PORED_MESAU
ID PORED_MESAU Reviewed; 330 AA.
AC C7T2J9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Polyprenol reductase;
DE EC=1.3.1.94;
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 {ECO:0000303|Ref.1};
DE Short=S5AR 3;
DE Short=SR type 3;
GN Name=Srd5a3 {ECO:0000303|Ref.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Harderian gland;
RA Vilchis F., Ramos L., Chavez B.;
RT "Cloning, sequence analysis and tissue distribution of the steroid 5alpha-
RT reductase 3 (Srd5a3) full-length cDNA from Syrian hamster.";
RL Submitted (MAR-2009) 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}.
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DR EMBL; FJ851160; ACV30167.1; -; mRNA.
DR RefSeq; NP_001268635.1; NM_001281706.1.
DR AlphaFoldDB; C7T2J9; -.
DR SMR; C7T2J9; -.
DR STRING; 10036.XP_005080829.1; -.
DR GeneID; 101843963; -.
DR CTD; 79644; -.
DR eggNOG; KOG1640; Eukaryota.
DR OrthoDB; 1574389at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000189706; 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: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..330
FT /note="Polyprenol reductase"
FT /id="PRO_0000398649"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..74
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..277
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 38164 MW; 6E7990C37A6D27D6 CRC64;
MASWVGTELS ALNPLRTLWL ALAAAFLLAL LLQLAPAGLL PNCALFQDLI RYGKTKLSGP
RRPAVCRAFD VPKRYFSHFY VVSVLWNGFL LWFLSRSLFL GAPFPNWLRA LLRTLGSTQF
RALEMESKAS QMLVGELALS AFLVLVFLWV HSVRRLFECF YISVFSNAVM HVVQYCFGLV
YYVLVGLTVL SQVPMDDKNV YMLGKNLLLP ARWFHVLGMM MFLWSSAHQY ECHVILSNLR
RNKKGAIVHC QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGFHNFTWW LVVAYVFFCQ
ALSAFFNHKF YKSTFVSYPK HRKAFLPFLF
