Asparagine Linked Glycosylation Protein 10 (ALG10)

KCR1 coimmunoprecipitated with HERG, the pore-forming subunit of the cardiac potassium channel, I(Kr). HERG is blocked by many common therapeutic compounds and that in certain individuals, even transient exposure to some drugs evokes a life-threatening cardiac rhythm disturbance, known as acquired long QT syndrome (aLQTS). Functional analyses showed that KCR1 reduced the sensitivity of HERG to classic proarrhythmic HERG blockers in both cardiac and noncardiac cell lines.The 474-amino acid Kcr1 protein has 12 putative transmembrane domains and several putative glycosylation sites. The sequence lacks the conserved ion pore domain of K+ channels. Northern blot analysis revealed that the gene was expressed at varying levels in all rat tissues tested.