ID   F6WPW1_MOUSE            Unreviewed;       206 AA.
AC   F6WPW1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Polyprenol reductase {ECO:0000256|ARBA:ARBA00017362, ECO:0000256|RuleBase:RU367081};
DE            EC=1.3.1.22 {ECO:0000256|ARBA:ARBA00012049, ECO:0000256|RuleBase:RU367081};
DE            EC=1.3.1.94 {ECO:0000256|ARBA:ARBA00012522, ECO:0000256|RuleBase:RU367081};
GN   Name=Srd5a3 {ECO:0000313|Ensembl:ENSMUSP00000109135.2,
GN   ECO:0000313|MGI:MGI:1930252};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000109135.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000109135.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000109135.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000109135.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000109135.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Also able to convert testosterone (T) into 5-alpha-
CC       dihydrotestosterone (DHT). {ECO:0000256|RuleBase:RU367081}.
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=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:0000256|ARBA:ARBA00023677};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822;
CC         Evidence={ECO:0000256|ARBA:ARBA00023677};
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:0000256|ARBA:ARBA00033710};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54386;
CC         Evidence={ECO:0000256|ARBA:ARBA00033710};
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:0000256|ARBA:ARBA00023719};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50818;
CC         Evidence={ECO:0000256|ARBA:ARBA00023719};
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|ARBA:ARBA00033658};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34281;
CC         Evidence={ECO:0000256|ARBA:ARBA00033658};
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|ARBA:ARBA00008951,
CC       ECO:0000256|RuleBase:RU367081}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU367081}.
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DR   ProteomicsDB; 329067; -.
DR   Ensembl; ENSMUST00000113506.2; ENSMUSP00000109134.2; ENSMUSG00000029233.16.
DR   Ensembl; ENSMUST00000113507.8; ENSMUSP00000109135.2; ENSMUSG00000029233.16.
DR   AGR; MGI:1930252; -.
DR   MGI; MGI:1930252; Srd5a3.
DR   VEuPathDB; HostDB:ENSMUSG00000029233; -.
DR   GeneTree; ENSGT00500000044920; -.
DR   HOGENOM; CLU_044409_3_0_1; -.
DR   UniPathway; UPA00378; -.
DR   ChiTaRS; Srd5a3; mouse.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000029233; Expressed in lumbar dorsal root ganglion and 235 other cell types or tissues.
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:0047751; F:3-oxo-5alpha-steroid 4-dehydrogenase (NADP+); 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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|EPD:F6WPW1,
KW   ECO:0007829|MaxQB:F6WPW1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
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        44..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367081"
FT   TRANSMEM        87..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367081"
FT   DOMAIN          94..181
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
SQ   SEQUENCE   206 AA;  24108 MW;  EB4CCE795F647A7A CRC64;
     MESKASRMPA AELALSAFLV LVFLWVHSLR RLFECFYVSV FSNAAIHVVQ YCFGLVYYVL
     VGLTVLSQVP MDDKNVYVLG KNLLIQARWF HILGMVMFFW SSAHQYKCHV ILSNLRRNKK
     GVVIHCQHRI PFGDWFEYVS SANYLAELMI YISMAVTFGL HNLTWWLVVT YVFSSQALSA
     FFNHKFYRST FVSYPKHRKA FLPFLF
//