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:	Hsd3b1
	Synonyms:	Hsd3b

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 [MRNA]. STRAIN=CD-1; 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).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=C57BL/6J; TISSUE=Egg; 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).

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: Steroidogenic tissues (includes testes, ovaries and adrenal glands).
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

M58567; AAA37860.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC052659; AAH52659.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I49762; I49762.

UniGene

Mm.140811

3D structure databases

ModBase

P24815.

Organism-specific databases

MGI

MGI:96233; Hsd3b1.

Gene expression databases

ArrayExpress

P24815; -.

GermOnline

ENSMUSG00000027871; Mus musculus.

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

P24815.

Genome annotation databases

Ensembl

ENSMUSG00000027871; Mus musculus. [Contig view]

Phylogenomic databases

HOVERGEN

P24815; -.

Other

SOURCE

Hsd3b1; Mus musculus.

ProtoNet

P24815.

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 1.`	`PRO_0000087780`
`TRANSMEM`	`288 308`	`21`	`Potential.`
`CONFLICT`	`128 128`		`V -> A (in Ref. 2; AAH52659).`
`CONFLICT`	`319 319`		`L -> S (in Ref. 2; AAH52659).`

Sequence information

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

Molecular weight: 42062 Da [This is the MW of the unprocessed precursor]

CRC64: 395F9D786C7BA010 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGWSCLVTG AGGFVGQRII KMLVQEKELQ EVRALDKVFR PETKEEFSKL QTKTKVTVLE 

        70         80         90        100        110        120 
GDILDAQCLR RACQGISVVI HTAAVIDVTG VIPRQTILDV NLKGTQNLLE ACVQASVPAF 

       130        140        150        160        170        180 
IFCSSVDVAG PNSYKKIVLN GHEEQNHEST WSDPYPYSKK MAEKAVLAAN GSMLKNGGTL 

       190        200        210        220        230        240 
NTCALRPMYI YGERSPFIFN AIIRALKNKG ILCVTGKFSI ANPVYVENVA WAHILAARGL 

       250        260        270        280        290        300 
RDPKKSTSIQ GQFYYISDDT PHQSYDDLNY TLSKEWGLRP NASWSLPLPL LYWLAFLLET 

       310        320        330        340        350        360 
VSFLLRPVYR YRPLFNRHLI TLSNSTFTFS YKKAQRDLGY EPLVNWEEAK QKTSEWIGTI 

       370 
VEQHREILDT KCQ

P24815 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