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Database: UniProt
Entry: A0A0N4TE55_BRUPA
LinkDB: A0A0N4TE55_BRUPA
Original site: A0A0N4TE55_BRUPA 
ID   A0A0N4TE55_BRUPA        Unreviewed;       198 AA.
AC   A0A0N4TE55;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
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};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000649301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0000649301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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   AlphaFoldDB; A0A0N4TE55; -.
DR   STRING; 6280.A0A0N4TE55; -.
DR   WBParaSite; BPAG_0000649301-mRNA-1; BPAG_0000649301-mRNA-1; BPAG_0000649301.
DR   Proteomes; UP000038020; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          93..173
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
SQ   SEQUENCE   198 AA;  22770 MW;  A5B61D9F111F2118 CRC64;
     LPSLCIPLYY LIIGIIDLPL INAFILILFC LHYINRTLIY PFLIKQGTGT PAHIFLLCLL
     FCTVNGYMQG KWHSCNNVVY NESPMNTLFC FIGTSTFIIG MIINITSDSI LRNLRKDGKS
     NYKIPYGGLF EYISGANFFG ECIEWIGYAL LARTPPAFAF AFSTLCNLAP RAYHHHRWYH
     EKFDNYPKDR KAFIPFVI
//
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