Summary: Synapsin N-terminal
Synapsin N-terminal Provide feedback
This highly conserved domain of synapsin proteins has a serine at position 9 or 10 which is a phosphorylation site. The domain appears to be the part of the molecule that binds to calmodulin .
Heierhorst J, Mitchelhill KI, Mann RJ, Tiganis T, Czernik AJ, Greengard P, Kemp BE; , Biochem J. 1999;344:577-583.: Synapsins as major neuronal Ca2+/S100A1-interacting proteins. PUBMED:10567243 EPMC:10567243
Gitler D, Xu Y, Kao HT, Lin D, Lim S, Feng J, Greengard P, Augustine GJ; , J Neurosci. 2004;24:3711-3720.: Molecular determinants of synapsin targeting to presynaptic terminals. PUBMED:15071120 EPMC:15071120
Benfenati F, Ferrari R, Onofri F, Arcuri C, Giambanco I, Donato R; , J Neurochem. 2004;89:1260-1270.: S100A1 codistributes with synapsin I in discrete brain areas and inhibits the F-actin-bundling activity of synapsin I. PUBMED:15147519 EPMC:15147519
This tab holds annotation information from the InterPro database.
InterPro entry IPR019736
The synapsins are a family of neuron-specific phosphoproteins that coat synaptic vesicles and are involved in the binding between these vesicles and the cytoskeleton (including actin filaments). The family comprises 5 homologous proteins Ia, Ib, IIa, IIb and III. Synapsins I, II, and III are encoded by 3 different genes. The a and b isoforms of synapsin I and II are splice variants of the primary transcripts [PUBMED:10940454].
Synapsin I is mainly associated with regulation of neurotransmitter release from presynaptic neuron terminals [PUBMED:2859595]. Synapsin II, as well as being involved in neurotransmitter release, has a role in the synaptogenesis and synaptic plasticity responsible for long term potentiation [PUBMED:7777057]. 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 [PUBMED:10804215].
Structurally, synapsins are multidomain proteins, of which 3 domains are common to all the mammalian forms. The N-terminal `A' domain is ~30 residues long and contains a serine residue that serves as an acceptor site for protein kinase-mediated phosphorylation. This is followed by the `B' linker domain, which is ~80 residues long and is relatively poorly conserved. Domain `C' is the longest, spanning approximately 300 residues. This domain is highly conserved across all the synapsins (including those from Drosophila) and is possessed by all splice variants. The remaining six domains, D-I, are not shared by all the synapsins and differ both between the primary transcripts and the splice variants.
This entry represents a conserved octapeptide in the immediate N-terminal domain, which contains the phosphorylated serine residue.
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This example describes an architecture with one
Gladomain, followed by two consecutive
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Author:||Finn R, Coggill P|
|Number in seed:||3|
|Number in full:||174|
|Average length of the domain:||31.80 aa|
|Average identity of full alignment:||81 %|
|Average coverage of the sequence by the domain:||6.99 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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