Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei335NADPBy similarity1
Binding sitei339NADPBy similarity1
Binding sitei358NADP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei363NADPBy similarity1
Binding sitei410NADPBy similarity1
Binding sitei425NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi370 – 371NADPBy similarity2
Nucleotide bindingi414 – 418NADPBy similarity5

GO - Molecular functioni

  • delta14-sterol reductase activity Source: SGD
  • NADP binding Source: UniProtKB

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 13LumenalSequence analysisAdd BLAST13
Transmembranei14 – 34HelicalSequence analysisAdd BLAST21
Topological domaini35 – 71CytoplasmicSequence analysisAdd BLAST37
Transmembranei72 – 90HelicalSequence analysisAdd BLAST19
Topological domaini91 – 109LumenalSequence analysisAdd BLAST19
Transmembranei110 – 127HelicalSequence analysisAdd BLAST18
Topological domaini128 – 147CytoplasmicSequence analysisAdd BLAST20
Transmembranei148 – 172HelicalSequence analysisAdd BLAST25
Topological domaini173 – 242LumenalSequence analysisAdd BLAST70
Transmembranei243 – 263HelicalSequence analysisAdd BLAST21
Topological domaini264 – 308CytoplasmicSequence analysisAdd BLAST45
Transmembranei309 – 328HelicalSequence analysisAdd BLAST20
Topological domaini329 – 368LumenalSequence analysisAdd BLAST40
Transmembranei369 – 387HelicalSequence analysisAdd BLAST19
Topological domaini388 – 438CytoplasmicSequence analysisAdd BLAST51

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002074941 – 438Delta(14)-sterol reductaseAdd BLAST438

Proteomic databases

MaxQBiP32462.
PRIDEiP32462.
TopDownProteomicsiP32462.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP32462.
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.
OrthoDBiEOG092C2JRW.

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)DescriptionActionsGraphical viewLength
Sequence conflicti253L → S in AAB30203 (PubMed:8125337).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP32462.
PRIDEiP32462.
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.
OrthoDBiEOG092C2JRW.

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...

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: November 2, 2016
This is version 136 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.