3BHS3_MESAU
ID 3BHS3_MESAU Reviewed; 373 AA.
AC O35296;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=NADPH-dependent 3-keto-steroid reductase HSD3B3 {ECO:0000305|PubMed:8547173};
DE AltName: Full=3 beta-hydroxysteroid dehydrogenase type 3 {ECO:0000303|PubMed:8547173};
DE AltName: Full=3 beta-hydroxysteroid dehydrogenase type III;
DE Short=3 beta-HSD III;
DE EC=1.1.1.270 {ECO:0000269|PubMed:8547173};
DE AltName: Full=Dihydrotestosterone 3-ketoreductase {ECO:0000305|PubMed:8547173};
DE EC=1.1.1.210 {ECO:0000269|PubMed:8547173};
GN Name=HSD3B3;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND PATHWAY.
RC TISSUE=Liver;
RX PubMed=8547173; DOI=10.1016/0960-0760(95)00197-2;
RA Rogerson F.M., Lehoux J.-G., Mason J.I.;
RT "Expression and characterization of isoforms of 3 beta-hydroxysteroid
RT dehydrogenase/delta 5-->4-isomerase in the hamster.";
RL J. Steroid Biochem. Mol. Biol. 55:481-487(1995).
CC -!- FUNCTION: Responsible for the reduction of the oxo group on the C-3 of
CC 5alpha-androstane steroids. Catalyzes the conversion of
CC dihydrotestosterone to its inactive form 5alpha-androstanediol, that
CC does not bind androgen receptor/AR. Does not function as an isomerase.
CC {ECO:0000269|PubMed:8547173}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3beta-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) +
CC NADPH; Xref=Rhea:RHEA:34787, ChEBI:CHEBI:15378, ChEBI:CHEBI:36836,
CC ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.270; Evidence={ECO:0000269|PubMed:8547173};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5alpha-androstane-3beta,17beta-diol + NADP(+) = 17beta-
CC hydroxy-5alpha-androstan-3-one + H(+) + NADPH; Xref=Rhea:RHEA:16297,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.210;
CC Evidence={ECO:0000269|PubMed:8547173};
CC -!- PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:8547173}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Mitochondrion membrane; Single-pass membrane protein.
CC -!- TISSUE SPECIFICITY: High levels in adrenal gland, kidney and male liver
CC (at protein level). Low levels in female liver (at protein level).
CC Expressed in ovaries (at protein level). {ECO:0000269|PubMed:8547173}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR EMBL; AF017636; AAB70302.1; -; mRNA.
DR RefSeq; NP_001268326.1; NM_001281397.1.
DR AlphaFoldDB; O35296; -.
DR SMR; O35296; -.
DR STRING; 10036.XP_005084274.1; -.
DR GeneID; 101837099; -.
DR eggNOG; KOG1430; Eukaryota.
DR OrthoDB; 930591at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR GO; GO:0000253; F:3-keto sterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0047024; F:5alpha-androstane-3beta,17beta-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102176; F:cycloeucalenone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid metabolism; Membrane; Mitochondrion; NADP;
KW Oxidoreductase; Reference proteome; Steroid metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..373
FT /note="NADPH-dependent 3-keto-steroid reductase HSD3B3"
FT /id="PRO_0000087779"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 159
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
SQ SEQUENCE 373 AA; 41806 MW; B588DDC2D3F15DF1 CRC64;
MPAWSCLVTG AGGFLGQRII RMLAQEKELQ EVRTLFRSFT PKHREELSKL QTKTKVTVLE
GDILDAQCLR RACQGISVVI HTAAAIDVFG AIPRQTVIDI NLKGTQHLLD ACIGARVPVF
IYSSSVAVAG PNSYKVIIQN GSEEENHEST WSDPYAYSKK MAEKAVLAAN GSTLKDGGTL
HTCALRLPFI YGEKSKFISD TMDRALKNNG LINGFSRFSV ISSVYVNNAA WAHVLAARGL
QDPKKSPNIQ GQFYYISDDT PHQSYDDLCY TLSKDWGLRP DSSWKPPVAL LYWFGFLLET
VSFLLRPVYN YQPPFNRHLV TLLNSVFTFS YKKAQRDLGY EPLVSWEEAR EKTSEWIGSL
VEQHKGTLNI KAQ
