SIP30, characterized by a coiled-coil functional domain, plays a key role in regulating synaptic vesicle exocytosis and is implicated in neuropathic pain resulting from peripheral nerve injury. Because neuropathic pain is studied in primates (including human), domesticated animals, and rodents, we conducted a phylogenetic analysis of SIP30 in selected species of these three groups of mammals. SIP30 exhibits a high degree of sequence divergence in comparison to its protein binding partners SNAP25 and ZW10, which show broad sequence conservation. Notably, we observed an increased rate of change in the highly conserved coiled-coil domain in the SIP30 protein, specifically within primates. This observation suggests an accelerated adaptation of this functional domain in primate species.
SIP30 plays a pivotal role in regulating synaptic vesicle exocytosis and neuropathic pain.
SIP30 exhibits greater sequence divergence compared to its binding partners.
The coiled-coil domain shows an elevated rate of change only within primates, and not in domesticated animals or rodents.
This suggests an accelerated adaptation of this functional domain in primates.