3BHS4_RAT
ID 3BHS4_RAT Reviewed; 373 AA.
AC Q62878; Q5FVK0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 4.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4;
DE AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type IV;
DE Short=3-beta-HSD IV;
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=Hsd3b6;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=7690038; DOI=10.1016/s0021-9258(19)36567-6;
RA Simard J., Couet J., Durocher F., Labrie Y., Sanchez R., Breton N.,
RA Turgeon C., Labrie F.;
RT "Structure and tissue-specific expression of a novel member of the rat 3
RT beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD)
RT family. The exclusive 3 beta-HSD gene expression in the skin.";
RL J. Biol. Chem. 268:19659-19668(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
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: Skin, placenta, also detectable in ovary and
CC adrenal gland.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR EMBL; L17138; AAA40606.1; -; mRNA.
DR EMBL; BC089937; AAH89937.1; -; mRNA.
DR PIR; A48769; A48769.
DR RefSeq; NP_058961.4; NM_017265.4.
DR RefSeq; XP_017446814.1; XM_017591325.1.
DR AlphaFoldDB; Q62878; -.
DR SMR; Q62878; -.
DR STRING; 10116.ENSRNOP00000026306; -.
DR PaxDb; Q62878; -.
DR Ensembl; ENSRNOT00000026306; ENSRNOP00000026306; ENSRNOG00000019441.
DR GeneID; 29632; -.
DR KEGG; rno:29632; -.
DR UCSC; RGD:67377; rat.
DR CTD; 3284; -.
DR RGD; 67377; Hsd3b6.
DR eggNOG; KOG1430; Eukaryota.
DR GeneTree; ENSGT00940000155444; -.
DR HOGENOM; CLU_007383_6_3_1; -.
DR InParanoid; Q62878; -.
DR OMA; ERDCLEN; -.
DR OrthoDB; 930591at2759; -.
DR PhylomeDB; Q62878; -.
DR TreeFam; TF343138; -.
DR Reactome; R-RNO-193048; Androgen biosynthesis.
DR Reactome; R-RNO-193993; Mineralocorticoid biosynthesis.
DR Reactome; R-RNO-194002; Glucocorticoid biosynthesis.
DR UniPathway; UPA00062; -.
DR PRO; PR:Q62878; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019441; Expressed in ovary and 1 other tissue.
DR Genevisible; Q62878; RN.
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; IDA:RGD.
DR GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; TAS:RGD.
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; IDA:RGD.
DR GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; TAS:RGD.
DR GO; GO:0006702; P:androgen biosynthetic process; IDA:RGD.
DR GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IDA:RGD.
DR GO; GO:0008207; P:C21-steroid hormone metabolic process; IBA:GO_Central.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0033327; P:Leydig cell differentiation; IEP:RGD.
DR GO; GO:0034757; P:negative regulation of iron ion transport; IMP:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0006694; P:steroid biosynthetic process; ISO:RGD.
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 Acetylation; 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 4"
FT /id="PRO_0000087790"
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 MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61694"
FT CONFLICT 208
FT /note="S -> N (in Ref. 1; AAA40606)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="K -> E (in Ref. 1; AAA40606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 41957 MW; 1B8A0FB794D05540 CRC64;
MPGWSCLVTG AGGFLGQRIV QLLVQEKDLK EVRVLDKVFR PETREEFFNL GTSIKVTVLE
GDILDTQCLR RACQGISVVI HTAALIDVTG VNPRQTILDV NLKGTQNLLE ACVQASVPAF
IYCSTVDVAG PNSYKKIILN GHEEEHHEST WSNPYPYSKK MAEKAVLAAN GSILKNGGTL
HTCALRPMYI YGERSPFLSV MILAALKSKG ILNVTGKFSI ANPVYVGNVA WAHILAARGL
RDPKKSQNVQ GQFYYISDDT PHQSYDDLNY TLSKEWGLHL DSSWSLPLPL LYWLAFLLEI
VSFFLHPVYN YRPSFNRHLV TLSNSKFTFS YKKAQRDLGY KPLVSWEEAK QKTSEWIGTL
VEQHRETLDT KSQ
