| IED ID | IndEnz0001000350 |
| Enzyme Type ID | amylase000350 |
| Protein Name |
Vesicle-associated membrane protein 8 VAMP-8 Endobrevin Edb |
| Gene Name | Vamp8 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MEEASGSAGNDRVRNLQSEVEGVKNIMTQNVERILSRGENLDHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVIICVIVLIIVILIILFATGTIPT |
| Enzyme Length | 101 |
| Uniprot Accession Number | O70404 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Plays also a role in regulated enzyme secretion in pancreatic acinar cells (PubMed:15363411). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). Participates also in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (By similarity). {ECO:0000250|UniProtKB:Q9BV40, ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:22118466}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Helix (1); Modified residue (7); Mutagenesis (2); Sequence conflict (2); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | 3D-structure;Acetylation;Antiviral defense;Autophagy;Cell membrane;Coiled coil;Cytoplasmic vesicle;Endosome;Lysosome;Membrane;Phosphoprotein;Protein transport;Reference proteome;Transmembrane;Transmembrane helix;Transport |
| Interact With | O55012 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:27628032}; Single-pass type IV membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:22118466}; Single-pass type IV membrane protein {ECO:0000305}. Zymogen granule membrane {ECO:0000269|PubMed:15363411}; Single-pass type IV membrane protein {ECO:0000305}. Note=Perinuclear vesicular structures of the early and late endosomes, coated pits, and trans-Golgi (By similarity). Sub-tight junctional domain in retinal pigment epithelium cells (By similarity). Midbody region during cytokinesis (By similarity). Lumenal oriented, apical membranes of nephric tubular cell (By similarity). Cycles through the apical but not through the basolateral plasma membrane (By similarity). Apical region of acinar cells; in zymogen granule membranes (PubMed:15363411). {ECO:0000250|UniProtKB:Q9WUF4, ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:9614193}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:Q9BV40; MOD_RES 5; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9BV40; MOD_RES 18; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9BV40; MOD_RES 28; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9BV40; MOD_RES 48; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9BV40; MOD_RES 54; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:19144319; MOD_RES 55; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19144319 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3ZYM; |
| Mapped Pubmed ID | 10379359; 10725249; 11217851; 12466851; 14610273; 14668490; 16602821; 16615898; 16935260; 17065550; 17215514; 18203950; 18227281; 18250339; 18292538; 18321981; 18388320; 18535671; 18614015; 18692471; 18923845; 19097053; 19274433; 19395672; 19564343; 19607812; 19759285; 19830729; 19841070; 20876717; 21151919; 21224474; 21733851; 22144578; 22450911; 22589474; 22841572; 23213422; 23217709; 23341629; 23870310; 24194600; 24550300; 25138214; 26209658; 27009205; 27280768; 27480124; 28242757; 28688576; 28974617; 30681394; 31541089; 33332551; 33454017; 9560157; 9878266; |
| Motif | |
| Gene Encoded By | |
| Mass | 11,451 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |