S5A1_MACFA
ID S5A1_MACFA Reviewed; 263 AA.
AC Q28891;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 1;
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;
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 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-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:P24008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50817;
CC Evidence={ECO:0000250|UniProtKB:P24008};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimally active at alkaline 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; S77162; AAB34212.1; -; mRNA.
DR RefSeq; NP_001274227.1; NM_001287298.1.
DR AlphaFoldDB; Q28891; -.
DR SMR; Q28891; -.
DR STRING; 9541.XP_005556630.1; -.
DR Ensembl; ENSMFAT00000009778; ENSMFAP00000035539; ENSMFAG00000002749.
DR GeneID; 102126671; -.
DR CTD; 6715; -.
DR VEuPathDB; HostDB:ENSMFAG00000002749; -.
DR eggNOG; KOG1638; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR OMA; WLEWLGF; -.
DR OrthoDB; 1574389at2759; -.
DR Proteomes; UP000233100; Chromosome 6.
DR Bgee; ENSMFAG00000002749; Expressed in thymus and 8 other tissues.
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:0050213; F:progesterone 5-alpha-reductase activity; IEA:RHEA.
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 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; PTHR10556; 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..263
FT /note="3-oxo-5-alpha-steroid 4-dehydrogenase 1"
FT /id="PRO_0000213675"
FT TRANSMEM 16..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 263 AA; 30018 MW; 8830E1FB8F7365C4 CRC64;
MATAVAEELL LAEERMLAAL AYLQCAVGCA VLARNRETNL AYGRHASPSF RVRVPARAAW
VVQELPSLAL PLYQYASESA PRLRSAPNCI LLAMFLVHYG HRCLIYPFLM RGGKPMPLLA
CTMAIMFCTF NGYLQSRYLS HWAVYADDWV TDPRFLIGFG LWLAGMLINI HSDHILRNLR
KPGDTGYKIP RGGLFEYVTA ANYFGEIMEW CGYALASWSV QGAAFAFFTF CFLSGRAKEH
HRWYLQKFEE YPKFRKILIP FLF
