##gff-version 3 P37840 UniProtKB Chain 1 140 . . . ID=PRO_0000184022;Note=Alpha-synuclein P37840 UniProtKB Repeat 20 30 . . . Note=1 P37840 UniProtKB Repeat 31 41 . . . Note=2 P37840 UniProtKB Repeat 42 56 . . . Note=3%3B approximate P37840 UniProtKB Repeat 57 67 . . . Note=4 P37840 UniProtKB Region 20 67 . . . Note=4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4) P37840 UniProtKB Region 100 140 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P37840 UniProtKB Region 111 140 . . . Note=Interaction with SERF1A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22854022;Dbxref=PMID:22854022 P37840 UniProtKB Compositional bias 116 140 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P37840 UniProtKB Binding site 2 2 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 P37840 UniProtKB Binding site 50 50 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 P37840 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22407793;Dbxref=PMID:22407793 P37840 UniProtKB Modified residue 87 87 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10617630;Dbxref=PMID:10617630 P37840 UniProtKB Modified residue 125 125 . . . Note=Phosphotyrosine%3B by FYN;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11162638,ECO:0000269|PubMed:12893833;Dbxref=PMID:11162638,PMID:12893833 P37840 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine%3B by BARK1%2C PLK2%2C CK2%2C CK1 and GRK5;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10617630,ECO:0000269|PubMed:11813001,ECO:0000269|PubMed:24936070;Dbxref=PMID:10617630,PMID:11813001,PMID:24936070 P37840 UniProtKB Alternative sequence 41 54 . . . ID=VSP_006363;Note=In isoform 2-5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7601450;Dbxref=PMID:7601450 P37840 UniProtKB Alternative sequence 103 130 . . . ID=VSP_006364;Note=In isoform 2-4. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:7601450,ECO:0000303|PubMed:7802671;Dbxref=PMID:7601450,PMID:7802671 P37840 UniProtKB Natural variant 30 30 . . . ID=VAR_007957;Note=In PARK1%3B no effect on oligomerization. A->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:9462735;Dbxref=dbSNP:rs104893878,PMID:25561023,PMID:9462735 P37840 UniProtKB Natural variant 46 46 . . . ID=VAR_022703;Note=In PARK1 and DLB%3B significant increase in binding to negatively charged phospholipid liposomes%3B increases oligomerization. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14755719,ECO:0000269|PubMed:15498564,ECO:0000269|PubMed:25561023;Dbxref=dbSNP:rs104893875,PMID:14755719,PMID:15498564,PMID:25561023 P37840 UniProtKB Natural variant 50 50 . . . ID=VAR_070171;Note=In PARK1%3B no effect on protein structure%3B no effect on phosphorylation of the protein%3B no effect on membrane- and lipid-binding%3B increases oligomerization%3B increases fibril formation%3B increases secretion of the protein%3B impairs copper-binding. H->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23427326,ECO:0000269|PubMed:23457019,ECO:0000269|PubMed:24936070,ECO:0000269|PubMed:25561023;Dbxref=dbSNP:rs201106962,PMID:23427326,PMID:23457019,PMID:24936070,PMID:25561023 P37840 UniProtKB Natural variant 53 53 . . . ID=VAR_007454;Note=In PARK1%3B no effect on osmotic stress-induced phosphorylation%3B increases oligomerization. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12893833,ECO:0000269|PubMed:25561023,ECO:0000269|PubMed:9197268;Dbxref=dbSNP:rs104893877,PMID:12893833,PMID:25561023,PMID:9197268 P37840 UniProtKB Mutagenesis 2 2 . . . Note=Impairs copper-binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 P37840 UniProtKB Mutagenesis 35 35 . . . Note=No effect on oligomerization. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25561023;Dbxref=PMID:25561023 P37840 UniProtKB Mutagenesis 39 39 . . . Note=No effect on osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 P37840 UniProtKB Mutagenesis 50 50 . . . Note=Impairs copper-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21319811;Dbxref=PMID:21319811 P37840 UniProtKB Mutagenesis 57 57 . . . Note=Increases oligomerization. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25561023;Dbxref=PMID:25561023 P37840 UniProtKB Mutagenesis 67 71 . . . Note=Reduces polymerization into amyloid fibrils. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19722699;Dbxref=PMID:19722699 P37840 UniProtKB Mutagenesis 71 82 . . . Note=Impairs polymerization into amyloid fibrils. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19722699;Dbxref=PMID:19722699 P37840 UniProtKB Mutagenesis 76 77 . . . Note=Impairs polymerization into amyloid fibrils. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19722699;Dbxref=PMID:19722699 P37840 UniProtKB Mutagenesis 76 76 . . . Note=Does not affect polymerization into amyloid fibrils. Missing P37840 UniProtKB Mutagenesis 77 77 . . . Note=Does not affect polymerization into amyloid fibrils. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19722699;Dbxref=PMID:19722699 P37840 UniProtKB Mutagenesis 78 78 . . . Note=Does not affect polymerization into amyloid fibrils. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19722699;Dbxref=PMID:19722699 P37840 UniProtKB Mutagenesis 85 94 . . . Note=Reduces polymerization into amyloid fibrils. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19722699;Dbxref=PMID:19722699 P37840 UniProtKB Mutagenesis 125 125 . . . Note=Abolishes osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 P37840 UniProtKB Mutagenesis 133 133 . . . Note=No effect on osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 P37840 UniProtKB Mutagenesis 136 136 . . . Note=No effect on osmotic stress-induced phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12893833;Dbxref=PMID:12893833 P37840 UniProtKB Helix 3 11 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3Q25 P37840 UniProtKB Beta strand 16 18 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6XYP P37840 UniProtKB Helix 21 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3Q26 P37840 UniProtKB Beta strand 34 36 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8A4L P37840 UniProtKB Beta strand 38 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7V48 P37840 UniProtKB Helix 41 44 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3Q27 P37840 UniProtKB Beta strand 46 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OSJ P37840 UniProtKB Helix 52 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3Q27 P37840 UniProtKB Beta strand 60 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7E0F P37840 UniProtKB Helix 66 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3Q28 P37840 UniProtKB Beta strand 71 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7XO3 P37840 UniProtKB Beta strand 82 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8A9L P37840 UniProtKB Beta strand 88 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UFR P37840 UniProtKB Beta strand 110 113 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XQ8 P37840 UniProtKB Turn 120 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XQ8 P37840 UniProtKB Turn 124 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XQ8 P37840 UniProtKB Turn 133 136 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2N0A