ID   H9KV08_MOUSE            Unreviewed;        74 AA.
AC   H9KV08;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Polyprenol reductase {ECO:0000256|RuleBase:RU367081};
DE            EC=1.3.1.22 {ECO:0000256|RuleBase:RU367081};
DE            EC=1.3.1.94 {ECO:0000256|RuleBase:RU367081};
DE   Flags: Fragment;
GN   Name=Srd5a3 {ECO:0000313|Ensembl:ENSMUSP00000116801.2,
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:ENSMUSP00000116801.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000116801.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000116801.2,
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:ENSMUSP00000116801.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000116801.2};
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|RuleBase:RU367081};
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|RuleBase:RU367081};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|RuleBase:RU367081}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU367081}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol
CC       reductase subfamily. {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   AlphaFoldDB; H9KV08; -.
DR   Ensembl; ENSMUST00000127278.8; ENSMUSP00000116801.2; ENSMUSG00000029233.16.
DR   AGR; MGI:1930252; -.
DR   MGI; MGI:1930252; Srd5a3.
DR   VEuPathDB; HostDB:ENSMUSG00000029233; -.
DR   GeneTree; ENSGT00500000044920; -.
DR   HOGENOM; CLU_2694255_0_0_1; -.
DR   OMA; HMFFEVV; -.
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   ExpressionAtlas; H9KV08; baseline and differential.
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; IPR039698; Dfg10/SRD5A3.
DR   PANTHER; PTHR14624; DFG10 PROTEIN; 1.
DR   PANTHER; PTHR14624:SF0; POLYPRENOL REDUCTASE; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU367081};
KW   Membrane {ECO:0000256|RuleBase:RU367081};
KW   NADP {ECO:0000256|RuleBase:RU367081};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU367081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transmembrane {ECO:0000256|RuleBase:RU367081};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU367081}.
FT   TRANSMEM        44..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367081"
FT   NON_TER         74
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000116801.2"
SQ   SEQUENCE   74 AA;  8391 MW;  E592DED311716432 CRC64;
     MESKASRMPA AELALSAFLV LVFLWVHSLR RLFECFYVSV FSNAAIHVVQ YCFGLVYYVL
     VGLTVLSQVP MDDK
//