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:

Hsd3b6

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].
STRAIN=Sprague-Dawley;
TISSUE=Ovary;
PubMed=7690038 [NCBI, ExPASy, EBI, Israel, Japan]
Simard J., Couet J., Durocher F., Labrie Y., Sanchez R., Breton N., Turgeon C., Labrie F.;
"Structure and tissue-specific expression of a novel member of the rat 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD) family. The exclusive 3 beta-HSD gene expression in the skin.";
J. Biol. Chem. 268:19659-19668(1993).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
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: Skin, placenta, also detectable in ovary and adrenal gland.
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

L17138; AAA40606.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC089937; AAH89937.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A48769; A48769.

NP_058961.4; -.

3D structure databases

ModBase

Q62878.

Organism-specific databases

RGD

67377; Hsd3b6.

Gene expression databases

ArrayExpress

Q62878; -.

GermOnline

ENSRNOG00000019441; 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

Q62878.

Genome annotation databases

Ensembl

ENSRNOG00000019441; Rattus norvegicus. [Contig view]

GeneID

29632; -.

KEGG

rno:29632; -.

NMPDR

fig|10116.3.peg.16692; -.

Phylogenomic databases

HOVERGEN

Q62878; -.

Other

ProtoNet

Q62878.

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 4.`	`PRO_0000087790`
`TRANSMEM`	`288 308`	`21`	`Potential.`
`CONFLICT`	`208 208`		`S -> N (in Ref. 1; AAA40606).`
`CONFLICT`	`341 341`		`K -> E (in Ref. 1; AAA40606).`

Sequence information

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

Molecular weight: 41957 Da [This is the MW of the unprocessed precursor]

CRC64: 1B8A0FB794D05540 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPGWSCLVTG AGGFLGQRIV QLLVQEKDLK EVRVLDKVFR PETREEFFNL GTSIKVTVLE 

        70         80         90        100        110        120 
GDILDTQCLR RACQGISVVI HTAALIDVTG VNPRQTILDV NLKGTQNLLE ACVQASVPAF 

       130        140        150        160        170        180 
IYCSTVDVAG PNSYKKIILN GHEEEHHEST WSNPYPYSKK MAEKAVLAAN GSILKNGGTL 

       190        200        210        220        230        240 
HTCALRPMYI YGERSPFLSV MILAALKSKG ILNVTGKFSI ANPVYVGNVA WAHILAARGL 

       250        260        270        280        290        300 
RDPKKSQNVQ GQFYYISDDT PHQSYDDLNY TLSKEWGLHL DSSWSLPLPL LYWLAFLLEI 

       310        320        330        340        350        360 
VSFFLHPVYN YRPSFNRHLV TLSNSKFTFS YKKAQRDLGY KPLVSWEEAK QKTSEWIGTL 

       370 
VEQHRETLDT KSQ

Q62878 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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