| Literature References | 1. LAVEDAN, C.
The synuclein family.
GENOME RES. 8 871-880 (1998).
2. TOBE, T., NAKAJO, S., TANAKA, A., MITOYA, A., OMATA, K., NAKAYA, K.,
TOMITA, M. AND NAKAMURA, Y.
Cloning and characterization of the cDNA encoding a novel brain-specific
14kDa protein.
J.NEUROCHEM. 59 1624-1629 (1992).
3. GEORGE, J.M., JIN, H., WOODS, W.S. AND CLAYTON, D.F.
Characterization of a novel protein regulated during the critical period
for song learning in the zebra finch.
NEURON 15 361-372 (1995).
4. NAKAJO, S., TSUKADA, K., OMATA, K., NAKAMURA, Y. AND NAKAYA, K.
A new brain-specific 14kDa protein is a phosphoprotein. Its complete amino
acid sequence and evidence for phosphorylation.
EUR.J.BIOCHEMISTRY 217 1057-1063 (1993).
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| Documentation | Human synuclein has been shown to belong to a gene family [1]. To date,
three different proteins, termed alpha, beta and gamma, have been
characterised. The amino acid sequences of synucleins share a similar
overall structure: hydropathy analysis reveals a central hydrophobic domain
of ~30 amino acids, flanked by highly hydrophilic stretches; the N-terminal
flanking region contains four repeating motifs (EKTKEGV); and the C-terminal
domain is rich in glutamic acid and proline [2]
Synelfin, a homologue of synuclein, is a soluble presynaptic protein that
is predicted to form an amphipathic alpha-helical structure typical of the
lipid-binding domain in apolipoproteins [3]. This protein is believed to
serve a novel function critical to the regulation of vertebrate neural
plasticity [3].
Beta-synuclein is expressed in the brain, specifically in synapses around
neurons, but not in glial cells [4]. The protein, which has been designated
a phosphoneuroprotein, has been found to be phosphorylated in vitro and in
vivo [4]. It is believed that the physiological functions of beta-synuclein
may be controlled by the phosphorylation reaction.
BSYNUCLEIN is a 4-element fingerprint that provides a signature for
beta-synucleins. The fingerprint was derived from an initial alignment of
3 sequences: the motifs were drawn from short conserved regions spanning
virtually the full alignment length, focusing on those sections that
characterise the beta-synucleins but distinguish them from the rest of the
synuclein family - motif 1 lies in the N-terminal region of the hydrophobic
domain; and motifs 2-4 span the Glu-Pro-rich C-terminal domain. A single
iteration on SPTR37_10f was required to reach convergence, no further
sequences being identified beyond the starting set.
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