STX6
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2NPS, 4J2C
Identifiers
Aliases	STX6, syntaxin 6
External IDs	OMIM: 603944 MGI: 1926235 HomoloGene: 115622 GeneCards: STX6
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q25.3 Start 180,972,712 bp[1] End 181,023,121 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 G3 Start 155,034,461 bp[2] End 155,084,002 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte endothelial cell ganglionic eminence Brodmann area 23 monocyte middle temporal gyrus prefrontal cortex cerebellar hemisphere postcentral gyrus superior frontal gyrus Top expressed in external carotid artery internal carotid artery conjunctival fornix medullary collecting duct endocardial cushion hair follicle left lung lobe ureter nucleus accumbens parotid gland More reference expression data BioGPS n/a
Gene ontology Molecular function protein binding syntaxin binding SNAP receptor activity SNARE binding Cellular component membrane plasma membrane SNARE complex early endosome phagocytic vesicle perinuclear region of cytoplasm clathrin-coated vesicle trans-Golgi network integral component of membrane Golgi membrane trans-Golgi network membrane Golgi apparatus nucleoplasm cytosol synaptic vesicle integral component of synaptic vesicle membrane endomembrane system Biological process endosome organization regulation of protein localization vesicle docking retrograde transport, endosome to Golgi Golgi vesicle transport protein transport vesicle fusion Golgi ribbon formation vesicle-mediated transport intracellular protein transport endocytic recycling synaptic vesicle to endosome fusion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10228 58244 Ensembl ENSG00000135823 ENSMUSG00000026470 UniProt O43752 Q9JKK1 RefSeq (mRNA) NM_001286210 NM_005819 NM_021433 RefSeq (protein) NP_001273139 NP_005810 NP_067408 Location (UCSC) Chr 1: 180.97 – 181.02 Mb Chr 1: 155.03 – 155.08 Mb PubMed search [3] [4]
Wikidata
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Syntaxin-6 is a protein that in humans is encoded by the STX6 gene.^[5][6]

Interactions

STX6 has been shown to interact with SNAP23,^[7] VAMP3^[8] and VAMP4.^[8]

N terminal protein domain

The protein domain Syntaxin 6 N terminal protein domain is a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) found in endosomal transport vesicles. It is part of the family, of target SNAREs (t-SNAREs). It is a vital aid to exporting and importing cell cargo through a process called cell trafficking. Its SNARE motif shows significant homology to both syntaxin 1a and S25C, indicating similarity through evolutionary conservation. The structure of the syntaxin 6 N-terminal domain shows strong structural similarity with the N-terminal domains of syntaxin 1a, Sso1p, and Vam3p; despite a very low level of sequence similarity. SNARE functions essentially as a tether to hold the vesicle. The cytoplasmic regions of SNARE found on transport vesicles and target membranes interact, then a four-helix coiled coil forms. This links the cell membrane and vesicles together in such a way that it overcomes the energetic barrier to fusing two lipid bilayers. This is the way cell cargo is exchanged. This particular entry focuses on the N-terminal domain of Syntaxin 6.^[9]

Structure

Members of this entry, which are found in the amino terminus of various SNARE proteins, adopt a structure consisting of an antiparallel three-helix bundle. Their exact function has not been determined, though it is known that they regulate the SNARE motif, as well as mediate various protein-protein interactions involved in membrane-transport.^[10]

Function

SNAREs play a vital role in the trafficking of cell cargo. The vesicles fuse to the cell membrane with the help of SNARE proteins. The SNARE motifs form a four-helix bundle that contributes to the fusion of two membranes. More specifically, the N-terminal domain binds to the SNARE motif, and this intramolecular interaction decreases the rate of association with the partner SNARE. However the N terminal domain's function still remains to fully elucidated.^[10]