Abstract
Synphilin-1 has been shown to interact with alpha-synuclein, which in turn is associated with Parkinson's disease. However, the function of synphilin-1 is unknown. We have cloned mouse synphilin in an attempt to describe conserved and therefore likely functional domains. The deduced amino acid sequence of the protein shows extensive homology with its human counterpart, with greatest similarities in those regions that contain ankyrin-like motifs and the coiled-coil domain. Expression of mouse synphilin-1 across tissues is similar to its human counterpart and not limited to brain. The results show that the synphilin-1 sequence and expression patterns are conserved across species.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Ankyrin Repeat / genetics
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Binding Sites / genetics
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Brain / metabolism*
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Brain / physiopathology
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Cloning, Molecular
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Gene Expression Regulation / physiology
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Humans
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Intracellular Signaling Peptides and Proteins
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Mice
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism*
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Neurons / metabolism*
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Parkinson Disease / genetics
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Parkinson Disease / metabolism*
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Parkinson Disease / physiopathology
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Protein Structure, Tertiary / genetics
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Sequence Homology, Amino Acid
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Sequence Homology, Nucleic Acid
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Synucleins
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alpha-Synuclein
Substances
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Carrier Proteins
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Intracellular Signaling Peptides and Proteins
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Nerve Tissue Proteins
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SNCA protein, human
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SNCAIP protein, human
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Snca protein, mouse
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Sncaip protein, mouse
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Synucleins
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alpha-Synuclein