3-beta-hydroxy-Delta(5)-steroid dehydrogenase
     (EC 1.1.1.145)
     (3-beta-hydroxy-5-ene steroid dehydrogenase)
     (Progesterone reductase)
Steroid Delta-isomerase
     (EC 5.3.3.1)
     (Delta-5-3-ketosteroid isomerase)

Gene name

Name:

Hsd3b

From

Rattus norvegicus (Rat)

[TaxID: 10116]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.

Protein existence

2: Evidence at transcript level;

References

[1]

NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1985917 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao H.-F., Labrie C., Simard J., de Launoit Y., Trudel C., Martel C., Rheaume E., Dupont E., Luu-The V., Pelletier G., Labrie F.;
"Characterization of rat 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase cDNAs and differential tissue-specific expression of the corresponding mRNAs in steroidogenic and peripheral tissues.";
J. Biol. Chem. 266:583-593(1991).

[2]

NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1944305 [NCBI, ExPASy, EBI, Israel, Japan]
Naville D., Keeney D.S., Jenkin G., Murry B.A., Head J.R., Mason J.I.;
"Regulation of expression of male-specific rat liver microsomal 3 beta-hydroxysteroid dehydrogenase.";
Mol. Endocrinol. 5:1090-1100(1991).

Comments

FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.
CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta⁵-steroid + NAD⁺ = a 3-oxo-Delta⁵-steroid + NADH.
CATALYTIC ACTIVITY: A 3-oxo-Delta⁵-steroid = a 3-oxo-Delta⁴-steroid.
PATHWAY: Lipid metabolism; steroid biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
TISSUE SPECIFICITY: Adrenal glands, testes and ovaries.
SIMILARITY: Belongs to the 3-beta-HSD family.
CAUTION: Rat 3-beta-HSD type II may possess only one transmembrane domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M38179; AAA63475.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S63167; AAB20228.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A40378; DERTHM.
B39051; DERTH2.

RefSeq

NP_001036084.1; -.

UniGene

Rn.128814

3D structure databases

ModBase

P22072.

Organism-specific databases

RGD

1592771; Hsd3b.

Gene expression databases

ArrayExpress

P22072; -.

GermOnline

ENSRNOG00000019454; Rattus norvegicus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004769;	Molecular function: steroid delta-isomerase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR002225; 3Beta_OHSteriod_DHase/Estase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01073; 3Beta_HSD; 1.
Pfam graphical view of domain structure.

BLOCKS

P22072.

Genome annotation databases

Ensembl

ENSRNOG00000019454; Rattus norvegicus. [Contig view]

GeneID

682974; -.

KEGG

rno:682974; -.

Phylogenomic databases

HOVERGEN

P22072; -.

Other

ProtoNet

P22072.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 373`	`372`	`3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2.`	`PRO_0000087788`
`TRANSMEM`	`288 308`	`21`	`Potential.`
`CONFLICT`	`115 115`		`A -> T (in Ref. 2; AAB20228).`
`CONFLICT`	`165 165`		`A -> S (in Ref. 2; AAB20228).`
`CONFLICT`	`341 341`		`E -> V (in Ref. 2; AAB20228).`

Sequence information

Length: 373 AA [This is the length of the unprocessed precursor]

Molecular weight: 42277 Da [This is the MW of the unprocessed precursor]

CRC64: 0F922E9632DE9526 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPGWSCLVTG AGGFVGQRII RMLVQEKELQ EVRALDKVFR PETKEEFSKL QTKAKVTMLE 

        70         80         90        100        110        120 
GDILDAQYLR RACQGISVVI HTASVMDFSR VLPRQTILDV NLKGTQNLLE AGIHASVPAF 

       130        140        150        160        170        180 
IYCSTVDVAG PNSYKKTILN GREEEHHEST WSNPYPYSKK MAEKAVLAAN GSILKNGGTL 

       190        200        210        220        230        240 
HTCALRPMYI YGERGQFLSR IIIMALKNKG VLNVTGKFSI VNPVYVGNVA WAHILAARGL 

       250        260        270        280        290        300 
RDPKKSQNIQ GQFYYISDDT PHQSYDDLNC TLSKEWGLRL DSSWSLPLPL LYWLAFLLET 

       310        320        330        340        350        360 
VSFLLRPFYN YRPPFNCHLV TLSNSKFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL 

       370 
VEQHRETLDT KSQ

P22072 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools