Reviewed,
UniProtKB/Swiss-Prot P50171 (DHB8_MOUSE)
Last modified
November 25, 2008.
Version 75.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Estradiol 17-beta-dehydrogenase 8 EC=1.1.1.62 Alternative name(s): Testosterone 17-beta-dehydrogenase 8 EC=1.1.1.63 17-beta-hydroxysteroid dehydrogenase 8 Short name=17-beta-HSD 8 Protein Ke6 Short name=Ke-6 | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 260 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Uses estradiol as its preferred substrate. |
| Catalytic activity | Estradiol-17-beta + NAD(P)(+) = estrone + NAD(P)H. Testosterone + NAD(+) = androst-4-ene-3,17-dione + NADH. |
| Pathway | |
| Tissue specificity | Kidney, liver, testis, ovary, oviduct, uterus, mammary gland, vagina, prostate, clitoral gland and moderately in spleen, heart, dorsal skin, brain and lung. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
| Biophysicochemical properties | Kinetic parameters: KM=0.110 µM for estradiol KM=0.422 µM for testosterone KM=0.368 µM for estrone KM=0.360 µM for dihydrotestosterone Vmax=0.405 nmol/min/mg enzyme for estradiol as substrate Vmax=0.123 nmol/min/mg enzyme for testosterone as substrate Vmax=0.186 nmol/min/mg enzyme for estrone as substrate Vmax=0.081 nmol/min/mg enzyme for dihydrotestosterone as substrate |
Ontologies
Keywords | |
|---|---|
| Biological process | Lipid synthesis Steroid biosynthesis |
| Coding sequence diversity | Alternative splicing |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
Gene Ontology (GO) | |
| Biological process | androgen metabolic process Ref.5 Inferred from direct assay. Source: MGI estrogen metabolic process Ref.5Inferred from direct assay. Source: MGI oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW steroid biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | membrane fraction Inferred from direct assay. Source: MGI mitochondrial envelopeInferred from direct assay. Source: MGI plasma membraneInferred from direct assay. Source: MGI |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro estradiol 17-beta-dehydrogenase activity Ref.5Inferred from direct assay. Source: MGI testosterone 17-beta-dehydrogenase activity Ref.5Inferred from direct assay. Source: MGI |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Short (identifier: P50171-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform Long (identifier: P50171-2) The sequence of this isoform differs from the canonical sequence as follows: 257-260: GLFM → MRPSWGGGQENRTQVVMRK |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 260 | 260 | Estradiol 17-beta-dehydrogenase 8 | PRO_0000054599 | |||||
Regions | |||||||||
| Nucleotide binding | 13 – 38 | 26 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 168 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 155 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 67 | 1 | N6-acetyllysine | ||||||
Natural variations | |||||||||
| Alternative sequence | 257 – 260 | 4 | GLFM → MRPSWGGGQENRTQVVMRK in isoform Long. | VSP_006030 | |||||
Experimental info | |||||||||
| Sequence conflict | 16 | 1 | G → GSGVPSQ in AAC69902. Ref.3 | ||||||
| Sequence conflict | 17 | 1 | Missing in AAC53573 and AAC53574. Ref.1 | ||||||
| Sequence conflict | 230 | 1 | E → EG in AAC53573 and AAC53574. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Downregulation of Ke 6, a novel gene encoded within the major histocompatibility complex, in murine polycystic kidney disease." Aziz N., Maxwell M.M., St Jacques B., Brenner B.M. Mol. Cell. Biol. 13:1847-1853(1993) [PubMed: 8441417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DBA/2J. Tissue: Kidney. |
| [2] | Erratum Aziz N., Maxwell M.M., St Jacques B., Brenner B.M. Mol. Cell. Biol. 13:6614-6614(1993) |
| [3] | "Ke 6 gene. Sequence and organization and aberrant regulation in murine polycystic kidney disease." Maxwell M.M., Nearing J., Aziz N. J. Biol. Chem. 270:25213-25219(1995) [PubMed: 7559658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C57BL/6. |
| [4] | "Sequence of the mouse major histocomaptibility locus class II region." Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J., Lasky S., Hood L. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 129/SvJ. |
| [5] | "Characterization of Ke 6, a new 17beta-hydroxysteroid dehydrogenase, and its expression in gonadal tissues." Fomitcheva J., Baker M.E., Anderson E., Lee G.Y., Aziz N. J. Biol. Chem. 273:22664-22671(1998) [PubMed: 9712896] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. |
| [6] | "Localization of type 8 17beta-hydroxysteroid dehydrogenase mRNA in mouse tissues as studied by in situ hybridization." Pelletier G., Luu-The V., Li S., Labrie F. J. Histochem. Cytochem. 53:1257-1271(2005) [PubMed: 15923359] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [7] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." 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. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| U34072 Genomic DNA. Translation: AAC53573.1. U34072 Genomic DNA. Translation: AAC53574.1. AF100956 Genomic DNA. Translation: AAC69902.1. | |
| PIR | A48154. |
| UniGene | Mm.275452 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GZ6 based on UniProtKB P97852. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P50171. |
2-D gel databases | |
| REPRODUCTION-2DPAGE | P50171. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000073422. Mus musculus. [Contig view] |
Organism-specific databases | |
| MGI | MGI:95911. H2-Ke6. |
Phylogenomic databases | |
| HOGENOM | P50171. |
| HOVERGEN | P50171. |
Gene expression databases | |
| CleanEx | MM_H2-KE6. |
| GermOnline | ENSMUSG00000073422. Mus musculus. |
Family and domain databases | |
| InterPro | IPR002198. DHase_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DHase. IPR016040. NAD(P)-bd. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR19410. ADH_short_C2. 1 hit. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| SOURCE | Search... |
Entry information
| Entry name | DHB8_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P50171 Secondary accession number(s): Q60958, Q60959, Q9Z1W2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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