Snca
entrez
20617
canonical
uniprot
O55042
canonical
ensembl
ENSMUSG00000025889
resolver
ensp
ENSMUSP00000109907
resolver
ensp
ENSMUSP00000126067
resolver
genesymbol
Snca
resolver
genesymbol_syn
Syn
resolver
uniprot
Q3U130
resolver
uniprot
Q9CXF8
resolver
uniprot
Q9EQC3
resolver
uniprot
Q9QUR3
resolver
uniprot_entry
SYUA_MOUSE
resolver
uniprot_sec
Q3U130
resolver
uniprot_sec
Q9CXF8
resolver
uniprot_sec
Q9EQC3
resolver
uniprot_sec
Q9QUR3
resolver
amino_acid_sequence
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA
uniprot
proteins
function
FUNCTION: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Also acts as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed:20798282, PubMed:25246573). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity). {ECO:0000250|UniProtKB:P37840, ECO:0000269|PubMed:20798282, ECO:0000269|PubMed:25246573}.
uniprot
proteins
mass_dalton
14485
uniprot
proteins
post_translational_modification
PTM: Phosphorylated, predominantly on serine residues. Phosphorylated on Tyr-125 upon osmotic stress. {ECO:0000250|UniProtKB:P37840}.; PTM: Ubiquitinated. The predominant conjugate is the diubiquitinated form. {ECO:0000250|UniProtKB:P37377}.; PTM: Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure. {ECO:0000250|UniProtKB:P37840}.
uniprot
proteins
protein_family
Synuclein family
uniprot
proteins
pubmed
10707987
uniprot
proteins
pubmed
11156617
uniprot
proteins
pubmed
12732244
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17296554
uniprot
proteins
pubmed
19004816
uniprot
proteins
pubmed
20798282
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25246573
uniprot
proteins
pubmed
31034892
uniprot
proteins
pubmed
9601701
uniprot
proteins
pubmed
9648883
uniprot
proteins
sequence_length
140
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31034892}. Membrane {ECO:0000250|UniProtKB:P37840}. Nucleus {ECO:0000250|UniProtKB:P37840}. Synapse {ECO:0000250|UniProtKB:P37840}. Secreted {ECO:0000250|UniProtKB:P37840}. Cell projection, axon {ECO:0000269|PubMed:17296554}. Note=Membrane-bound in dopaminergic neurons (By similarity). Expressed and colocalized with SEPTIN4 in dopaminergic axon terminals, especially at the varicosities (PubMed:17296554). {ECO:0000250|UniProtKB:P37840, ECO:0000269|PubMed:17296554}.
uniprot
proteins