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Sequence conservation between mouse and human synphilin-1.

Casey O'Farrell·Fiona Pickford·Liselot Vink·Eileen McGowan·Mark R Cookson
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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.

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AnimalsAnkyrin RepeatBinding SitesBrainCarrier ProteinsCloning, MolecularGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsMiceMolecular Sequence DataNerve Tissue ProteinsNeuronsParkinson DiseaseProtein Structure, TertiarySequence Homology, Amino AcidSequence Homology, Nucleic AcidSynucleinsalpha-SynucleinJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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Casey O'Farrell, Fiona Pickford, Liselot Vink, Eileen McGowan, Mark R Cookson. 2002-03-29. Sequence conservation between mouse and human synphilin-1.. https://doi.org/10.1016/s0304-3940(02)00068-x

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