Reviewed, UniProtKB/Swiss-Prot Q54PP1 (ERG24_DICDI)

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
ORF Names:	DDB_G0284407

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
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.
Pathway	Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 2/6.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 462	462	Delta(14)-sterol reductase		PRO_0000331122
Regions
	Transmembrane	40 – 60	21	Potential
	Transmembrane	103 – 123	21	Potential
	Transmembrane	143 – 163	21	Potential
	Transmembrane	172 – 192	21	Potential
	Transmembrane	253 – 273	21	Potential
	Transmembrane	293 – 313	21	Potential
	Transmembrane	327 – 347	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q54PP1-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: F414DFF497147FA1	FASTA	462	53,763
	10 20 30 40 50 60 MSAVRNRNNV EKQSNNGAQL TEVQKKELAD LQKVHPANEF GGIIGTFLLT FILPVVVYWI 70 80 90 100 110 120 WASIEFNNGY LLRPETLSVE GVKAFLAQLY HYVITYAYPT KEAAIIYFSW FGFQAFLQHV 130 140 150 160 170 180 VPGRKVLGSP LPGGARLEYT LNGWASWWIT LIVIPIAIYF GLFKATILID NYAPMMTVVN 190 200 210 220 230 240 IWSFVFTFLL KIHAKLKGEE ERMSGHFFYD FWMGFARNPR IGSFDLKLFC EARPGLILWV 250 260 270 280 290 300 LMNFSIAAKQ LEVYGEISLS VILVCCFHFW YIADYYYHEE AILTTMDIIT EKFGYMLVYG 310 320 330 340 350 360 DLSWVPFTYC FQCYYLYKHL VNGAPLHISI GYAIFVVSLK CFGFYLFRWV NSQKHDFRRN 370 380 390 400 410 420 PEAPVWGKPA EFILTKRGTK LLCSGFWGIC RHLNYTGDII LSWAWCLPCQ FDSLAPYFYG 430 440 450 460 IYFTSLDLHR CWRDHNACLV KYGDDWRAYC KRVPYNFIPG LI

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000064 Genomic DNA. Translation: EAL65252.1.
RefSeq	XP_638613.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3390188.
KEGG	ddi:DDB_0232079.
Organism-specific databases
dictyBase	DDB_G0284407. erg24.
Phylogenomic databases
OMA	Q54PP1. TMFHLLL.
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. False negative. PS01018. STEROL_REDUCT_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ERG24_DICDI

Accession

Primary (citable) accession number: Q54PP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 24, 2005
Last modified:	June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)