ID A0A1S3PHK0_SALSA Unreviewed; 219 AA.
AC A0A1S3PHK0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 2 {ECO:0000256|ARBA:ARBA00039430};
DE AltName: Full=5 alpha-SR2 {ECO:0000256|ARBA:ARBA00042576};
DE AltName: Full=SR type 2 {ECO:0000256|ARBA:ARBA00041663};
DE AltName: Full=Steroid 5-alpha-reductase 2 {ECO:0000256|ARBA:ARBA00042580};
GN Name=s5a2 {ECO:0000313|RefSeq:XP_014027097.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014027097.1};
RN [1] {ECO:0000313|RefSeq:XP_014027097.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014027097.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC {ECO:0000256|ARBA:ARBA00007742}.
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DR RefSeq; XP_014027097.1; XM_014171622.1.
DR AlphaFoldDB; A0A1S3PHK0; -.
DR OrthoDB; 152402at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.120.1630; -; 1.
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 PROSITE; PS50244; S5A_REDUCTASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 127..194
FT /note="Steroid 5-alpha reductase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50244"
SQ SEQUENCE 219 AA; 25408 MW; F2B1D8F152099F8B CRC64;
MECKENVIHY LSWGFIVSGV AYLFWQTRFQ TPYGRYVTSD GTPGRTCPAK LAWFLQELPS
FLVPMLLLLS TDTQPSLGKD LLLWTFCLHY FQRTFIYSLL TKGRPSPLYI VFSAVVFCSV
NGFLQGHYML HCATYDDAWQ TDIRLYTGGM FEYVSGANFF GEILEWCGYA LATWSLPTFS
FALFTMCSIG PRAFHHHRYY QEKFEDYPQS RKAVIPFIL
//