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Database: UniProt
Entry: A0A3Q1BRT4_AMPOC
LinkDB: A0A3Q1BRT4_AMPOC
Original site: A0A3Q1BRT4_AMPOC 
ID   A0A3Q1BRT4_AMPOC        Unreviewed;       255 AA.
AC   A0A3Q1BRT4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase {ECO:0000256|PIRNR:PIRNR015596};
DE            EC=1.3.1.22 {ECO:0000256|PIRNR:PIRNR015596};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000017085.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000017085.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|PIRNR:PIRNR015596}.
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=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:0000256|ARBA:ARBA00034445};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21954;
CC         Evidence={ECO:0000256|ARBA:ARBA00034445};
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|ARBA:ARBA00001683,
CC         ECO:0000256|PIRNR:PIRNR015596};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Microsome
CC       membrane {ECO:0000256|ARBA:ARBA00004154}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004154}.
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC       {ECO:0000256|ARBA:ARBA00007742, ECO:0000256|PIRNR:PIRNR015596}.
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DR   AlphaFoldDB; A0A3Q1BRT4; -.
DR   STRING; 80972.ENSAOCP00000017085; -.
DR   Ensembl; ENSAOCT00000026256.1; ENSAOCP00000017085.1; ENSAOCG00000022107.1.
DR   GeneTree; ENSGT00950000182886; -.
DR   OMA; HRDYQQR; -.
DR   OrthoDB; 152402at2759; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0016020; C: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-EC.
DR   GO; GO:0006702; P:androgen biosynthetic process; IEA:UniProt.
DR   GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Differentiation {ECO:0000256|ARBA:ARBA00022928};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR015596};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Sexual differentiation {ECO:0000256|ARBA:ARBA00022928};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|PIRNR:PIRNR015596};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|PIRNR:PIRNR015596}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT   TRANSMEM        108..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT   TRANSMEM        147..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT   TRANSMEM        199..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT   DOMAIN          150..230
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
SQ   SEQUENCE   255 AA;  29237 MW;  C66E1D8B14C45D79 CRC64;
     MECRDAAVSG LSWTLIVVGG LYLWRQTRTG ARYGRYVEAN SRCCPARLAW FLQEFPAFLL
     PLLLLLLPGQ RDAERRDDGR RLLLLGSFML HYFHRSFIYA FLTRGRPVPL FIVLCSAIFC
     SLNGFLQAHY LLHCRRLEDT WLTDAHLAAG LLVFVVGMTI NIHSDHILRS LRKPGETVYR
     IPHGGLFELV SGANFFGEIV QWCGFAVAAG SLPAFAFFFF TVCSIGPRAY QHHRDYQRRF
     EDYPRCRKAL VPFIL
//
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