ID H3DGV9_TETNG Unreviewed; 261 AA.
AC H3DGV9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000019753.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000019753.1}
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PIRNR:PIRNR015596}.
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DR AlphaFoldDB; H3DGV9; -.
DR STRING; 99883.ENSTNIP00000019753; -.
DR Ensembl; ENSTNIT00000019983.1; ENSTNIP00000019753.1; ENSTNIG00000016646.1.
DR GeneTree; ENSGT00950000182886; -.
DR HOGENOM; CLU_065395_1_1_1; -.
DR InParanoid; H3DGV9; -.
DR OMA; FREREFK; -.
DR TreeFam; TF314668; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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 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:UP000007303};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 110..133
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT TRANSMEM 204..227
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR015596"
FT DOMAIN 152..232
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 261 AA; 29902 MW; 9EDDB8C803C6D7BD CRC64;
ASQPEMHCHR TLVDALSLGF VLAGFAHLLH HRKTQLSYGR HMRPTPLLRT VPAPLAWFLQ
EMPAFLIPLL LTLTPHQASG TGKRLLLGTF VTHYFQRTFI YSFLTRGRPF PLNVMVAGAF
FCSLSGFLQG HYLLHCAQYD QHWTAGFRCR TGLLLFYTGM AINIHSDSVL RNLREPGEVV
YRIPTGGFFR YVSGANFFGE ITEWMGYAVA TWSLPALSFA LFSLCFIGPR ALHHHRELEI
FREREFKRDP ECRKELNPVV F
//
