PORED_XENTR
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 03-AUG-2022, entry version 78.
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-androstan-
CC 3,17-dione + NADP(+); Xref=Rhea:RHEA:50816, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15994, ChEBI:CHEBI:16422, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC122039; AAI22040.1; -; mRNA.
DR RefSeq; NP_001072539.1; NM_001079071.1.
DR AlphaFoldDB; Q0P4J9; -.
DR STRING; 8364.ENSXETP00000045522; -.
DR PaxDb; Q0P4J9; -.
DR DNASU; 779994; -.
DR GeneID; 779994; -.
DR KEGG; xtr:779994; -.
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; 1574389at2759; -.
DR Reactome; R-XTR-193048; Androgen biosynthesis.
DR Reactome; R-XTR-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0047751; F:cholestenone 5-alpha-reductase activity; IEA:UniProtKB-EC.
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: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; PTHR14624; 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
