ERG24_DICDI
ID ERG24_DICDI Reviewed; 462 AA.
AC Q54PP1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Delta(14)-sterol reductase;
DE EC=1.3.1.70;
DE AltName: Full=C-14 sterol reductase;
DE AltName: Full=Sterol C14-reductase;
GN Name=erg24; ORFNames=DDB_G0284407;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-
CC 8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) =
CC 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH;
CC Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813,
CC ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70;
CC -!- PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from
CC lanosterol: step 2/6.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ERG4/ERG24 family. {ECO:0000305}.
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DR EMBL; AAFI02000064; EAL65252.1; -; Genomic_DNA.
DR RefSeq; XP_638613.1; XM_633521.1.
DR AlphaFoldDB; Q54PP1; -.
DR SMR; Q54PP1; -.
DR STRING; 44689.DDB0232079; -.
DR TCDB; 1.I.1.1.5; the nuclear pore complex (npc) family.
DR PaxDb; Q54PP1; -.
DR EnsemblProtists; EAL65252; EAL65252; DDB_G0284407.
DR GeneID; 8624584; -.
DR KEGG; ddi:DDB_G0284407; -.
DR dictyBase; DDB_G0284407; erg24.
DR eggNOG; KOG1435; Eukaryota.
DR HOGENOM; CLU_015631_0_3_1; -.
DR InParanoid; Q54PP1; -.
DR OMA; GWIILNC; -.
DR PhylomeDB; Q54PP1; -.
DR Reactome; R-DDI-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00770; UER00755.
DR PRO; PR:Q54PP1; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:dictyBase.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:dictyBase.
DR GO; GO:0050613; F:delta14-sterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000246; F:delta24(24-1) sterol reductase activity; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IBA:GO_Central.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001171; ERG24_DHCR-like.
DR Pfam; PF01222; ERG4_ERG24; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..462
FT /note="Delta(14)-sterol reductase"
FT /id="PRO_0000331122"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 354
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 358
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 382
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 387
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 394..395
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 434
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 438..442
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 449
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ SEQUENCE 462 AA; 53763 MW; F414DFF497147FA1 CRC64;
MSAVRNRNNV EKQSNNGAQL TEVQKKELAD LQKVHPANEF GGIIGTFLLT FILPVVVYWI
WASIEFNNGY LLRPETLSVE GVKAFLAQLY HYVITYAYPT KEAAIIYFSW FGFQAFLQHV
VPGRKVLGSP LPGGARLEYT LNGWASWWIT LIVIPIAIYF GLFKATILID NYAPMMTVVN
IWSFVFTFLL KIHAKLKGEE ERMSGHFFYD FWMGFARNPR IGSFDLKLFC EARPGLILWV
LMNFSIAAKQ LEVYGEISLS VILVCCFHFW YIADYYYHEE AILTTMDIIT EKFGYMLVYG
DLSWVPFTYC FQCYYLYKHL VNGAPLHISI GYAIFVVSLK CFGFYLFRWV NSQKHDFRRN
PEAPVWGKPA EFILTKRGTK LLCSGFWGIC RHLNYTGDII LSWAWCLPCQ FDSLAPYFYG
IYFTSLDLHR CWRDHNACLV KYGDDWRAYC KRVPYNFIPG LI
