| IED ID | IndEnz0018001318 |
| Enzyme Type ID | peroxidase001318 |
| Protein Name |
Alpha-synuclein Synelfin |
| Gene Name | SNCA |
| Organism | Serinus canaria (Island canary) (Fringilla canaria) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Passeriformes Passeroidea Fringillidae Carduelinae Serinus Serinus canaria (Island canary) (Fringilla canaria) |
| Enzyme Sequence | MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSRTKEGVVHGVTTVAEKTKEQVSNVGGAVVTGVTAVAQKTVEGAGNIAAATGLVKKDQLAKQNEEGFLQEGMVNNTGAAVDPDNEAYEMPPEEEYQDYEPEA |
| Enzyme Length | 143 |
| Uniprot Accession Number | Q91448 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: May be involved in the regulation of dopamine release and transport.; FUNCTION: May be involved in neuronal plasticity. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Metal binding (2); Modified residue (1); Region (2); Repeat (4) |
| Keywords | Acetylation;Cell junction;Copper;Cytoplasm;Membrane;Metal-binding;Nucleus;Repeat;Secreted;Synapse |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {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}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 14,874 |
| Kinetics | |
| Metal Binding | METAL 2; /note=Copper; /evidence=ECO:0000250; METAL 50; /note=Copper; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |