Primary Information |
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| BoMiProt ID | Bomi55 |
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| Protein Name | Dehydrogenase/reductase SDR family member 9 |
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| Organism | Bos taurus |
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| Uniprot Id | Q8HYR6 |
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| Milk Fraction | MFGM |
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| Ref Sequence Id | NP_777158.1 |
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| Aminoacid Length | 319 |
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| Molecular Weight | 35388 |
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| Fasta Sequence | https://www.uniprot.org/uniprot/Q8HYR6.fasta |
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| Gene Name | DHRS9 |
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| Gene Id | 282851 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Protein Function | member of the short-chain dehydrogenase/reductase (SDR) superfamily; play an important role in various (patho)biochemical pathways including intermediary
metabolism and biotransformation of xenobiotics. 3 alpha-Hydroxysteroid dehydrogenase (3 alpha HSD) is one of the main enzymes involved in the metabolism of the active androgen, dihydrotestosterone (DHT). |
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| Biochemical Properties | integral protein of the endoplasmic reticulum,facing towards the lumen with a reducing activity toward several substrates bearing carbonyl groups, such as steroid hormones,xenobiotics and model substrates prerferably NADPH as the cofactor; mostly three transmembrane segments; hydrophobic middle and C-term predicted transmembrane segments might be part of the homodimer formation/interaction sites. 3 alpha HSD catalyzes the reversible reduction of DHT to 5 alpha-androstane-3 alpha, 17 beta-diol (3 alpha DIOL). The equilibrium of 3 alpha HSD reductive and oxidative activity is an important factor in the regulation of intracellular levels of DHT. |
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| Significance in milk | oxidoreductase enzyme in milk |
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| PTMs | No glycosylation motif |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Linking IDs | |
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| Bibliography | 1. Hirokawa, T., Boon-Chieng, S., & Mitaku, S. (1998). SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics (Oxford, England), 14(4), 378–379. https://doi.org/10.1093/bioinformatics/14.4.378.
2. Stambergova, H., Skarydova, L., Dunford, J. E., & Wsol, V. (2014). Biochemical properties of human dehydrogenase/reductase (SDR family) member 7. Chemico-Biological Interactions, 207, 52–57. https://doi.org/10.1016/j.cbi.2013.11.003. 3.Pirog EC, Collins DC. 3 Alpha-hydroxysteroid dehydrogenase activity in rat liver and skin. Steroids. 1994 Apr;59(4):259-64. doi: 10.1016/0039-128x(94)90110-4. PMID: 8079380. |
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