ID   PORED_CAEEL             Reviewed;         309 AA.
AC   Q17428; Q7JLP4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Polyprenol reductase;
DE            EC=1.3.1.94;
GN   ORFNames=B0024.13;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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 (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; Z71178; CAA94885.2; -; Genomic_DNA.
DR   PIR; T18648; T18648.
DR   RefSeq; NP_001256209.1; NM_001269280.1.
DR   AlphaFoldDB; Q17428; -.
DR   SMR; Q17428; -.
DR   STRING; 6239.B0024.13.1; -.
DR   EPD; Q17428; -.
DR   PaxDb; 6239-B0024-13; -.
DR   PeptideAtlas; Q17428; -.
DR   EnsemblMetazoa; B0024.13.1; B0024.13.1; WBGene00007102.
DR   GeneID; 179438; -.
DR   KEGG; cel:CELE_B0024.13; -.
DR   UCSC; B0024.13a; c. elegans.
DR   AGR; WB:WBGene00007102; -.
DR   WormBase; B0024.13; CE35376; WBGene00007102; -.
DR   eggNOG; KOG1640; Eukaryota.
DR   GeneTree; ENSGT00500000044920; -.
DR   HOGENOM; CLU_044409_2_1_1; -.
DR   InParanoid; Q17428; -.
DR   OMA; FEICIYL; -.
DR   OrthoDB; 2896758at2759; -.
DR   PhylomeDB; Q17428; -.
DR   Reactome; R-CEL-193048; Androgen biosynthesis.
DR   Reactome; R-CEL-446199; Synthesis of Dolichyl-phosphate.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q17428; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00007102; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019408; P:dolichol biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019348; P:dolichol metabolic process; ISS:UniProtKB.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0016095; P:polyprenol catabolic process; ISS:UniProtKB.
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; Membrane; NADP; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..309
FT                   /note="Polyprenol reductase"
FT                   /id="PRO_0000398653"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   309 AA;  35430 MW;  1D4F125A25B3A9EC CRC64;
     MLDRLWEVRQ ALPLYLLVST LGLAISCCFT LICPHVCRLI PALTTYGKAA DQQEDNSLVE
     KISVPKKWFK HFYAIGLLTL FICLHTVHSL IYNPNYLHPV VLKILATLTR SYSIPPITPS
     TSILALLLIS LHVARRLYET IFVSVYSDSR MNLFHYAVGI VHYIILPISI MCETQGVASK
     LPQLHVSIDD ISLTQWAGAV LFWICNWKQH QLAEQIANTR KGPRGLIRNY AYGICFGGWF
     NLVSCPHFLF EICIYLSLFL VIPDAYVYRF IIMFVCINQT FAALITHSWY HKTFPKYPKS
     RKALIPYVL
//