdd
BLAST
Transmembranei243 – 26321HelicalSequence analysisAdd
BLAST
Topological domaini264 – 30845CytoplasmicSequence analysisAdd
BLAST
Transmembranei309 – 32820HelicalSequence analysisAdd
BLAST
Topological domaini329 – 36840LumenalSequence analysisAdd
BLAST
Transmembranei369 – 38719HelicalSequence analysisAdd
BLAST
Topological domaini388 – 43851CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Delta(14)-sterol reductasePRO_0000207494Add
BLAST

Proteomic databases

MaxQBiP32462.
TopDownProteomicsiP32462.

Interactioni

Protein-protein interaction databases

BioGridi35561. 36 interactions.
DIPiDIP-5155N.
IntActiP32462. 16 interactions.
MINTiMINT-507875.

Structurei

3D structure databases

ProteinModelPortaliP32462.
SMRiP32462. Positions 56-438.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ERG4/ERG24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000000417.
HOGENOMiHOG000193296.
InParanoidiP32462.
KOiK00222.
OMAiVCNDISG.
OrthoDBiEOG7HB5MF.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32462-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSALNPRTT EFEFGGLIGA LGISIGLPVF TIILNQMIRP DYFIKGFFQN
60 70 80 90 100
FDIVELWNGI KPLRYYLGNR ELWTVYCLWY GILAVLDVIL PGRVMKGVQL
110 120 130 140 150
RDGSKLSYKI NGIAMSTTLV LVLAIRWKLT DGQLPELQYL YENHVSLCII
160 170 180 190 200
SILFSFFLAT YCYVASFIPL IFKKNGNGKR EKILALGGNS GNIIYDWFIG
210 220 230 240 250
RELNPRLGPL DIKMFSELRP GMLLWLLINL SCLHHHYLKT GKINDALVLV
260 270 280 290 300
NFLQGFYIFD GVLNEEGVLT MMDITTDGFG FMLAFGDLSL VPFTYSLQAR
310 320 330 340 350
YLSVSPVELG WVKVVGILAI MFLGFHIFHS ANKQKSEFRQ GKLENLKSIQ
360 370 380 390 400
TKRGTKLLCD GWWAKSQHIN YFGDWLISLS WCLATWFQTP LTYYYSLYFA
410 420 430
TLLLHRQQRD EHKCRLKYGE NWEEYERKVP YKIIPYVY
Length:438
Mass (Da):50,615
Last modified:October 1, 1993 - v1
Checksum:iB9368B004506C0F3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531L → S in AAB30203 (PubMed:8125337).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99419 Genomic DNA. Translation: AAA18256.1.
S69420 Genomic DNA. Translation: AAB30203.1.
Z71556 Genomic DNA. Translation: CAA96192.1.
BK006947 Genomic DNA. Translation: DAA10280.1.
PIRiS30769.
RefSeqiNP_014119.1. NM_001183118.1.

Genome annotation databases

EnsemblFungiiYNL280C; YNL280C; YNL280C.
GeneIDi855441.
KEGGisce:YNL280C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M99419 Genomic DNA. Translation: AAA18256.1.
S69420 Genomic DNA. Translation: AAB30203.1.
Z71556 Genomic DNA. Translation: CAA96192.1.
BK006947 Genomic DNA. Translation: DAA10280.1.
PIRiS30769.
RefSeqiNP_014119.1. NM_001183118.1.

3D structure databases

ProteinModelPortaliP32462.
SMRiP32462. Positions 56-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35561. 36 interactions.
DIPiDIP-5155N.
IntActiP32462. 16 interactions.
MINTiMINT-507875.

Proteomic databases

MaxQBiP32462.
TopDownProteomicsiP32462.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL280C; YNL280C; YNL280C.
GeneIDi855441.
KEGGisce:YNL280C.

Organism-specific databases

EuPathDBiFungiDB:YNL280C.
SGDiS000005224. ERG24.

Phylogenomic databases

GeneTreeiENSGT00390000000417.
HOGENOMiHOG000193296.
InParanoidiP32462.
KOiK00222.
OMAiVCNDISG.
OrthoDBiEOG7HB5MF.

Enzyme and pathway databases

UniPathwayiUPA00770; UER00755.
BioCyciMetaCyc:YNL280C-MONOMER.
YEAST:YNL280C-MONOMER.
ReactomeiR-SCE-191273. Cholesterol biosynthesis.
R-SCE-2426168. Activation of gene expression by SREBF (SREBP).
R-SCE-6807047. Cholesterol biosynthesis via desmosterol.
R-SCE-6807062. Cholesterol biosynthesis via lathosterol.

Miscellaneous databases

PROiP32462.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
IPR018083. Sterol_reductase_CS.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 1 hit.
[Graphical view]
PROSITEiPS01017. STEROL_REDUCT_1. 1 hit.
PS01018. STEROL_REDUCT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiERG24_YEAST
AccessioniPrimary (citable) accession number: P32462
Secondary accession number(s): D6W0R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 6, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.