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:

Hsd3b2

From

Mus musculus (Mouse)

[TaxID: 10090]

Taxonomy

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

Protein existence

2: Evidence at transcript level;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Kidney, and Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 109-373. STRAIN=BALB/c; PubMed=1924345 [NCBI, ExPASy, EBI, Israel, Japan] Bain P.A., Yoo M., Clarke T., Hammond S.H., Payne A.H.; "Multiple forms of mouse 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase and differential expression in gonads, adrenal glands, liver, and kidneys of both sexes."; Proc. Natl. Acad. Sci. U.S.A. 88:8870-8874(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: Liver and kidney.
SIMILARITY: Belongs to the 3-beta-HSD family.

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

BC026757; AAH26757.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC040397; AAH40397.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M75886; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

UniGene

Mm.196405

3D structure databases

ModBase

P26149.

PTM databases

PhosphoSite

P26149; -.

Organism-specific databases

MGI

MGI:96234; Hsd3b2.

Gene expression databases

ArrayExpress

P26149; -.

GermOnline

ENSMUSG00000063730; Mus musculus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003854;	Molecular function: 3-beta-hydroxy-delta5-steroid dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004769;	Molecular function: steroid delta-isomerase activity (inferred from electronic annotation from EC).
GO:0006700;	Biological process: C21-steroid hormone biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Genome annotation databases

Ensembl

ENSMUSG00000063730; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

P26149; -.

HOVERGEN

P26149; -.

Other

SOURCE

Hsd3b2; Mus musculus.

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_0000087781`
`TRANSMEM`	`288 308`	`21`	`Potential.`

Sequence information

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

Molecular weight: 41995 Da [This is the MW of the unprocessed precursor]

CRC64: 40EEA59227611D77 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPGWSCLVTG AKGFLGQRII QLLVQEEDLE EIRVLDKVFR PETRKEFFNL ETSNKVTVLE 

        70         80         90        100        110        120 
GDILDTQYLR RACQGISVVI HTAAIIDVTG VIPRQTILDV NLKGTQNLLE ACIQASVPAF 

       130        140        150        160        170        180 
IFSSSVDVAG PNSYKEIVLN GHEEECHEST WSDPYPYSKK MAEKAVLAAN GSMLKNGGTL 

       190        200        210        220        230        240 
QTCALRPMCI YGERSPLISN IIIMALKHKG ILRSFGKFNT ANPVYVGNVA WAHILAARGL 

       250        260        270        280        290        300 
RDPKKSPNIQ GEFYYISDDT PHQSFDDISY TLSKEWGFCL DSSWSLPVPL LYWLAFLLET 

       310        320        330        340        350        360 
VSFLLSPIYR YIPPFNRHLV TLSGSTFTFS YKKAQRDLGY EPLVSWEEAK QKTSEWIGTL 

       370 
VEQHRETLDT KSQ

P26149 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