ID   S5A2_MACFA              Reviewed;         254 AA.
AC   Q28892;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 2;
DE            EC=1.3.1.22 {ECO:0000250|UniProtKB:P31213};
DE   AltName: Full=5 alpha-SR2;
DE   AltName: Full=SR type 2;
DE   AltName: Full=Steroid 5-alpha-reductase 2;
DE            Short=S5AR 2;
GN   Name=SRD5A2;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Prostate;
RX   PubMed=7734398; DOI=10.1016/0960-0760(94)00183-m;
RA   Levy M.A., Brandt M., Sheedy K.M., Holt D.A., Heaslip J.I., Trill J.J.,
RA   Ryan P.J., Morris R.A., Garrison L.M., Bergsma D.J.;
RT   "Cloning, expression and functional characterization of type 1 and type 2
RT   steroid 5 alpha-reductases from Cynomolgus monkey: comparisons with human
RT   and rat isoenzymes.";
RL   J. Steroid Biochem. Mol. Biol. 52:307-319(1995).
CC   -!- FUNCTION: Converts testosterone (T) into 5-alpha-dihydrotestosterone
CC       (DHT) and progesterone or corticosterone into their corresponding 5-
CC       alpha-3-oxosteroids. It plays a central role in sexual differentiation
CC       and androgen physiology. {ECO:0000250|UniProtKB:P31213}.
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:P31213};
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:P31213};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822;
CC         Evidence={ECO:0000250|UniProtKB:P31213};
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:P31213};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21954;
CC         Evidence={ECO:0000250|UniProtKB:P31213};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimally active at acidic pHs.;
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein.
CC       Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC       {ECO:0000305}.
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DR   EMBL; S77165; AAB34213.1; -; mRNA.
DR   RefSeq; NP_001270396.1; NM_001283467.1.
DR   AlphaFoldDB; Q28892; -.
DR   SMR; Q28892; -.
DR   STRING; 9541.ENSMFAP00000009161; -.
DR   eggNOG; KOG1638; Eukaryota.
DR   OrthoDB; 152402at2759; -.
DR   Proteomes; UP000233100; Unplaced.
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:InterPro.
DR   GO; GO:0047751; F:3-oxo-5alpha-steroid 4-dehydrogenase (NADP+); IEA:UniProtKB-EC.
DR   GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; ISS:UniProtKB.
DR   GO; GO:0006702; P:androgen biosynthetic process; IEA:UniProt.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0061370; P:testosterone biosynthetic process; ISS:UniProtKB.
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:SF43; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE 2; 1.
DR   Pfam; PF02544; Steroid_dh; 1.
DR   PIRSF; PIRSF015596; 5_alpha-SR2; 1.
DR   PROSITE; PS50244; S5A_REDUCTASE; 1.
PE   1: Evidence at protein level;
KW   Differentiation; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW   Microsome; NADP; Oxidoreductase; Reference proteome;
KW   Sexual differentiation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..254
FT                   /note="3-oxo-5-alpha-steroid 4-dehydrogenase 2"
FT                   /id="PRO_0000213677"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   254 AA;  28504 MW;  0699C2E07C77653B CRC64;
     MQVQCQQSPV LAGSATLVAL GALVLYVAKP SGYGKHTESL KPAATRLPAR AAWFLQELPS
     FAVPAGILAR QPLSLFGPPG TVLLGLFCVH YFHRTFVYSL LNRGRPYPAV LIFRGIAFCA
     GNGFLQSYYL IYCAEYPDGW YTDIRFCLGV FLFILGMGVN IHSDYILRQL RKPGEITYRI
     PKGGLFTYVS GANFLGEIIE WIGYALATWS LPALAFAFFS VCFLGLRAFH HHRFYLKMFE
     DYPKSRKALI PFIF
//