| IED ID |
IndEnz0018001317 |
| Enzyme Type ID |
peroxidase001317 |
| Protein Name |
Alpha-synuclein
|
| Gene Name |
Snca |
| Organism |
Rattus norvegicus (Rat) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Deuterostomia
Chordata
Craniata
Vertebrata
Gnathostomata (jawed vertebrates)
Teleostomi
Euteleostomi
Sarcopterygii
Dipnotetrapodomorpha
Tetrapoda
Amniota
Mammalia
Theria
Eutheria
Boreoeutheria
Euarchontoglires
Glires (Rodents and rabbits)
Rodentia
Myomorpha (mice and others)
Muroidea
Muridae
Murinae
Rattus
Rattus norvegicus (Rat)
|
| Enzyme Sequence |
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPSSEAYEMPSEEGYQDYEPEA |
| Enzyme Length |
140 |
| Uniprot Accession Number |
P37377 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme 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). Acts also 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 (By similarity). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Plays also 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}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Alternative sequence (3); Chain (1); Metal binding (2); Modified residue (3); Region (3); Repeat (4) |
| Keywords |
Acetylation;Alternative splicing;Cell junction;Cell projection;Copper;Cytoplasm;Direct protein sequencing;Membrane;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Repeat;Secreted;Synapse;Ubl conjugation |
| Interact With |
|
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P37840}. Membrane {ECO:0000250|UniProtKB:P37840}. Nucleus {ECO:0000250|UniProtKB:P37840}. Cell junction, synapse {ECO:0000250|UniProtKB:P37840}. Secreted {ECO:0000250|UniProtKB:P37840}. Cell projection, axon {ECO:0000250|UniProtKB:O55042}. Note=Membrane-bound in dopaminergic neurons (By similarity). Expressed and colocalized with SEPTIN4 in dopaminergic axon terminals, especially at the varicosities (By similarity). {ECO:0000250|UniProtKB:O55042, ECO:0000250|UniProtKB:P37840}. |
| Modified Residue |
MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P37840; MOD_RES 125; /note=Phosphotyrosine; by FYN; /evidence=ECO:0000250|UniProtKB:P37840; MOD_RES 129; /note=Phosphoserine; by PLK2; /evidence=ECO:0000250|UniProtKB:P37840 |
| 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:0000269|PubMed:12408865}.; PTM: Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure. {ECO:0000250|UniProtKB:P37840}. |
| Signal Peptide |
|
| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
10319874;
10777786;
11032911;
11679584;
11698390;
11810180;
11821392;
11918289;
11943812;
11956199;
12000718;
12037467;
12122208;
12127102;
12162735;
12562524;
12787066;
12821390;
12917442;
14622225;
14645218;
15322100;
15466467;
15590652;
15691713;
15795473;
15804428;
15863497;
16020543;
16030137;
16077187;
16174552;
16176937;
16227205;
16423428;
16460685;
16503161;
16837598;
16854843;
16981894;
17029600;
17085784;
17101231;
17273802;
17275196;
17318638;
17380380;
17592526;
17635667;
17645694;
17676786;
17714497;
17868672;
18001274;
18178617;
18195004;
18427558;
18449945;
18566453;
18704197;
18761401;
18790059;
18800064;
18804502;
18817762;
19046408;
19112474;
19118601;
19224863;
19429081;
19493164;
19549071;
19664623;
19692427;
19813144;
19818834;
20026244;
20071342;
20081243;
20098715;
20203178;
20345648;
20405200;
20511551;
20551914;
20617407;
20664530;
20959456;
21050448;
21252228;
21272005;
21330369;
21338582;
21832049;
22251432;
22315227;
22619171;
22639889;
22737239;
22833673;
23077527;
23128054;
23278133;
23291291;
23431141;
23441091;
23454680;
23567316;
23567651;
23610405;
23629650;
23809578;
23954626;
24248062;
24403142;
24664141;
24687852;
24698767;
24722055;
24747612;
24810576;
24833599;
24927544;
24983211;
25019582;
25089700;
25090657;
25195598;
25251017;
25446002;
25484190;
25669123;
25756858;
25896939;
26075822;
26076669;
26078453;
26158517;
26192120;
26212128;
26378614;
26822976;
26907683;
26989132;
27133445;
27477055;
27581683;
27597756;
27640673;
27708338;
28193887;
28900007;
28933786;
28984618;
29180624;
29198021;
29229832;
29337114;
29563864;
29702063;
29749529;
30081046;
30132200;
30155513;
30901378;
31758091;
32059750;
32113849;
32385113;
32878882;
32948930;
33428933;
33774037;
34875351;
34904280;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
14,515 |
| Kinetics |
|
| Metal Binding |
METAL 2; /note=Copper; /evidence=ECO:0000250; METAL 50; /note=Copper; /evidence=ECO:0000250 |
| Rhea ID |
|
| Cross Reference Brenda |
|