ID   PORED_XENTR             Reviewed;         308 AA.
AC   Q0P4J9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Polyprenol reductase;
DE            EC=1.3.1.94 {ECO:0000250|UniProtKB:Q9H8P0};
DE   AltName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3;
DE            EC=1.3.1.22 {ECO:0000250|UniProtKB:Q9H8P0};
DE   AltName: Full=Steroid 5-alpha-reductase 3;
DE            Short=S5AR 3;
DE            Short=SR type 3;
GN   Name=srd5a3;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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. Also able to convert testosterone (T) into 5-
CC       alpha-dihydrotestosterone (DHT). {ECO:0000250|UniProtKB:Q9H8P0}.
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:0000250|UniProtKB:Q9H8P0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34281;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid +
CC         H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.3.1.22;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54386;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-4-ene-3,17-dione + H(+) + NADPH = 5alpha-
CC         androstan-3,17-dione + NADP(+); Xref=Rhea:RHEA:50816,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16422,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50818;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = H(+) + NADPH
CC         + testosterone; Xref=Rhea:RHEA:50820, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16330, ChEBI:CHEBI:17347, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.3.1.22;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822;
CC         Evidence={ECO:0000250|UniProtKB:Q9H8P0};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9H8P0}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9H8P0}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9H8P0}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; BC122039; AAI22040.1; -; mRNA.
DR   RefSeq; NP_001072539.1; NM_001079071.1.
DR   AlphaFoldDB; Q0P4J9; -.
DR   SMR; Q0P4J9; -.
DR   STRING; 8364.ENSXETP00000029132; -.
DR   PaxDb; 8364-ENSXETP00000045522; -.
DR   DNASU; 779994; -.
DR   GeneID; 779994; -.
DR   KEGG; xtr:779994; -.
DR   AGR; Xenbase:XB-GENE-985511; -.
DR   CTD; 79644; -.
DR   Xenbase; XB-GENE-985511; srd5a3.
DR   eggNOG; KOG1640; Eukaryota.
DR   HOGENOM; CLU_044409_2_1_1; -.
DR   InParanoid; Q0P4J9; -.
DR   OrthoDB; 2896758at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:InterPro.
DR   GO; GO:0047751; F:3-oxo-5alpha-steroid 4-dehydrogenase (NADP+); ISS:UniProtKB.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:UniProtKB.
DR   GO; GO:0102389; F:polyprenol reductase activity; IEA:UniProtKB-EC.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..308
FT                   /note="Polyprenol reductase"
FT                   /id="PRO_0000317706"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..65
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..148
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..255
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        277..308
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   308 AA;  35876 MW;  FFE931DCDB0D558A CRC64;
     MTLLALVWLL LDATFLITLL WHLLQGCKSG HSLLCSVFQD LIRYGKTKTG LQRPAWLQWF
     DIPKRCFWHF YCVSLIWNGC LLWILLRLLL QSVPVPEWLQ LVLHFLHAGS EPQILDRELS
     VILALALLWL HSLRRLLECL FVSVFSNGVI HLVQYCFGLG YYFLIGITVL TYCPLDRRTV
     STDNLLTQCH WYHILGLALY IWASLHQYRC HCILAGLRKS ASGNVINLNH SVPCGDWFER
     VSCPHYFAEL LIYVSIAVVF GLLNTIWWLV VLYVLLNQAL AALLCHEFYH EKFDTYPIHR
     KAFIPFIF
//