Stomatin
| Stomatin | ||
|---|---|---|
| other names |
|
|
| Properties of human protein | ||
| Mass / length primary structure | 31,731 daltons / 288 amino acids (isoform 1)
13,475 daltons / 123 amino acids (isoform 2) |
|
| Isoforms | 2 | |
| Identifier | ||
| Gene names | STOM BND7, EPB72 | |
| External IDs | ||
| Orthologue | ||
| human | House mouse | |
| Entrez | 2040 | 13830 |
| Ensemble | ENSG00000148175 | ENSMUSG00000026880 |
| UniProt | P27105 | P54116 |
| Refseq (mRNA) | NM_001270526 | NM_013515 |
| Refseq (protein) | NP_001257455 | NP_038543 |
| Gene locus | Chr 9: 121.34 - 121.37 Mb | Chr 2: 35.31 - 35.34 Mb |
| PubMed search | 2040 |
13830
|
Stomatin is an integral membrane protein that is encoded by the STOM gene . It regulates the activity of ion channels , ion transport and the activity of the ASIC2 and ASIC3 channels. The protein is localized on the inner cell membrane of erythrocytes , which faces the cytoplasm . If this location is lost, hereditary stomatocytosis, a subtype of hemolytic anemia , can develop . It is activated by phosphorylation by a cAMP -dependent protein kinase .
The 3D protein structure of the mouse stomatin was elucidated in 2012 and the dimerization site was characterized.
Individual evidence
- ↑ UniProt P27105
- ↑ STOM stomatin (human) .
- ↑ Stomatin. In: Online Mendelian Inheritance in Man . (English)
- ↑ Janko Brand et al .: A stomatin dimer modulates the activity of acid-sensing ion channels . In: The Embo Journal . 31, No. 17, 29 August 2012. doi : 10.1038 / emboj.2012.203 . PMC 3433786 (free full text).