ID   S5A1_MOUSE              Reviewed;         255 AA.
AC   Q68FF9; Q505K7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-NOV-2023, entry version 117.
DE   RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 1 {ECO:0000305};
DE            EC=1.3.1.22 {ECO:0000250|UniProtKB:P18405};
DE   AltName: Full=SR type 1;
DE   AltName: Full=Steroid 5-alpha-reductase 1;
DE            Short=S5AR 1;
GN   Name=Srd5a1 {ECO:0000312|MGI:MGI:98400};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Converts testosterone into 5-alpha-dihydrotestosterone and
CC       progesterone or corticosterone into their corresponding 5-alpha-3-
CC       oxosteroids. It plays a central role in sexual differentiation and
CC       androgen physiology. {ECO:0000250|UniProtKB:P24008}.
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:P24008};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54386;
CC         Evidence={ECO:0000250|UniProtKB:P24008};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5alpha-pregnane-3,20-dione + NADP(+) = H(+) + NADPH +
CC         progesterone; Xref=Rhea:RHEA:21952, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17026, ChEBI:CHEBI:28952, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.3.1.22;
CC         Evidence={ECO:0000250|UniProtKB:P24008};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21954;
CC         Evidence={ECO:0000250|UniProtKB:P24008};
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:P24008};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822;
CC         Evidence={ECO:0000250|UniProtKB:P24008};
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:P24008};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50817;
CC         Evidence={ECO:0000250|UniProtKB:P24008};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC       {ECO:0000305}.
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DR   EMBL; BC079863; AAH79863.1; -; mRNA.
DR   EMBL; BC094503; AAH94503.1; -; mRNA.
DR   CCDS; CCDS26624.1; -.
DR   RefSeq; NP_780492.2; NM_175283.3.
DR   AlphaFoldDB; Q68FF9; -.
DR   SMR; Q68FF9; -.
DR   STRING; 10090.ENSMUSP00000089097; -.
DR   iPTMnet; Q68FF9; -.
DR   PhosphoSitePlus; Q68FF9; -.
DR   jPOST; Q68FF9; -.
DR   MaxQB; Q68FF9; -.
DR   PaxDb; 10090-ENSMUSP00000089097; -.
DR   ProteomicsDB; 260801; -.
DR   DNASU; 78925; -.
DR   GeneID; 78925; -.
DR   KEGG; mmu:78925; -.
DR   UCSC; uc007rck.1; mouse.
DR   AGR; MGI:98400; -.
DR   CTD; 6715; -.
DR   MGI; MGI:98400; Srd5a1.
DR   eggNOG; KOG1638; Eukaryota.
DR   InParanoid; Q68FF9; -.
DR   OrthoDB; 152402at2759; -.
DR   PhylomeDB; Q68FF9; -.
DR   TreeFam; TF314668; -.
DR   Reactome; R-MMU-193048; Androgen biosynthesis.
DR   BioGRID-ORCS; 78925; 1 hit in 80 CRISPR screens.
DR   ChiTaRS; Srd5a1; mouse.
DR   PRO; PR:Q68FF9; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q68FF9; Protein.
DR   GO; GO:0070852; C:cell body fiber; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IMP:MGI.
DR   GO; GO:0047751; F:3-oxo-5alpha-steroid 4-dehydrogenase (NADP+); IEA:UniProtKB-EC.
DR   GO; GO:0033218; F:amide binding; ISO:MGI.
DR   GO; GO:0070402; F:NADPH binding; ISO:MGI.
DR   GO; GO:0006702; P:androgen biosynthetic process; IMP:MGI.
DR   GO; GO:0006710; P:androgen catabolic process; ISO:MGI.
DR   GO; GO:0008209; P:androgen metabolic process; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0042448; P:progesterone metabolic process; ISO:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR   GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006694; P:steroid biosynthetic process; ISO:MGI.
DR   Gene3D; 1.20.120.1630; -; 1.
DR   InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH.
DR   InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR   InterPro; IPR039357; SRD5A/TECR.
DR   PANTHER; PTHR10556; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE; 1.
DR   PANTHER; PTHR10556:SF57; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE 1; 1.
DR   Pfam; PF02544; Steroid_dh; 1.
DR   PIRSF; PIRSF015596; 5_alpha-SR2; 1.
DR   PROSITE; PS50244; S5A_REDUCTASE; 1.
PE   2: Evidence at transcript level;
KW   Differentiation; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW   Microsome; NADP; Oxidoreductase; Reference proteome;
KW   Sexual differentiation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..255
FT                   /note="3-oxo-5-alpha-steroid 4-dehydrogenase 1"
FT                   /id="PRO_0000317711"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        7
FT                   /note="C -> R (in Ref. 1; AAH79863)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        142
FT                   /note="V -> I (in Ref. 1; AAH94503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="E -> D (in Ref. 1; AAH94503)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   255 AA;  29344 MW;  80A5624B25D46D1A CRC64;
     MELDELCLLD ALVYLEGFLA FVAFVGLQMV GSSYGRYSSQ WSGRRVPARP AWFLQELPSM
     AWPLYECIRP AAARLGNLPN RVLLAMFLIH YVQRTLVFPV LIRGGKPTLL FTFVLAFLFC
     TLNGYLQSRY LSQFAVYAED WVTHPCFLTG FALWLVGMVI NIHSDHILRN LRKPGETGYK
     IPRGGLFEYV SSANYFGELV EWCGFALASW SLQGVVFALF TLCALFTRAR QHHQWYLEKF
     EDYPKTRKIL IPFLL
//