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SYT2

Domain

The first C2 domain mediates Ca(2+)-dependent phospholipid binding.

The second C2 domain mediates interaction with Stonin 2. The second C2 domain mediates phospholipid and inositol polyphosphate binding in a calcium-independent manner.

Function

Exhibits calcium-dependent phospholipid and inositol polyphosphate binding properties (By similarity). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003).

Involvement in disease

Myasthenic syndrome, congenital, 7A, presynaptic, and distal motor neuropathy, autosomal dominant

CMS7A

A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS7A is an autosomal dominant, presynaptic disorder resembling Lambert-Eaton myasthenic syndrome. Affected individuals have a variable degree of proximal and distal limb weakness, muscle fatigue that improves with rest, mild gait difficulties, and reduced or absent deep tendon reflexes.

None

The disease is caused by variants affecting the gene represented in this entry.

Myasthenic syndrome, congenital, 7B, presynaptic, autosomal recessive

CMS7B

An autosomal recessive form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS7B is characterized by defects at the pre-synaptic neuromuscular junction and severe generalized muscle weakness apparent from birth. Decreased fetal movements may be apparent in utero. Affected infants have generalized hypotonia, head lag, and facial muscle weakness with ptosis. Some patients may have respiratory involvement.

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

Phosphorylation at Thr-199 by WNK1, changes the calcium requirement for SYT2-binding to phospholipid membranes.

Sequence Similarities

Belongs to the synaptotagmin family.

Tissue Specificity

Expressed at the neuromuscular junction (PubMed:33659639). Expressed in melanocytes (PubMed:23999003).

Cellular localization

Alternative names

Synaptotagmin-2, Synaptotagmin II, SytII, SYT2

swissprot:Q8N9I0 omim:600103 omim:600327 omim:600782 omim:600104 entrezGene:84258 entrezGene:127833 omim:185605 entrezGene:6861 entrezGene:6860 entrezGene:6857 swissprot:Q9BQG1 swissprot:O00445 swissprot:P21579 swissprot:Q9H2B2