ID G0W3M8_NAUDC Unreviewed; 252 AA.
AC G0W3M8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Polyprenol reductase {ECO:0000256|RuleBase:RU367081};
DE EC=1.3.1.94 {ECO:0000256|RuleBase:RU367081};
GN Name=NDAI0A02580 {ECO:0000313|EMBL:CCD22416.1};
GN OrderedLocusNames=NDAI_0A02580 {ECO:0000313|EMBL:CCD22416.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD22416.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD22416.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- FUNCTION: Plays a key role in early steps of protein N-linked
CC glycosylation by being required for the conversion of polyprenol into
CC dolichol. Dolichols are required for the synthesis of dolichol-linked
CC monosaccharides and the oligosaccharide precursor used for N-
CC glycosylation. Acts as a polyprenol reductase that promotes the
CC reduction of the alpha-isoprene unit of polyprenols into dolichols in a
CC NADP-dependent mechanism. {ECO:0000256|RuleBase:RU367081}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,poly-cis-dolichol + NADP(+) = di-trans,cis-polyprenol
CC + H(+) + NADPH; Xref=Rhea:RHEA:34279, Rhea:RHEA-COMP:9521, Rhea:RHEA-
CC COMP:9525, ChEBI:CHEBI:15378, ChEBI:CHEBI:16091, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:67132; EC=1.3.1.94;
CC Evidence={ECO:0000256|RuleBase:RU367081};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367081}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367081}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC reductase subfamily. {ECO:0000256|RuleBase:RU367081}.
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DR EMBL; HE580267; CCD22416.1; -; Genomic_DNA.
DR RefSeq; XP_003667659.1; XM_003667611.1.
DR AlphaFoldDB; G0W3M8; -.
DR STRING; 1071378.G0W3M8; -.
DR GeneID; 11495325; -.
DR KEGG; ndi:NDAI_0A02580; -.
DR eggNOG; KOG1640; Eukaryota.
DR HOGENOM; CLU_044409_0_0_1; -.
DR OMA; HMFFEVV; -.
DR OrthoDB; 2896758at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000689; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016095; P:polyprenol catabolic process; IEA:UniProtKB-UniRule.
DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR InterPro; IPR039698; Dfg10/SRD5A3.
DR PANTHER; PTHR14624; DFG10 PROTEIN; 1.
DR PANTHER; PTHR14624:SF0; POLYPRENOL REDUCTASE; 1.
DR Pfam; PF02544; Steroid_dh; 1.
DR PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367081};
KW NADP {ECO:0000256|RuleBase:RU367081};
KW Oxidoreductase {ECO:0000256|RuleBase:RU367081};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367081}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 70..99
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 119..142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT TRANSMEM 198..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367081"
FT DOMAIN 154..232
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 252 AA; 30218 MW; 88B9EBA9EF795DD3 CRC64;
MEIDPLLQLV TYLYRISFFI GFLSVIVAKL YLPDFLEYGK TLKDHDEPQN KTILQKIIHF
TVPKAYFSHF YYLSSVLSLV TFCYYPSYPI VWMLLFHSLR RLYETLYTSK YSAKSRMNWS
HYVVGIWFYS TLHIILGIKL HYQEIPRYPR DTFTFLIFFL ASWDQYKNHE VLANLVKYSL
PKERLFKLVS CPHYLDELII YGSFIAFNNE FCWLFVWVFV SLGISALETK AFYQLKFKDE
VVPKYAMVPF IL
//