ID   3BHS3_MOUSE             Reviewed;         373 AA.
AC   P26150;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-NOV-2008, entry version 63.
DE   RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 3;
DE   AltName: Full=3-beta-HSD III;
DE   Includes:
DE     RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase;
DE              EC=1.1.1.145;
DE     AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase;
DE     AltName: Full=Progesterone reductase;
DE   Includes:
DE     RecName: Full=Steroid Delta-isomerase;
DE              EC=5.3.3.1;
DE     AltName: Full=Delta-5-3-ketosteroid isomerase;
GN   Name=Hsd3b3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=92020952; PubMed=1924345;
RA   Bain P.A., Yoo M., Clarke T., Hammond S.H., Payne A.H.;
RT   "Multiple forms of mouse 3 beta-hydroxysteroid dehydrogenase/delta 5-
RT   delta 4 isomerase and differential expression in gonads, adrenal
RT   glands, liver, and kidneys of both sexes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8870-8874(1991).
CC   -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the
CC       oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and
CC       the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic
CC       system plays a crucial role in the biosynthesis of all classes of
CC       hormonal steroids.
CC   -!- CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a
CC       3-oxo-Delta(5)-steroid + NADH.
CC   -!- CATALYTIC ACTIVITY: A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-
CC       steroid.
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein. Mitochondrion membrane; Single-pass membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Liver and kidney. Greater expression in liver.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family.
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DR   EMBL; M77015; -; NOT_ANNOTATED_CDS; mRNA.
DR   UniGene; Mm.158717; -.
DR   Ensembl; ENSMUSG00000062410; Mus musculus.
DR   MGI; MGI:96235; Hsd3b3.
DR   HOGENOM; P26150; -.
DR   HOVERGEN; P26150; -.
DR   ArrayExpress; P26150; -.
DR   GermOnline; ENSMUSG00000062410; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase...; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; IEA:EC.
DR   GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DHase/Estase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01073; 3Beta_HSD; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion;
KW   Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis;
KW   Transmembrane.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    373       3 beta-hydroxysteroid dehydrogenase/Delta
FT                                5-->4-isomerase type 3.
FT                                /FTId=PRO_0000087782.
FT   TRANSMEM    288    308       Potential.
SQ   SEQUENCE   373 AA;  42031 MW;  6F320FF1707974A6 CRC64;
     MPGWSCLVTG AGGFLGQRII QLLVQEKDLE EIRVLDKVFK PETREQFFNL GTSIKVTVLE
     GDILDTQYLR RACQGISVVI HTAAIIDVTG VIPRQTILDV NLKGTQNLLE ACIQASVPAF
     IFSSSVDVAG PNSYKDIVLN GHEDEHREST WSDPYPYSKK MAEKAVLAAN GSMLKNGGTL
     QTCALRPMCI YGERSQFLSN TIIKALKNKF ILRGGGKFST ANPVYVGNVA WAHILAARGL
     RNPKKSPNIQ GEFYYISDDT PHQSYDDLNY TLSKEWGFCL NSRWYLPVPI LYWLAFLLET
     VSFLLSPIYR YIPPFNRHLV TLTASTFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL
     VEQHRETLDT KSQ
//