Reviewed,
UniProtKB/Swiss-Prot O54753 (H17B6_RAT)
Last modified
November 25, 2008.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Hydroxysteroid 17-beta dehydrogenase 6 EC=1.1.1.62 EC=1.1.1.63 EC=1.1.1.105 Alternative name(s): 17-beta-HSD6 Oxidative 3-alpha hydroxysteroid dehydrogenase 3-alpha->beta-hydroxysteroid epimerase Short name=3-alpha->beta-HSE | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 317 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro) By similarity. Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). |
| Catalytic activity | Estradiol-17-beta + NAD(P)(+) = estrone + NAD(P)H. Testosterone + NAD(+) = androst-4-ene-3,17-dione + NADH. Retinol + NAD(+) = retinal + NADH. |
| Enzyme regulation | Competitively inhibited by 9-cis-retinoic ancid and 13-cis-retinoic acid. |
| Subcellular location | Microsome membrane; Peripheral membrane protein; Lumenal sideBy similarity. Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal sideBy similarity. |
| Tissue specificity | Detected in prostate, liver and kidney. |
| Induction | Up-regulated by testosterone. Levels are very low in castrated male rats. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
| Biophysicochemical properties | Kinetic parameters: Vmax was measured using transfected cell lysates. KM=0.1 µM for 5-alpha-androstan-3-alpha,17-beta-diol KM=0.2 µM for androsterone KM=0.5 µM for dihydrotestosterone KM=1.1 µM for testosterone KM=0.8 µM for estradiol KM=3 µM for NAD KM=1 mM for NADP Vmax=2.5 nmol/min/mg enzyme for 5-alpha-androstan-3-alpha,17-beta-diol Vmax=0.1 nmol/min/mg enzyme for androsterone Vmax=0.5 nmol/min/mg enzyme for dihydrotestosterone Vmax=1.1 nmol/min/mg enzyme for testosterone Vmax=2.1 nmol/min/mg enzyme for estradiol |
Ontologies
Keywords | |
|---|---|
| Biological process | Lipid metabolism Steroid metabolism |
| Cellular component | Endoplasmic reticulum Membrane Microsome |
| Domain | Signal |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Glycoprotein |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW steroid metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsomeInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro estradiol 17-beta-dehydrogenase activityInferred from electronic annotation. Source: EC retinol dehydrogenase activityInferred from electronic annotation. Source: EC testosterone 17-beta-dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Potential | ||||||
| Chain | 18 – 317 | 300 | Hydroxysteroid 17-beta dehydrogenase 6 | PRO_0000303213 | |||||
Regions | |||||||||
| Nucleotide binding | 33 – 57 | 25 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 176 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 164 | 1 | Substrate Potential | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 161 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 219 | 1 | I → S in AAB88253. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate." Biswas M.G., Russell D.W. J. Biol. Chem. 272:15959-15966(1997) [PubMed: 9188497] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INDUCTION, TISSUE SPECIFICITY. Tissue: Prostate. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| U89280 mRNA. Translation: AAB88253.1. Different initiation. BC088104 mRNA. Translation: AAH88104.1. Different initiation. BC091114 mRNA. Translation: AAH91114.1. Different initiation. | |
| RefSeq | NP_775427.1. |
| UniGene | Rn.10857 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FDS based on UniProtKB P14061. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOG00000007758. Rattus norvegicus. [Contig view] |
| GeneID | 286964. |
| KEGG | rno:286964. |
Organism-specific databases | |
| RGD | 708343. Hsd17b6. |
Phylogenomic databases | |
| HOVERGEN | O54753. |
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 | |
| NextBio | 625175. |
Entry information
| Entry name | H17B6_RAT | ||||||||
| Accession | Primary (citable) accession number: O54753 Secondary accession number(s): Q5M8C8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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