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Cerebellin-3 precursor (CBLN3) is a member of the precerebellin protein family, which includes structurally related secreted proteins with a C-terminal C1q signature domain, allowing trimeric complex assembly. CBLN3 is co-expressed with CBLN1 in the cerebellum (mostly in granule cells) and has weak homomeric but strong heteromeric binding affinity with CBLN1, suggesting it forms secreted heteromeric protein complexes, potentially influencing synaptic integrity and organization in the CNS[1][2][3]. Although it shares sequence similarity with conventional neuropeptide precursors, CBLN3 is not a classic neuroactive peptide and does not possess a collagen motif. No drugs or approved molecular therapies target CBLN3 directly, and it is primarily considered relevant for fundamental neuroscience rather than clinical pharmacology at present[1][3][5].
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