Alternative names
- Alpha synuclein
- Alpha-synuclein
- Alpha-synuclein, isoform NACP140
- alphaSYN
- MGC105443
- MGC110988
- MGC127560
- MGC64356
- NACP
- Non A beta component of AD amyloid
- Non A4 component of amyloid
- Non A4 component of amyloid precursor
- Non-A beta component of AD amyloid
- Non-A-beta component of alzheimers disease amyloid , precursor of
- Non-A4 component of amyloid precursor
- Non-A4 component of amyloid, precursor of
- OTTHUMP00000218549
- OTTHUMP00000218551
- OTTHUMP00000218552
- OTTHUMP00000218553
- OTTHUMP00000218554
- PARK 1
- PARK 4
- PARK1
- PARK4
- Parkinson disease (autosomal dominant, Lewy body) 4
- Parkinson disease familial 1
- SNCA
- Snca synuclein
- Snca synuclein, alpha (non A4 component of amyloid precursor)
- SYN
- Synuclein alpha
- Synuclein alpha 140
- Synuclein, alpha (non A4 component of amyloid precursor)
- SYUA_HUMAN
see all
Function
May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation.
Tissue specificity
Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals.
Involvement in disease
Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1.Parkinson disease 1Parkinson disease 4Dementia Lewy body
Sequence similarities
Belongs to the synuclein family.
Domain
The "non A-beta component of Alzheimer disease amyloid plaque" domain (NAC domain) is involved in fibrils formation. The middle hydrophobic region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments.
Post-translationalmodifications
Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress.Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.Ubiquitinated. The predominant conjugate is the diubiquitinated form.Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
Cellular localization
Cytoplasm, cytosol. Membrane. Nucleus. Cell junction, synapse. Secreted. Membrane-bound in dopaminergic neurons.
Target information above from: UniProt accessionP37840The UniProt ConsortiumThe Universal Protein Resource (UniProt) in 2010Nucleic Acids Res. 38:D142-D148 (2010).
Information by UniProt