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0STX8_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005783 endoplasmic reticulum (TAS)
0005887 integral to plasma membrane (TAS)
0006810 transport (TAS)

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Domain Architecture (Details)
InterPro domains assigned to SynO:
The process of vesicular fusion with target membranes depends on a set of SNAREs (SNAP-Receptors).hich are associated with the fusing membranes . Target SNAREs (t-SNAREs) are localised on the target membrane and belong to two different families.he syntaxin-like family and the SNAP-25 like family. One member of each family.ogether with av-SNARE localised on the vesicular required for fusion. The Syntaxins are type-I transmembrane proteins that contain several regions with coiled-coil propensity in their cytosolic part.he SNARE motif. SNAP-25 () is a protein consisting of two coiled-coil regions.hich is associated with the membrane by lipid anchors. SNARE motifs assemble into parallel four helix bundles stabilised by the burial of these hydrophobic helix faces in the bundle core. Monomeric SNARE motifs are disordered so this assembly reaction is accompanied by a dramatic increase in alpha-helical secondary structure . The parallel arrangement of SNARE motifs within complexes bring the transmembrane anchors.nd the two membranes.nto close proximity. Recently.t was shown that the two coiled-coil regions of SNAP-25 andone of the coiled-coil regions of the syntaxins are related . This domain is found in both Syntaxin and SNAP-25 families as well as in other proteins.
  IPR000727:Target SNARE coiled-coil region
Soluble N-ethylmaleimide attachment protein receptor (SNARE) proteins are a family of membrane-associated proteins characterised by an alpha-helical coiled-coil domain called the SNARE motif . These proteins are classified as v-SNAREs and t-SNAREs based on their localisation on vesicle or target membrane; another classification scheme defines R-SNAREs and Q-SNAREs.s based on the conserved arginine or glutamine residue in the centre of the SNARE motif. SNAREs are localised to distinct membrane compartments of the secretory and endocytic trafficking pathways.nd contribute to the specificity of intracellular membrane fusion processes.The t-SNARE domain consists of a 4-helical bundle with a coiled-coil twist. The SNARE motif contributes to the fusion of two membranes. SNARE motifs fall into four classes: homologues of syntaxin 1a (t-SNARE).AMP-2 (v-SNARE).nd the N- and C-terminal SNARE motifs of SNAP-25. It is thought that one member from each class interacts to form a SNARE complex.The SNARE motif represented in this entry is found in the N-terminal domains of certain syntaxin family members: syntaxin 1a.hich is required for neurotransmitter release.yntaxin 6.hich is found in endosomal transport vesicles .east Sso1p .nd Vam3p. yeast syntaxin essential for vacuolar fusion . The SNARE motifs in these proteins share structural similarity.espite having a low level of sequence similarity.
SequencesProtein: STX8_HUMAN (236 aa)
mRNA: NM_004853
Local Annotation
Synapse Ontology
Fusion of intracellular membrane-bound vesicles with the pre-synaptic membrane of the neuronal cell resulting in release of neurotransmitter into the synaptic cleft.
sdb:0049 synaptic vesicle fusion  (Evidence:keywords,domains)
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords,domains)
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords,domains)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords,domains)
priming for exocytosis prepares the calcium-dependent release and may involve partial fusion process. The vesicles are primed and become responsive to calcium.
sdb:0120 priming  (Evidence:keywords,domains)
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:keywords,domains)
sdb:0328 transmitters release and endocytosis  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 59 residues, 9094513-9094687Exon2: 36 residues, 9222593-9222695Exon3: 33 residues, 9335870-9335963Exon4: 43 residues, 9349079-9349204Exon5: 39 residues, 9389213-9389324Exon6: 33 residues, 9401475-9401570Exon7: 35 residues, 9412412-9412512Exon8: 57 residues, 9419833-9420000Exon9: 2 residues, -Jump to STX8_HUMAN  
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