ID   ERG24_ASCIM             Reviewed;         430 AA.
AC   P78575;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=ERG3;
OS   Ascobolus immersus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Ascobolaceae; Ascobolus.
OX   NCBI_TaxID=5191;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RN42;
RA   Kasbekar D.P.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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; Y10624; CAA71650.1; -; Genomic_DNA.
DR   AlphaFoldDB; P78575; -.
DR   SMR; P78575; -.
DR   UniPathway; UPA00770; UER00755.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050613; F:delta14-sterol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001171; ERG24_DHCR-like.
DR   InterPro; IPR018083; Sterol_reductase_CS.
DR   Pfam; PF01222; ERG4_ERG24; 1.
DR   PROSITE; PS01017; STEROL_REDUCT_1; 1.
DR   PROSITE; PS01018; STEROL_REDUCT_2; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..430
FT                   /note="Delta(14)-sterol reductase"
FT                   /id="PRO_0000207495"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         323
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         327
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         350
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         355
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         362..363
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         402
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         406..410
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
FT   BINDING         417
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ   SEQUENCE   430 AA;  49126 MW;  7A61F01A4701B59D CRC64;
     MGGKDYEFGG PIGTGVLMLI LPPISHYLHF LITPRGAPPP EFWSAPLETL KSVTPTFSSL
     FSLHATLAVA AYYLLLVALM YVLPAEIAEG VVLKDGSRLK YRCNAFTTFL VFFTFLGTMT
     VLEGPTWWFW SYLTDNFAQL QSASIVFSYA MSLWVYIRSY RPMPKGKEVI LSPVGFKGNH
     IHDFWMGREL NPRIGEWLDI KQLHELRPGL MGWILFNLAW TVKQYNTHGF VSDSIVLVNL
     FETWYVVDAL WNESKVLTTM DITTDGLGVM LLFGNAVWVP FMYCLQARYL ASFPVHLGLL
     GIAGVLAVQF TGYAIFRGAN NQKNAFRTNP ADPAVSHLKF MTTKSGSKLL ISGWWGVARH
     VNYFGDWIMA WSYCLTTGFN TPLTYFYVIY FGILLLHRDR RDEAKCREKY GKDWDRYCKV
     VKWRIIPGIY