Reviewed, UniProtKB/Swiss-Prot P32462 (ERG24_YEAST)

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.4
Sequence similarities	Belongs to the ERG4/ERG24 family.

Ontologies

Keywords
Biological process	Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Membrane
Domain	Transmembrane
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	delta14-sterol reductase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P38800	1	EBI-6502,EBI-24597
AGP1	P25376	1	EBI-6502,EBI-2357
CHO1	P08456	1	EBI-6502,EBI-14055
GAP1	P19145	1	EBI-6502,EBI-7314
OST1	P41543	1	EBI-6502,EBI-12651
PMP2	P40975	1	EBI-6502,EBI-2043041
PRP40	P33203	1	EBI-6502,EBI-701
SAS10	Q12136	1	EBI-6502,EBI-36084
SPF1	P39986	1	EBI-6502,EBI-3128

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 438	438	Delta(14)-sterol reductase		PRO_0000207494
Regions
	Topological domain	1 – 13	13	Lumenal Potential
	Transmembrane	14 – 34	21	Potential
	Topological domain	35 – 71	37	Cytoplasmic Potential
	Transmembrane	72 – 90	19	Potential
	Topological domain	91 – 109	19	Lumenal Potential
	Transmembrane	110 – 127	18	Potential
	Topological domain	128 – 147	20	Cytoplasmic Potential
	Transmembrane	148 – 172	25	Potential
	Topological domain	173 – 242	70	Lumenal Potential
	Transmembrane	243 – 263	21	Potential
	Topological domain	264 – 308	45	Cytoplasmic Potential
	Transmembrane	309 – 328	20	Potential
	Topological domain	329 – 368	40	Lumenal Potential
	Transmembrane	369 – 387	19	Potential
	Topological domain	388 – 438	51	Cytoplasmic Potential
Experimental info
	Sequence conflict	253	1	L → S in AAB30203. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P32462-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: B9368B004506C0F3	FASTA	438	50,615
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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].
[5]	"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
EMBLGenBankDDBJ	M99419 Genomic DNA. Translation: AAA18256.1. S69420 Genomic DNA. Translation: AAB30203.1. Z71556 Genomic DNA. Translation: CAA96192.1.
PIR	S30769.
RefSeq	NP_014119.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5155N.
IntAct	P32462. 26 interactions.
Proteomic databases
PeptideAtlas	P32462.
Genome annotation databases
Ensembl	YNL280C. Saccharomyces cerevisiae. [Contig view]
GeneID	855441.
GenomeReviews	Gene locus YNL280C in contig Y13139_GR.
KEGG	sce:YNL280C.
NMPDR	fig|4932.3.peg.5183.
Organism-specific databases
CYGD	YNL280c.
SGD	S000005224. ERG24.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P32462.
OMA	P32462. TMFHLLL.
Enzyme and pathway databases
BioCyc	MetaCyc:YNL280C-MON.
BRENDA	1.3.1.70. 250.
Gene expression databases
ArrayExpress	P32462.
GermOnline	YNL280C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001171. Ergosterol_biosynth_ERG4_ERG24. IPR018083. Sterol_reductase_CS. [Graphical view]
Pfam	PF01222. ERG4_ERG24. 1 hit. [Graphical view]
PROSITE	PS01017. STEROL_REDUCT_1. 1 hit. PS01018. STEROL_REDUCT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	979334.

Entry information

Entry name

ERG24_YEAST

Accession

Primary (citable) accession number: P32462

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)