ERG24_NEUCR
ID ERG24_NEUCR Reviewed; 490 AA.
AC P38670; Q7RV50;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=erg-3; Synonyms=erg3; ORFNames=B2G14.010, NCU08762;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RA Papavinasasundaram K.G., Kasbekar D.P.;
RT "The Neurospora crassa erg3 gene encodes a protein with sequence homology
RT to both yeast sterol C-14 reductase and chicken lamin B receptor.";
RL J. Genet. 73:33-41(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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 -!- 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; X77955; CAA54919.1; -; Genomic_DNA.
DR EMBL; BX284753; CAD70446.1; -; Genomic_DNA.
DR EMBL; CM002238; EAA26875.1; -; Genomic_DNA.
DR PIR; S44170; S44170.
DR RefSeq; XP_956111.1; XM_951018.2.
DR AlphaFoldDB; P38670; -.
DR SMR; P38670; -.
DR STRING; 5141.EFNCRP00000004754; -.
DR EnsemblFungi; EAA26875; EAA26875; NCU08762.
DR GeneID; 3872249; -.
DR KEGG; ncr:NCU08762; -.
DR VEuPathDB; FungiDB:NCU08762; -.
DR HOGENOM; CLU_015631_0_3_1; -.
DR InParanoid; P38670; -.
DR OMA; GWIILNC; -.
DR UniPathway; UPA00770; UER00755.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0050613; F:delta14-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 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 Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..490
FT /note="Delta(14)-sterol reductase"
FT /id="PRO_0000207497"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 351
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 378
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 383
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 390..391
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 462
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 466..470
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
FT BINDING 477
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:G4SW86"
SQ SEQUENCE 490 AA; 54722 MW; 9CF3104EF3014085 CRC64;
MAGKQNQAAP KKAVAPRQQH YEFGGPIGAF GITFGLPILV HVFNLFCNDI SGCPAPSLLH
PKSLDLAQLK REIGWPDNGV FGLFSWSATL WTLGYYALSL VQYRFLPGHH VEGTELSTGG
RLKYKLNAFN SAMCTLAILA AGTIAQGAEF PVWTFISDNF AQIISANILF AFALAIFVYV
RSFDVKPGNK DMRQLAAGGV TGSLIYDFYI GRELNPRITL PLIGQVDIKE FMEMRPGLLG
WIILNCAFIA KQYRLYGYVT DSILFITAIQ AFYVFDGIYM EPAVLTTMDI TTDGFGFMLS
FGDVVWVPFM YSTQTRYLSV HPQQLGAFGL IAVGAVLAAG YSIFRLSNSQ KNNFRTNPED
PSVKHLTYLQ TKTGSRLITS GWWGIARHIN YLGDWLQSWP YSLPTGIAGY QILSAGSNAP
GAITMLDGRE VVQGEARGWG IVFTYFYILY FAILLIHRDL RDDEKCSKKY GDDWEKYKKL
VKWRIVPGIY
