ID 3BHS2_MOUSE Reviewed; 373 AA. AC P26149; B1ARN7; Q8R0J6; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 4. DT 27-MAR-2024, entry version 184. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2 {ECO:0000305}; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II; DE Short=3-beta-HSD II; DE Includes: DE RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase; DE EC=1.1.1.145 {ECO:0000250|UniProtKB:P26439}; 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 {ECO:0000250|UniProtKB:P26439}; DE AltName: Full=Delta-5-3-ketosteroid isomerase; GN Name=Hsd3b2 {ECO:0000312|MGI:MGI:96234}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-373. RC STRAIN=BALB/cJ; RX PubMed=1924345; DOI=10.1073/pnas.88.20.8870; 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-delta RT 4 isomerase and differential expression in gonads, adrenal glands, liver, RT and kidneys of both sexes."; RL Proc. Natl. Acad. Sci. U.S.A. 88:8870-8874(1991). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, and Liver; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the CC oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the CC oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system CC plays a crucial role in the biosynthesis of all classes of hormonal CC steroids. {ECO:0000250|UniProtKB:P26439}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)- CC steroid + H(+) + NADH; Xref=Rhea:RHEA:24076, ChEBI:CHEBI:1722, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47907, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.1.1.145; CC Evidence={ECO:0000250|UniProtKB:P26439}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid; CC Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909; CC EC=5.3.3.1; Evidence={ECO:0000250|UniProtKB:P26439}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + pregnenolone = H(+) + NADH + pregn-5-ene-3,20-dione; CC Xref=Rhea:RHEA:43924, ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:63837; CC Evidence={ECO:0000250|UniProtKB:P26439}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43925; CC Evidence={ECO:0000250|UniProtKB:P26439}; CC -!- CATALYTIC ACTIVITY: CC Reaction=pregn-5-ene-3,20-dione = progesterone; Xref=Rhea:RHEA:43928, CC ChEBI:CHEBI:17026, ChEBI:CHEBI:63837; CC Evidence={ECO:0000250|UniProtKB:P26439}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43929; CC Evidence={ECO:0000250|UniProtKB:P26439}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3beta-hydroxyandrost-5-en-17-one + NAD(+) = androst-5- CC ene-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:43932, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28689, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:83865; EC=1.1.1.145; CC Evidence={ECO:0000250|UniProtKB:P26439}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43933; CC Evidence={ECO:0000250|UniProtKB:P26439}; CC -!- CATALYTIC ACTIVITY: CC Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione; CC Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865; CC Evidence={ECO:0000250|UniProtKB:P26439}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937; CC Evidence={ECO:0000250|UniProtKB:P26439}; CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC {ECO:0000250|UniProtKB:P26439}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:P26439}; Single-pass membrane protein CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P26439}; CC Single-pass membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Liver and kidney. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL606755; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC026757; AAH26757.1; -; mRNA. DR EMBL; BC040397; AAH40397.1; -; mRNA. DR EMBL; M75886; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS17667.1; -. DR RefSeq; NP_694873.2; NM_153193.3. DR RefSeq; XP_006501101.1; XM_006501038.3. DR AlphaFoldDB; P26149; -. DR BioGRID; 200438; 1. DR STRING; 10090.ENSMUSP00000102636; -. DR iPTMnet; P26149; -. DR PhosphoSitePlus; P26149; -. DR jPOST; P26149; -. DR MaxQB; P26149; -. DR PaxDb; 10090-ENSMUSP00000102636; -. DR PeptideAtlas; P26149; -. DR ProteomicsDB; 296417; -. DR DNASU; 15493; -. DR Ensembl; ENSMUST00000107021.8; ENSMUSP00000102635.2; ENSMUSG00000063730.14. DR Ensembl; ENSMUST00000107022.8; ENSMUSP00000102636.2; ENSMUSG00000063730.14. DR Ensembl; ENSMUST00000177651.2; ENSMUSP00000136533.2; ENSMUSG00000063730.14. DR GeneID; 15493; -. DR KEGG; mmu:15493; -. DR UCSC; uc008qqc.2; mouse. DR AGR; MGI:96234; -. DR CTD; 3284; -. DR MGI; MGI:96234; Hsd3b2. DR VEuPathDB; HostDB:ENSMUSG00000063730; -. DR eggNOG; KOG1430; Eukaryota. DR GeneTree; ENSGT00940000155444; -. DR HOGENOM; CLU_007383_6_3_1; -. DR InParanoid; P26149; -. DR OMA; DTFYTCA; -. DR OrthoDB; 3675908at2759; -. DR PhylomeDB; P26149; -. DR TreeFam; TF343138; -. DR Reactome; R-MMU-193048; Androgen biosynthesis. DR Reactome; R-MMU-193993; Mineralocorticoid biosynthesis. DR Reactome; R-MMU-194002; Glucocorticoid biosynthesis. DR UniPathway; UPA00062; -. DR BioGRID-ORCS; 15493; 1 hit in 79 CRISPR screens. DR ChiTaRS; Hsd3b2; mouse. DR PRO; PR:P26149; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P26149; Protein. DR Bgee; ENSMUSG00000063730; Expressed in right kidney and 22 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045171; C:intercellular bridge; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI. DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central. DR GO; GO:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB. DR GO; GO:0006702; P:androgen biosynthetic process; ISS:UniProtKB. DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; ISO:MGI. DR GO; GO:0008207; P:C21-steroid hormone metabolic process; IBA:GO_Central. DR GO; GO:0021766; P:hippocampus development; IBA:GO_Central. DR GO; GO:0034757; P:negative regulation of iron ion transport; ISO:MGI. DR GO; GO:0051412; P:response to corticosterone; IBA:GO_Central. DR GO; GO:0006694; P:steroid biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR43245; BIFUNCTIONAL POLYMYXIN RESISTANCE PROTEIN ARNA; 1. DR PANTHER; PTHR43245:SF51; SHORT CHAIN DEHYDROGENASE_REDUCTASE FAMILY 42E, MEMBER 2; 1. DR Pfam; PF01073; 3Beta_HSD; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR Genevisible; P26149; MM. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Isomerase; Lipid metabolism; Membrane; KW Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; KW Reference proteome; Steroidogenesis; Transmembrane; Transmembrane helix. FT CHAIN 1..373 FT /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4- FT isomerase type 2" FT /id="PRO_0000087781" FT TRANSMEM 288..308 FT /note="Helical" FT /evidence="ECO:0000255" FT ACT_SITE 155 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 159 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT CONFLICT 12 FT /note="G -> K (in Ref. 2; AAH26757/AAH40397)" FT /evidence="ECO:0000305" FT CONFLICT 54 FT /note="I -> N (in Ref. 2; AAH26757/AAH40397)" FT /evidence="ECO:0000305" SQ SEQUENCE 373 AA; 41923 MW; 2500AF16F38C081B CRC64; MPGWSCLVTG AGGFLGQRII QLLVQEEDLE EIRVLDKVFR PETRKEFFNL ETSIKVTVLE GDILDTQYLR RACQGISVVI HTAAIIDVTG VIPRQTILDV NLKGTQNLLE ACIQASVPAF IFSSSVDVAG PNSYKEIVLN GHEEECHEST WSDPYPYSKK MAEKAVLAAN GSMLKNGGTL QTCALRPMCI YGERSPLISN IIIMALKHKG ILRSFGKFNT ANPVYVGNVA WAHILAARGL RDPKKSPNIQ GEFYYISDDT PHQSFDDISY TLSKEWGFCL DSSWSLPVPL LYWLAFLLET VSFLLSPIYR YIPPFNRHLV TLSGSTFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL VEQHRETLDT KSQ //