Primary Information | |
|---|---|
| BoMiProt ID | Bomi55 |
| Protein Name | Dehydrogenase/reductase SDR family member 9 |
| Organism | Bos taurus |
| Uniprot Id | Q8HYR6 |
| Milk Fraction | MFGM |
| Ref Sequence Id | NP_777158.1 |
| Amino Acid Lenth | 319 |
| Molecular Weight | 35388 |
| Fasta Sequence | https://www.uniprot.org/uniprot/Q8HYR6.fasta |
| Gene Name | DHRS9 |
| Gene Id | 282851 |
| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
Secondry Information | |
| 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 |
| 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 |
| Significance in milk | oxidoreductase enzyme in milk |
| PTMs | No glycosylation motif |
| Linking IDs | Bomi2599 Bomi2591 |
| 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. |