The domain within your query sequence starts at position 1 and ends at position 123; the E-value for the Synuclein domain shown below is 6.6e-58.
MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGTKTKENVVQSVTSVAEKTK EQANAVSEAVVSSVNTVANKTVEEAENIVVTTGVVRKEDLEPPAQDQEAKEQEENEEAKS GED
Synuclein |
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PFAM accession number: | PF01387 |
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Interpro abstract (IPR001058): | Synucleins are small, soluble proteins expressed primarily in neural tissue and in certain tumours [ (PUBMED:9750188) (PUBMED:11806835) ]. The family includes three known proteins: alpha-synuclein, beta-synuclein, and gamma-synuclein. All synucleins have in common a highly conserved alpha-helical lipid-binding motif with similarity to the class-A2 lipid-binding domains of the exchangeable apolipoproteins [ (PUBMED:10952980) ]. Synuclein family members are not found outside vertebrates, although they have some conserved structural similarity with plant 'late-embryo-abundant' proteins. The alpha- and beta-synuclein proteins are found primarily in brain tissue, where they are seen mainly in presynaptic terminals [ (PUBMED:7857654) (PUBMED:7877458) ]. The gamma-synuclein protein is found primarily in the peripheral nervous system and retina, but its expression in breast tumors is a marker for tumor progression [ (PUBMED:9044857) ]. Normal cellular functions have not been determined for any of the synuclein proteins, although some data suggest a role in the regulation of membrane stability and/or turnover. Mutations in alpha-synuclein are associated with rare familial cases of early-onset Parkinson's disease, and the protein accumulates abnormally in Parkinson's disease, Alzheimer's disease, and several other neurodegenerative illnesses [ (PUBMED:11433374) ]. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Synuclein