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

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=Testis; DOI=10.1016/0303-7207(91)90139-J; PubMed=1955079 [NCBI, ExPASy, EBI, Israel, Japan] Lorence M.C., Naville D., Graham-Lorence S.E., Mack S.O., Murry B.A., Trant J.M., Mason J.I.; "3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase expression in rat and characterization of the testis isoform."; Mol. Cell. Endocrinol. 80:21-31(1991).
[3]	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).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 227-358. STRAIN=Wistar; Si J.L., Li J., Xu X.Q.; Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.

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.

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

M38178; AAA63474.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC086578; AAH86578.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ515797; ABF70960.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A39051; DERTH1.

NP_001007720.3; -.

3D structure databases

ModBase

P22071.

Organism-specific databases

RGD

1308676; Hsd3b1.

Gene expression databases

ArrayExpress

P22071; -.

GermOnline

ENSRNOG00000019454; Rattus norvegicus.

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.

ProtoNet

P22071.

Genome annotation databases

Ensembl

ENSRNOG00000019454; Rattus norvegicus. [Contig view]

GeneID

360348; -.

KEGG

rno:360348; -.

Phylogenomic databases

HOVERGEN

P22071; -.

Other

NextBio

672781; -.

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_0000087787`
`TRANSMEM`	`288 308`	`21`	`Potential.`

Sequence information

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

Molecular weight: 42037 Da [This is the MW of the unprocessed precursor]

CRC64: 1BB058B5171C2F24 [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 HTAAVIDVSH VLPRQTILDV NLKGTQNILE ACVEASVPAF 

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

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

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

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

       370 
VEQHRETLDT KSQ

P22071 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