[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DBA/2J; TISSUE=Kidney; PubMed=8441417 [NCBI, ExPASy, EBI, Israel, Japan] Aziz N., Maxwell M.M., St Jacques B., Brenner B.M.; "Downregulation of Ke 6, a novel gene encoded within the major histocompatibility complex, in murine polycystic kidney disease."; Mol. Cell. Biol. 13:1847-1853(1993).
[2]	ERRATUM. Aziz N., Maxwell M.M., St Jacques B., Brenner B.M.; Mol. Cell. Biol. 13:6614-6614(1993).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=C57BL/6; DOI=10.1074/jbc.270.42.25213; PubMed=7559658 [NCBI, ExPASy, EBI, Israel, Japan] Maxwell M.M., Nearing J., Aziz N.; "Ke 6 gene. Sequence and organization and aberrant regulation in murine polycystic kidney disease."; J. Biol. Chem. 270:25213-25219(1995).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=129/SvJ; Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J., Lasky S., Hood L.; "Sequence of the mouse major histocomaptibility locus class II region."; Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[5]	CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. DOI=10.1074/jbc.273.35.22664; PubMed=9712896 [NCBI, ExPASy, EBI, Israel, Japan] Fomitcheva J., Baker M.E., Anderson E., Lee G.Y., Aziz N.; "Characterization of Ke 6, a new 17beta-hydroxysteroid dehydrogenase, and its expression in gonadal tissues."; J. Biol. Chem. 273:22664-22671(1998).
[6]	SUBCELLULAR LOCATION. DOI=10.1369/jhc.5A6692.2005; PubMed=15923359 [NCBI, ExPASy, EBI, Israel, Japan] Pelletier G., Luu-The V., Li S., Labrie F.; "Localization of type 8 17beta-hydroxysteroid dehydrogenase mRNA in mouse tissues as studied by in situ hybridization."; J. Histochem. Cytochem. 53:1257-1271(2005).
[7]	ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."; Mol. Cell 23:607-618(2006).

Comments

FUNCTION: Uses estradiol as its preferred substrate.
CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)⁺ = estrone + NAD(P)H.
CATALYTIC ACTIVITY: Testosterone + NAD⁺ = androst-4-ene-3,17-dione + NADH.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=0.110 µM for estradiol;
	K_M=0.422 µM for testosterone;
	K_M=0.368 µM for estrone;
	K_M=0.360 µM for dihydrotestosterone;
	V_max=0.405 nmol/min/mg enzyme for estradiol as substrate;
	V_max=0.123 nmol/min/mg enzyme for testosterone as substrate;
	V_max=0.186 nmol/min/mg enzyme for estrone as substrate;
	V_max=0.081 nmol/min/mg enzyme for dihydrotestosterone as substrate;

PATHWAY: Steroid metabolism; estrogen biosynthesis .
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name Short

Isoform ID P50171-1

This is the isoform sequence displayed in this entry.

Name Long

Isoform ID P50171-2

Features which should be applied to build the isoform sequence: VSP_006030.
TISSUE SPECIFICITY: Kidney, liver, testis, ovary, oviduct, uterus, mammary gland, vagina, prostate, clitoral gland and moderately in spleen, heart, dorsal skin, brain and lung.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) 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

U34072; AAC53573.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U34072; AAC53574.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF100956; AAC69902.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A48154; A48154.

UniGene

Mm.275452

3D structure databases

HSSP

P97852; 1GZ6. [HSSP ENTRY / PDB]

ModBase

P50171.

PTM databases

PhosphoSite

P50171; -.

2D gel databases

REPRODUCTION-2DPAGE

P50171; -.

Organism-specific databases

MGI

MGI:95911; H2-Ke6.

Gene expression databases

CleanEx

MM_H2-KE6; -.

GermOnline

ENSMUSG00000073422; Mus musculus.

Ontologies

GO:0005624;	Cellular component: membrane fraction (inferred from direct assay from MGI).
GO:0005740;	Cellular component: mitochondrial envelope (inferred from direct assay from MGI).
GO:0005886;	Cellular component: plasma membrane (inferred from direct assay from MGI).
GO:0004303;	Molecular function: estradiol 17-beta-dehydrogenase activity (inferred from direct assay from MGI).
GO:0050327;	Molecular function: testosterone 17-beta-dehydrogenase activity (inferred from direct assay from MGI).
GO:0008209;	Biological process: androgen metabolic process (inferred from direct assay from MGI).
GO:0008210;	Biological process: estrogen metabolic process (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

BLOCKS

P50171.

Genome annotation databases

Ensembl

ENSMUSG00000073422; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

P50171; -.

HOVERGEN

P50171; -.

Other

SOURCE

Hsd17b8; Mus musculus.

ProtoNet

P50171.

UniRef

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

Keywords

Acetylation; Alternative splicing; Lipid synthesis; NAD; Oxidoreductase; Steroid biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 260`	`260`	`Estradiol 17-beta-dehydrogenase 8.`	`PRO_0000054599`
`NP_BIND`	`13 38`	`26`	`NAD (By similarity).`
`ACT_SITE`	`168 168`		`Proton acceptor (By similarity).`
`BINDING`	`155 155`		`Substrate (By similarity).`
`MOD_RES`	`67 67`		`N6-acetyllysine.`
`VAR_SEQ`	`257 260`		`GLFM -> MRPSWGGGQENRTQVVMRK (in isoform Long).`	`VSP_006030`
`CONFLICT`	`16 16`		`G -> GSGVPSQ (in Ref. 3; AAC69902).`
`CONFLICT`	`17 17`		`Missing (in Ref. 1; AAC53573/AAC53574).`
`CONFLICT`	`230 230`		`E -> EG (in Ref. 1; AAC53573/AAC53574).`

Sequence information

Length: 260 AA [This is the length of the unprocessed precursor]

Molecular weight: 26645 Da [This is the MW of the unprocessed precursor]

CRC64: 19C712FCDD168B08 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASQLRLRSA LALVTGGAGS GIGRAISVRL AAEGAAVAAC DLDGAAAQDT VRLLGSPGSE 

        70         80         90        100        110        120 
DGAPRGKHAA FQADVSQGPA ARRLLEEVQA CFSRPPSVVV SCAGITRDEF LLHMSEEDWD 

       130        140        150        160        170        180 
RVIAVNLKGT FLVTQAAAQA LVSSGGRGSI INISSIIGKV GNIGQTNYAS SKAGVIGLTQ 

       190        200        210        220        230        240 
TAARELGRHG IRCNSVLPGF IATPMTQKMP EKVKDKVTAM IPLGHMGDPE DVADVVAFLA 

       250        260 
SEDSGYITGA SVEVSGGLFM

P50171 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