IED Industry Enzyme Database

Detail Information for IndEnz0018001313
IED ID IndEnz0018001313
Enzyme Type ID peroxidase001313
Protein Name Alpha-synuclein
Non-A beta component of AD amyloid
Non-A4 component of amyloid precursor
NACP
Gene Name SNCA NACP PARK1
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA
Enzyme Length 140
Uniprot Accession Number P37840
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 (PubMed:28288128, PubMed:30404828, PubMed:20798282, PubMed:26442590). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed:28288128, PubMed:30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed:30404828). 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 (PubMed:20798282). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed:20798282). Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed:26442590). {ECO:0000269|PubMed:20798282, ECO:0000269|PubMed:26442590, ECO:0000269|PubMed:28288128, ECO:0000269|PubMed:30404828}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (2); Beta strand (7); Chain (1); Compositional bias (1); Helix (5); Metal binding (2); Modified residue (4); Mutagenesis (15); Natural variant (4); Region (3); Repeat (4); Turn (3)
Keywords 3D-structure;Acetylation;Alternative splicing;Alzheimer disease;Amyloid;Cell junction;Cell projection;Copper;Cytoplasm;Direct protein sequencing;Disease variant;Membrane;Metal-binding;Neurodegeneration;Nucleus;Parkinson disease;Parkinsonism;Phosphoprotein;Reference proteome;Repeat;Secreted;Synapse;Ubl conjugation
Interact With Q6PCB6; P00519; P00519-1; P00519-2; Q6ZTN6-2; P63010-2; O00203; P02647; P02649; P05067; Q8N6T3-3; Q9NP61; Q0P5N6; Q8WXK3; P18847; Q9H0Y0; P46379-2; Q07812; Q07817; O15392; Q8WUW1; Q5SZD1; P62158; Q8N5S9-2; P55212; Q7Z7K6; Q9HD42; Q16740; P10909; Q9UNS2; Q8IUI8; P48730-2; P99999; O75398; Q8NDP9; O60479; A0AVK6; O75530-2; O00472; Q8TC29; O00471; Q9UHY8; Q0VDC6; Q6PIV2; P02792; P06241; P06241-3; P62879; P49841; P68431; Q71DI3; Q969S8; Q9HCC6; Q8WVV9-3; P09017; P08107; P42858; P80217-2; Q16352; Q6DN90-2; O14713; Q9UIH9; Q9Y2M5; Q92876; Q9BYQ4; Q96JM7-2; P13473-2; Q9BYZ2; Q9H2C1; Q9UPM6; Q8TBB1; Q8N448; A2RU56; Q5S007; O95777; P07948; Q8TD91-2; P10636-6; P10636-8; Q8N6F8; Q8TDB4; A4FUJ8; Q8N594; Q9Y3D2; P00414; P02795; Q9Y483-4; O00746; O15381-5; Q86WS3; Q96FW1; Q6GQQ9-2; Q6VY07; O96013-2; Q9NR21-5; Q9NV79; Q13113; O75925; Q6ZR37; P17252; Q02156; O60260-5; O75400-2; P62191; P17980; Q9UI14; Q9UJ41-4; P62826; Q13702-2; P57052; Q8N5U6; Q6ZNA4-2; Q9ULX5; Q8WVD3; Q8IYW5; Q96D59; Q8N488; O75446; O00560; O43236; O75920-2; Q2NKQ1-4; Q01959; Q9HCE7-2; Itself; Q9Y6H5; Q9Y6H5-2; Q16143; P23497-2; Q99932-2; Q8NHS9; Q8TCT7-2; Q13501; O75886; Q16623; Q9BR01-2; Q92797-2; Q16650; Q13569; P28347-2; Q15554-4; Q9H0E2; O94811; P19474; P68363; P07437; Q8WVJ9; P62987; Q9BSL1; O15205; Q04323-2; Q96RL1-2; O75604-3; P63027; P40337-2; Q9UBQ0-2; Q9GZS3; O00308; Q04917; O43167-2; Q96NC0; Q8WUU4; Q8N895; Q8N988-2; Q68EA5; Q8NBB4-2; A8K878; P0DTC9; Q61327; Itself; Q04917
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19762560, ECO:0000269|PubMed:24936070, ECO:0000269|PubMed:25561023, ECO:0000269|PubMed:26442590, ECO:0000269|PubMed:31034892}. Membrane {ECO:0000269|PubMed:24936070}. Nucleus {ECO:0000269|PubMed:12859192, ECO:0000269|PubMed:24936070}. Cell junction, synapse {ECO:0000269|PubMed:15282274}. Secreted {ECO:0000269|PubMed:24936070}. Cell projection, axon {ECO:0000250|UniProtKB:O55042}. Note=Membrane-bound in dopaminergic neurons (PubMed:15282274). Expressed and colocalized with SEPTIN4 in dopaminergic axon terminals, especially at the varicosities (By similarity). {ECO:0000250|UniProtKB:O55042, ECO:0000269|PubMed:15282274}.
Modified Residue MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0000269|PubMed:22407793"; MOD_RES 87; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:10617630"; MOD_RES 125; /note="Phosphotyrosine; by FYN"; /evidence="ECO:0000269|PubMed:11162638, ECO:0000269|PubMed:12893833"; MOD_RES 129; /note="Phosphoserine; by BARK1, PLK2, CK2, CK1 and GRK5"; /evidence="ECO:0000269|PubMed:10617630, ECO:0000269|PubMed:11813001, ECO:0000269|PubMed:24936070"
Post Translational Modification PTM: 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. {ECO:0000269|PubMed:10617630, ECO:0000269|PubMed:10852916, ECO:0000269|PubMed:11162638, ECO:0000269|PubMed:11813001, ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:24936070}.; PTM: 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.; 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:0000269|PubMed:22407793}.
Signal Peptide
Structure 3D X-ray crystallography (12); Electron microscopy (35); NMR spectroscopy (6)
Cross Reference PDB 1XQ8; 2JN5; 2KKW; 2M55; 2N0A; 2X6M; 3Q25; 3Q26; 3Q27; 3Q28; 3Q29; 4BXL; 4R0U; 4R0W; 4RIK; 4RIL; 4ZNN; 5CRW; 6A6B; 6CT7; 6CU7; 6CU8; 6FLT; 6H6B; 6I42; 6L1T; 6L1U; 6L4S; 6LRQ; 6OSJ; 6OSL; 6OSM; 6PEO; 6PES; 6RT0; 6RTB; 6SST; 6SSX; 6UFR; 6XYO; 6XYP; 6XYQ; 7C1D; 7E0F; 7L7H; 7LC9; 7NCA; 7NCG; 7NCH; 7NCI; 7NCJ; 7NCK; 7STX;
Mapped Pubmed ID 10319874; 10391242; 10411933; 10583407; 11078745; 11173882; 11207390; 11227130; 11357958; 11401442; 11425308; 11467836; 11472875; 11487204; 11532993; 11701929; 11724769; 11744621; 11748744; 11751692; 11812148; 11812782; 11814343; 11814405; 11823645; 11852183; 118839; 11889756; 11893734; 11900526; 12025860; 12042811; 12044636; 12059041; 12062445; 12070658; 12115139; 12122208; 12124613; 12138709; 12145295; 12151787; 12217698; 12220378; 12239163; 12351642; 12352614; 12367530; 12377775; 12428717; 12428728; 12493604; 12534279; 12534296; 12541013; 12551928; 12576551; 12586824; 12598733; 12672549; 12684441; 1270801; 12714745; 12716427; 12716914; 12727333; 12752402; 12783249; 12784265; 12807436; 12807439; 12815044; 12815663; 12819014; 12857790; 12867415; 12868067; 12868068; 12900507; 12923179; 12923682; 12928483; 12973692; 14506232; 14507911; 14572463; 14583385; 14593171; 14596606; 14627698; 14645218; 14657499; 14657500; 14690528; 14692700; 14699135; 14711827; 14742448; 14996933; 14997013; 15028717; 15050722; 15078109; 15096050; 15103328; 15109581; 15132984; 15135042; 15155902; 15159488; 15180968; 15234109; 15236975; 15247485; 15265037; 15289452; 15300629; 15317865; 15333840; 15338643; 15364911; 15365127; 15455394; 15459341; 15465356; 15496679; 15502874; 15522241; 15541000; 15542733; 15544803; 15576511; 15590652; 15590933; 15591046; 15596612; 15615715; 15622440; 15628875; 15628878; 15641770; 15670652; 15671022; 15671169; 15671870; 15672325; 15684072; 15685368; 15717024; 15718234; 15731118; 15732111; 15755676; 15765523; 15767574; 15791003; 15817478; 15840579; 15845543; 15863497; 15895422; 15896322; 15917102; 15935068; 15935070; 15939304; 15941712; 15944382; 15955578; 15962837; 15976091; 15978696; 15981014; 16020543; 16020550; 16037493; 16051265; 16081040; 16092093; 16110277; 16166095; 16176937; 16216085; 16227205; 16239214; 16242637; 16250025; 16291942; 16297908; 16330147; 16330551; 16338184; 16358335; 16399671; 16403519; 16406146; 16410343; 16455667; 16464864; 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Motif
Gene Encoded By
Mass 14,460
Kinetics
Metal Binding METAL 2; /note=Copper; /evidence=ECO:0000305; METAL 50; /note=Copper; /evidence=ECO:0000305
Rhea ID
Cross Reference Brenda