3BHS2_RAT
ID 3BHS2_RAT Reviewed; 373 AA.
AC P22072;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2;
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;
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=Hsd3b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1985917; DOI=10.1016/s0021-9258(18)52475-3;
RA Zhao H.-F., Labrie C., Simard J., de Launoit Y., Trudel C., Martel C.,
RA Rheaume E., Dupont E., Luu-The V., Pelletier G., Labrie F.;
RT "Characterization of rat 3 beta-hydroxysteroid dehydrogenase/delta 5-delta
RT 4 isomerase cDNAs and differential tissue-specific expression of the
RT corresponding mRNAs in steroidogenic and peripheral tissues.";
RL J. Biol. Chem. 266:583-593(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1944305; DOI=10.1210/mend-5-8-1090;
RA Naville D., Keeney D.S., Jenkin G., Murry B.A., Head J.R., Mason J.I.;
RT "Regulation of expression of male-specific rat liver microsomal 3 beta-
RT hydroxysteroid dehydrogenase.";
RL Mol. Endocrinol. 5:1090-1100(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 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.
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 -!- 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;
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Mitochondrion membrane; Single-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Adrenal glands, testes and ovaries.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
CC -!- CAUTION: Rat 3-beta-HSD type II may possess only one transmembrane
CC domain. {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; M38179; AAA63475.1; -; mRNA.
DR EMBL; S63167; AAB20228.1; -; mRNA.
DR PIR; A40378; DERTHM.
DR PIR; B39051; DERTH2.
DR RefSeq; NP_001036084.1; NM_001042619.1.
DR AlphaFoldDB; P22072; -.
DR SMR; P22072; -.
DR iPTMnet; P22072; -.
DR PhosphoSitePlus; P22072; -.
DR PRIDE; P22072; -.
DR Ensembl; ENSRNOT00000056172; ENSRNOP00000053018; ENSRNOG00000063905.
DR GeneID; 682974; -.
DR KEGG; rno:682974; -.
DR UCSC; RGD:1592771; rat.
DR CTD; 15494; -.
DR RGD; 1592771; Hsd3b.
DR GeneTree; ENSGT00940000155444; -.
DR InParanoid; P22072; -.
DR OrthoDB; 930591at2759; -.
DR UniPathway; UPA00062; -.
DR PRO; PR:P22072; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-EC.
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: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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion;
KW Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome;
KW Steroidogenesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..373
FT /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-
FT isomerase type 2"
FT /id="PRO_0000087788"
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 115
FT /note="A -> T (in Ref. 2; AAB20228)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="A -> S (in Ref. 2; AAB20228)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="E -> V (in Ref. 2; AAB20228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 42277 MW; 0F922E9632DE9526 CRC64;
MPGWSCLVTG AGGFVGQRII RMLVQEKELQ EVRALDKVFR PETKEEFSKL QTKAKVTMLE
GDILDAQYLR RACQGISVVI HTASVMDFSR VLPRQTILDV NLKGTQNLLE AGIHASVPAF
IYCSTVDVAG PNSYKKTILN GREEEHHEST WSNPYPYSKK MAEKAVLAAN GSILKNGGTL
HTCALRPMYI YGERGQFLSR IIIMALKNKG VLNVTGKFSI VNPVYVGNVA WAHILAARGL
RDPKKSQNIQ GQFYYISDDT PHQSYDDLNC TLSKEWGLRL DSSWSLPLPL LYWLAFLLET
VSFLLRPFYN YRPPFNCHLV TLSNSKFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL
VEQHRETLDT KSQ
