Primary Information |
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BoMiProt ID | Bomi3847 |
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Protein Name | Alpha-synuclein |
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Organism | Bos taurus |
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Uniprot ID | Q3T0G8 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001029213.1 |
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Aminoacid Length | 140 |
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Molecular Weight | 14508 |
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FASTA Sequence |
Download |
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Gene Name | SNCA |
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Gene ID | 282857 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | Abundant in axon terminals of presynaptic neurons. |
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Protein Function | highly enriched in presynaptic nerve terminals.synaptic vesicle trafficking and subsequent neurotransmitter release. |
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Biochemical Properties | The central half of the alpha-synuclein polypeptide, containing five tandem repeats as well as a part of the carboxyl-terminal acidic region, forms the core structure of alpha-synuclein filaments, which is coated by the amino- and carboxyl-terminal portions at the periphery. |
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PTMs | Phosphorylated.Ubiquitinated.Acetylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q3T0G8|SYUA_BOVIN Alpha-synuclein OS=Bos taurus OX=9913 GN=SNCA PE=2 SV=1
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGRTKEGVLYVGSKTKEGVVHGVTTVAEKTK
EQVTNVGEAVVTGVTAVAQKTVEGAGIAAATGFGKKDHMGKGEEGASQEGILEDMPVDP
DNEAEMPEEGYQDYEPEA
|
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Predicted Disorder Regions | 1 disordered segment; (1-140) |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | Phosphorylated on Tyr-125 upon osmotic stress.Acetylation at Met-1 for proper folding and native oligomeric structure. |
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Additional Comments | Accumulation of misfolded oligomers and larger aggregates of α-synuclein defines multiple neurodegenerative diseases called synucleinopathies |
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Bibliography | Burré J, Sharma M, Südhof TC. Cell Biology and Pathophysiology of α-Synuclein. Cold Spring Harb Perspect Med. 2018 Mar 1;8(3):a024091. doi: 10.1101/cshperspect.a024091. PMID: 28108534; PMCID: PMC5519445. |