ID A0A1V4JWK8_PATFA Unreviewed; 268 AA.
AC A0A1V4JWK8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=3-oxo-5alpha-steroid 4-dehydrogenase (NADP(+)) {ECO:0000256|PIRNR:PIRNR015596};
DE EC=1.3.1.22 {ECO:0000256|PIRNR:PIRNR015596};
GN Name=SRD5A1 {ECO:0000313|EMBL:OPJ76465.1};
GN ORFNames=AV530_016145 {ECO:0000313|EMBL:OPJ76465.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ76465.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ76465.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ76465.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ76465.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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:0000256|ARBA:ARBA00037789}.
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|PIRNR:PIRNR015596};
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:0000256|ARBA:ARBA00036869};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50817;
CC Evidence={ECO:0000256|ARBA:ARBA00036869};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ76465.1}.
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DR EMBL; LSYS01005643; OPJ76465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JWK8; -.
DR STRING; 372326.A0A1V4JWK8; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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: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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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: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 3: Inferred from homology;
KW Differentiation {ECO:0000256|ARBA:ARBA00022928};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR015596};
KW Reference proteome {ECO:0000313|Proteomes:UP000190648};
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 25..44
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 121..139
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 160..177
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 215..238
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT DOMAIN 163..243
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 268 AA; 30459 MW; 94454554C296E1BC CRC64;
MGLSSGVCEF WWRVSGPEER RLLELFSYGL VALGATSALL LRFIRMPYGR YSSRRFGCLL
PARPAWALQE LPSLLVPLGL AACGGAVSAA WPNRLLLGCF IVHYTHRALI FPLLIRQGKP
TPFFIFVLAL LFCVYNGYLQ GRSLTNYAKY HSGWLKDPRF ITGLIGWLVG MAINIHSDHI
LRNLRKPGET GYKIPRGGMF EYVSGANFFG EILEWFGFAL ACCTIESLAF ALCTLFILCS
RAKQHHQWYL EKFEDYPKDR KIVIPFVY
//
