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S5A1_BOVIN
ID   S5A1_BOVIN              Reviewed;         257 AA.
AC   A5PJS2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; BC142219; AAI42220.1; -; mRNA.
DR   RefSeq; NP_001092607.1; NM_001099137.1.
DR   RefSeq; XP_015314613.1; XM_015459127.1.
DR   AlphaFoldDB; A5PJS2; -.
DR   SMR; A5PJS2; -.
DR   STRING; 9913.ENSBTAP00000020570; -.
DR   PaxDb; A5PJS2; -.
DR   PRIDE; A5PJS2; -.
DR   Ensembl; ENSBTAT00000020570; ENSBTAP00000020570; ENSBTAG00000015478.
DR   GeneID; 614612; -.
DR   KEGG; bta:614612; -.
DR   CTD; 6715; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015478; -.
DR   VGNC; VGNC:35271; SRD5A1.
DR   eggNOG; KOG1638; Eukaryota.
DR   GeneTree; ENSGT00950000182886; -.
DR   HOGENOM; CLU_065395_1_1_1; -.
DR   InParanoid; A5PJS2; -.
DR   OMA; WLEWLGF; -.
DR   OrthoDB; 1574389at2759; -.
DR   TreeFam; TF314668; -.
DR   Reactome; R-BTA-193048; Androgen biosynthesis.
DR   Proteomes; UP000009136; Chromosome 20.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
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   GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
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   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..257
FT                   /note="3-oxo-5-alpha-steroid 4-dehydrogenase 1"
FT                   /id="PRO_0000317710"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   257 AA;  29186 MW;  2A49937DFB45FFB0 CRC64;
     MELAERFLLD ALAYLECALG VVCYVLLKLV GSPYGRYASS GSAFGLPARA AWTVQELPSL
     ALPLLACAGA GAPAERLNRW PNCILLAMFL VHYAQRSLVF PFLIRGGKPM PLYAFLLAFI
     FCTYNGYLQS RYLSQYAVYA DDWLSDPRFL TGSALWLIGM LINIHSDHVL RNLRKPGETG
     YKIPRGGLFE YISAANYFGE VVEWCGYALA SWSIQGWAFA VFTFCVLFTR AQQHHKWYHE
     KFEDYPKFRK IMIPFLV
 
 
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