ID R4GBJ8_ANOCA Unreviewed; 272 AA.
AC R4GBJ8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase {ECO:0000256|PIRNR:PIRNR015596};
DE EC=1.3.1.22 {ECO:0000256|PIRNR:PIRNR015596};
GN Name=SRD5A1 {ECO:0000313|Ensembl:ENSACAP00000022678.1};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000022678.1, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000022678.1, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000022678.1,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000022678.1}
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|ARBA:ARBA00037789,
CC 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|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}.
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DR RefSeq; XP_003220081.1; XM_003220033.3.
DR AlphaFoldDB; R4GBJ8; -.
DR STRING; 28377.ENSACAP00000022678; -.
DR Ensembl; ENSACAT00000030095.2; ENSACAP00000022678.1; ENSACAG00000029192.2.
DR GeneID; 100555660; -.
DR KEGG; acs:100555660; -.
DR CTD; 6715; -.
DR eggNOG; KOG1638; Eukaryota.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_065395_1_1_1; -.
DR InParanoid; R4GBJ8; -.
DR OrthoDB; 152402at2759; -.
DR Proteomes; UP000001646; Chromosome 4.
DR Bgee; ENSACAG00000029192; Expressed in embryo and 11 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IBA:GO_Central.
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 GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
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:UP000001646};
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..43
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 164..181
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 219..244
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT DOMAIN 167..247
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 272 AA; 30516 MW; 0B4BB2F046BED867 CRC64;
MGSLLAAALS AEFWRGLSGP EEARLLASLS WGLVGGLVLM LPLSNVVGMP YGRYTSPYFG
LPIPAAAAWL LQESPSCLVP ALLVLCSDGA QLGAWPNRIL LGLFLFHYTY RSFIFPFLIR
GGKPTPFVTC FLAFIFCSYN GYLQGRSLSN YADYPSNWLT DPRFILGLIA WMSGLTINIH
SDHILRNLRK PGETGYKIPR GGMFEYVTAA NYFGEVLEWF GFALACCTIE SAAFAISTLM
ILGLRSYKHH EWYQKKFEDY PRNRKILIPY VF
//
