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| Domain hiding | Altered binding specificity | Motif hiding | Composite binding site formation |
| Uncategorised | Rheostatic | Allostery | Avidity-sensing |
| Physicochemical compatibility | Pre-translational | Competition |
| Protein transport protein Sec61 subunit alpha isoform 1 (Canis) | Voltage-dependent L-type calcium channel subunit alpha-1D (Rattus) |
| Motif | Start | End | Switch Type | Switch Subtype | Switch Description | Information |
Protein transport protein Sec61 subunit alpha isoform 1 - SEC61A1 - Canis familiaris | |||||||
| LIG_IQ | 13 | 31 | Binary | Allostery | Binding of calcium(2+) to Calmodulin (Calm1) exposes a binding site on Calmodulin (Calm1) for the Calmodulin-binding IQ motif of Protein transport protein Sec61 subunit alpha isoform 1 (SEC61A1), an interaction that results in closure of the protein-conducting channel located in the ER. | ||
| LIG_IQ | 13 | 31 | Binary | Allostery | Binding of calcium(2+) to Calmodulin (Calm1) exposes a binding site on Calmodulin (Calm1) for the Calmodulin-binding IQ motif of Protein transport protein Sec61 subunit alpha isoform 1 (SEC61A1), an interaction that results in closure of the protein-conducting channel located in the ER. | ||
Voltage-dependent L-type calcium channel subunit alpha-1D - Cacna1d - Rattus norvegicus | |||||||
| LIG_IQ | 1650 | 1669 | Binary | Pre‑translational | Alternative splicing removes the IQ motif of Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d) abrogating binding to Calmodulin (Calm1). CaV1.3IQdelta (IQ-deleted Isoform CACN4B of Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d)) channels exhibit a lack of calcium-dependent inactivation. CaV1.3IQdelta channel immunoreactivity was preferentially localised to cochlear outer hair cells (OHCs), whereas that of CaV1.3IQfull channels (IQ-possessing Isoform CACN4A of Voltage-dependent L-type calcium channel subunit alpha-1D (Cacna1d)) labelled inner hair cells (IHCs). | ||