Protein-coding gene in the species Homo sapiens
STX6 |
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![](//upload.wikimedia.org/wikipedia/commons/thumb/a/ac/Protein_STX6_PDB_1lvf.png/250px-Protein_STX6_PDB_1lvf.png) |
Available structures |
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PDB | Ortholog search: PDBe RCSB |
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List of PDB id codes |
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2NPS, 4J2C |
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Identifiers |
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Aliases | STX6, syntaxin 6 |
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External IDs | OMIM: 603944; MGI: 1926235; HomoloGene: 115622; GeneCards: STX6; OMA:STX6 - orthologs |
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Gene location (Human) |
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![Chromosome 1 (human)](//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Ideogram_human_chromosome_1.svg/300px-Ideogram_human_chromosome_1.svg.png) | Chr. | Chromosome 1 (human)[1] |
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| Band | 1q25.3 | Start | 180,972,712 bp[1] |
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End | 181,023,121 bp[1] |
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Gene location (Mouse) |
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![Chromosome 1 (mouse)](//upload.wikimedia.org/wikipedia/commons/thumb/f/fb/Ideogram_house_mouse_chromosome_1.svg/260px-Ideogram_house_mouse_chromosome_1.svg.png) | Chr. | Chromosome 1 (mouse)[2] |
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| Band | 1|1 G3 | Start | 155,034,461 bp[2] |
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End | 155,084,002 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - secondary oocyte
- endothelial cell
- gingival epithelium
- ganglionic eminence
- Brodmann area 23
- skin of thigh
- skin of hip
- monocyte
- primary visual cortex
- cartilage tissue
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| Top expressed in | - external carotid artery
- internal carotid artery
- Rostral migratory stream
- conjunctival fornix
- epithelium of lens
- medullary collecting duct
- endocardial cushion
- hair follicle
- left lung lobe
- Gonadal ridge
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| More reference expression data |
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BioGPS | |
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Gene ontology |
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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 |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | | |
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RefSeq (protein) | | |
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Location (UCSC) | Chr 1: 180.97 – 181.02 Mb | Chr 1: 155.03 – 155.08 Mb |
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PubMed search | [3] | [4] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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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]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000135823 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026470 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Martín-Martín B, Nabokina SM, Lazo PA, Mollinedo F (March 1999). "Co-expression of several human syntaxin genes in neutrophils and differentiating HL-60 cells: variant isoforms and detection of syntaxin 1" (PDF). Journal of Leukocyte Biology. 65 (3): 397–406. doi:10.1002/jlb.65.3.397. hdl:10261/59829. PMID 10080545. S2CID 18988377.
- ^ "Entrez Gene: STX6 syntaxin 6".
- ^ Martín-Martín B, Nabokina SM, Blasi J, Lazo PA, Mollinedo F (October 2000). "Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis". Blood. 96 (7): 2574–83. doi:10.1182/blood.V96.7.2574. PMID 11001914.
- ^ a b Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, et al. (February 2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform". The Journal of Cell Biology. 156 (4): 653–64. doi:10.1083/jcb.200110081. PMC 2174079. PMID 11839770.
- ^ Jung JJ, Inamdar SM, Tiwari A, Choudhury A (August 2012). "Regulation of intracellular membrane trafficking and cell dynamics by syntaxin-6". Bioscience Reports. 32 (4): 383–91. doi:10.1042/BSR20120006. PMC 3392101. PMID 22489884.
- ^ a b Misura KM, Bock JB, Gonzalez LC, Scheller RH, Weis WI (July 2002). "Three-dimensional structure of the amino-terminal domain of syntaxin 6, a SNAP-25 C homolog". Proceedings of the National Academy of Sciences of the United States of America. 99 (14): 9184–9. doi:10.1073/pnas.132274599. PMC 123115. PMID 12082176.
Further reading
- Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
- Bock JB, Lin RC, Scheller RH (July 1996). "A new syntaxin family member implicated in targeting of intracellular transport vesicles". The Journal of Biological Chemistry. 271 (30): 17961–5. doi:10.1074/jbc.271.30.17961. PMID 8663448.
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, et al. (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- Simonsen A, Lippé R, Christoforidis S, Gaullier JM, Brech A, Callaghan J, et al. (July 1998). "EEA1 links PI(3)K function to Rab5 regulation of endosome fusion". Nature. 394 (6692): 494–8. Bibcode:1998Natur.394..494S. doi:10.1038/28879. PMID 9697774. S2CID 4305220.
- Wong SH, Xu Y, Zhang T, Griffiths G, Lowe SL, Subramaniam VN, et al. (January 1999). "GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6". Molecular Biology of the Cell. 10 (1): 119–34. doi:10.1091/mbc.10.1.119. PMC 25158. PMID 9880331.
- Steegmaier M, Klumperman J, Foletti DL, Yoo JS, Scheller RH (June 1999). "Vesicle-associated membrane protein 4 is implicated in trans-Golgi network vesicle trafficking". Molecular Biology of the Cell. 10 (6): 1957–72. doi:10.1091/mbc.10.6.1957. PMC 25394. PMID 10359608.
- Simonsen A, Gaullier JM, D'Arrigo A, Stenmark H (October 1999). "The Rab5 effector EEA1 interacts directly with syntaxin-6". The Journal of Biological Chemistry. 274 (41): 28857–60. doi:10.1074/jbc.274.41.28857. PMID 10506127.
- Scales SJ, Chen YA, Yoo BY, Patel SM, Doung YC, Scheller RH (May 2000). "SNAREs contribute to the specificity of membrane fusion". Neuron. 26 (2): 457–64. doi:10.1016/S0896-6273(00)81177-0. PMID 10839363.
- Martín-Martín B, Nabokina SM, Blasi J, Lazo PA, Mollinedo F (October 2000). "Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis". Blood. 96 (7): 2574–83. doi:10.1182/blood.V96.7.2574. PMID 11001914.
- Wade N, Bryant NJ, Connolly LM, Simpson RJ, Luzio JP, Piper RC, James DE (June 2001). "Syntaxin 7 complexes with mouse Vps10p tail interactor 1b, syntaxin 6, vesicle-associated membrane protein (VAMP)8, and VAMP7 in b16 melanoma cells" (PDF). The Journal of Biological Chemistry. 276 (23): 19820–7. doi:10.1074/jbc.M010838200. PMID 11278762. S2CID 38183181.
- Charest A, Lane K, McMahon K, Housman DE (August 2001). "Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6". The Journal of Biological Chemistry. 276 (31): 29456–65. doi:10.1074/jbc.M104137200. PMID 11384996.
- Rotem-Yehudar R, Galperin E, Horowitz M (August 2001). "Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29". The Journal of Biological Chemistry. 276 (35): 33054–60. doi:10.1074/jbc.M009913200. PMID 11423532.
- Cheng J, Moyer BD, Milewski M, Loffing J, Ikeda M, Mickle JE, et al. (February 2002). "A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression". The Journal of Biological Chemistry. 277 (5): 3520–9. doi:10.1074/jbc.M110177200. PMID 11707463.
- Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, et al. (February 2002). "Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform". The Journal of Cell Biology. 156 (4): 653–64. doi:10.1083/jcb.200110081. PMC 2174079. PMID 11839770.
- Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J, Proux-Gillardeaux V, et al. (July 2003). "A dual mechanism controlling the localization and function of exocytic v-SNAREs". Proceedings of the National Academy of Sciences of the United States of America. 100 (15): 9011–6. Bibcode:2003PNAS..100.9011M. doi:10.1073/pnas.1431910100. PMC 166429. PMID 12853575.
- Kim BY, Ueda M, Kominami E, Akagawa K, Kohsaka S, Akazawa C (November 2003). "Identification of mouse Vps16 and biochemical characterization of mammalian class C Vps complex". Biochemical and Biophysical Research Communications. 311 (3): 577–82. doi:10.1016/j.bbrc.2003.10.030. PMID 14623309.
- Huynh H, Bottini N, Williams S, Cherepanov V, Musumeci L, Saito K, et al. (September 2004). "Control of vesicle fusion by a tyrosine phosphatase". Nature Cell Biology. 6 (9): 831–9. doi:10.1038/ncb1164. PMID 15322554. S2CID 25311826.
External links