3BHS5_MOUSE
ID 3BHS5_MOUSE Reviewed; 373 AA.
AC Q61694; Q91X27;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=NADPH-dependent 3-keto-steroid reductase Hsd3b5 {ECO:0000305|PubMed:7491113};
DE AltName: Full=3 beta-hydroxysteroid dehydrogenase type 5;
DE AltName: Full=3 beta-hydroxysteroid dehydrogenase type V {ECO:0000303|PubMed:7491113};
DE Short=3 beta-HSD V;
DE EC=1.1.1.270 {ECO:0000269|PubMed:7491113};
DE AltName: Full=Dihydrotestosterone 3-ketoreductase {ECO:0000305|PubMed:7491113};
DE EC=1.1.1.210 {ECO:0000269|PubMed:7491113};
GN Name=Hsd3b5 {ECO:0000312|MGI:MGI:104645};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND PATHWAY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7491113; DOI=10.1210/mend.9.9.7491113;
RA Abbaszade I.G., Clarke T.R., Park C.-H.J., Payne A.H.;
RT "The mouse 3 beta-hydroxysteroid dehydrogenase multigene family includes
RT two functionally distinct groups of proteins.";
RL Mol. Endocrinol. 9:1214-1222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-350, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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:7491113}.
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:7491113};
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:7491113};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.47 uM for dihydrotestosterone {ECO:0000269|PubMed:7491113};
CC -!- PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:7491113}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Mitochondrion membrane; Single-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the male liver, starting in late
CC puberty. {ECO:0000269|PubMed:7491113}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR EMBL; L41519; AAB81242.1; -; mRNA.
DR EMBL; BC012715; AAH12715.1; -; mRNA.
DR CCDS; CCDS17666.1; -.
DR PIR; A57559; A57559.
DR RefSeq; NP_032321.2; NM_008295.2.
DR AlphaFoldDB; Q61694; -.
DR SMR; Q61694; -.
DR STRING; 10090.ENSMUSP00000041442; -.
DR iPTMnet; Q61694; -.
DR PhosphoSitePlus; Q61694; -.
DR SwissPalm; Q61694; -.
DR jPOST; Q61694; -.
DR MaxQB; Q61694; -.
DR PaxDb; Q61694; -.
DR PeptideAtlas; Q61694; -.
DR PRIDE; Q61694; -.
DR ProteomicsDB; 285686; -.
DR DNASU; 15496; -.
DR Ensembl; ENSMUST00000044094; ENSMUSP00000041442; ENSMUSG00000038092.
DR GeneID; 15496; -.
DR KEGG; mmu:15496; -.
DR UCSC; uc008qqb.1; mouse.
DR CTD; 15496; -.
DR MGI; MGI:104645; Hsd3b5.
DR VEuPathDB; HostDB:ENSMUSG00000038092; -.
DR eggNOG; KOG1430; Eukaryota.
DR GeneTree; ENSGT00940000155444; -.
DR HOGENOM; CLU_007383_6_3_1; -.
DR InParanoid; Q61694; -.
DR OMA; RTHTVEW; -.
DR OrthoDB; 930591at2759; -.
DR PhylomeDB; Q61694; -.
DR TreeFam; TF343138; -.
DR BioGRID-ORCS; 15496; 1 hit in 52 CRISPR screens.
DR PRO; PR:Q61694; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61694; protein.
DR Bgee; ENSMUSG00000038092; Expressed in left lobe of liver and 23 other tissues.
DR Genevisible; Q61694; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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: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; HDA:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; ISO:MGI.
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: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; 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:0051412; P:response to corticosterone; IBA:GO_Central.
DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central.
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 Acetylation; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Mitochondrion; NADP; Oxidoreductase; Reference proteome;
KW Steroid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..373
FT /note="NADPH-dependent 3-keto-steroid reductase Hsd3b5"
FT /id="PRO_0000087784"
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"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 89
FT /note="L -> R (in Ref. 1; AAB81242)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="R -> H (in Ref. 1; AAB81242)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="S -> R (in Ref. 1; AAB81242)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="N -> T (in Ref. 1; AAB81242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 41892 MW; EE35DE19075390A5 CRC64;
MPGWSCLVTG AGGFLGQRIV RMLVQEEELQ EIRALFRTFG RKHEEELSKL QTKAKVRVLK
GDILDAQCLK RACQGMSAVI HTAAAIDPLG AASRQTILDV NLKGTQLLLD ACVEASVPTF
IYSSSVLVAG PNSYKEIILN AHEEEHREST WPNPYPYSKR MAEKAVLATN GRLLKNGGTL
HTCALRLPFI YGEECQVTST TVKTALKNNS IIKKNATFSI ANPVYVGNAA WAHILAARSL
QDPKKSPSIQ GQFYYISDNT PHQSYDDLNY TLSKEWGLCL DSGWSLPLSL LYWLAFLLET
VSFLLRPVYN YRPPFNRLLI TVLNSVFTIS YKKAQRDLGY QPLVSWEEAK QKTSEWIGTL
VKQHRETLHK KSQ
