| Primary Identifier | IPR020898 | Type | Domain |
| Short Name | Synapsin_ATP-bd_dom |
| description | The synapsins are a family of neuron-specific phosphoproteins that coatsynaptic vesicles and are involved in the binding between these vesiclesand the cytoskeleton (including actin filaments). The family comprises 5homologous proteins Ia, Ib, IIa, IIb and III. Synapsins I, II, and III areencoded by 3 different genes. The a and b isoforms of synapsin I and II aresplice variants of the primary transcripts [].Synapsin I is mainly associated with regulation of neurotransmitter releasefrom presynaptic neuron terminals []. Synapsin II, as well as being involved in neurotransmitter release, has a role in the synaptogenesis and synaptic plasticity responsible for long term potentiation []. Recent studies implicate synapsin III with a developmental role in neurite elongation and synapse formation that is distinct from the functions of synapsins I and II [].Structurally, synapsins are multidomain proteins, of which 3 domains arecommon to all the mammalian forms. The N-terminal `A' domain is ~30 residueslong and contains a serine residue that serves as an acceptor site for protein kinase-mediated phosphorylation. This is followed by the `B' linkerdomain, which is ~80 residues long and is relatively poorly conserved.Domain `C' is the longest, spanning approximately 300 residues. This domainis highly conserved across all the synapsins (including those fromDrosophila) and is possessed by all splice variants. The remaining sixdomains, D-I, are not shared by all the synapsins and differ both betweenthe primary transcripts and the splice variants.This entry represent the ATP-grasp fold found in synapsins, which is responsible for Ca dependent ATP binding. |
