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STX6

From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens
STX6
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

2NPS,4J2C

Identifiers
AliasesSTX6, syntaxin 6
External IDsOMIM:603944;MGI:1926235;HomoloGene:115622;GeneCards:STX6;OMA:STX6 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for STX6
Genomic location for STX6
Band1q25.3Start180,972,712bp[1]
End181,023,121bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for STX6
Genomic location for STX6
Band1|1 G3Start155,034,461bp[2]
End155,084,002bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
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
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
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
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 MbChr 1: 155.03 – 155.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Syntaxin-6 is aprotein that in humans is encoded by theSTX6gene.[5][6]

Interactions

[edit]

STX6 has been shown tointeract withSNAP23,[7]VAMP3[8] andVAMP4.[8]

N terminal protein domain

[edit]

Theprotein domainSyntaxin 6 N terminal protein domain is a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) found in endosomal transportvesicles. 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 calledcell trafficking. Its SNARE motif shows significanthomology to both syntaxin 1a and S25C, indicating similarity throughevolutionary conservation. Thestructure of the syntaxin 6N-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 theenergetic 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

[edit]

Members of this entry, which are found in theamino terminus of various SNARE proteins, adopt astructure consisting of anantiparallel three-helix bundle. Their exact function has not been determined, though it is known that theyregulate the SNARE motif, as well as mediate variousprotein-protein interactions involved in membrane-transport.[10]

Function

[edit]

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 afour-helix bundle that contributes to the fusion of two membranes. More specifically, the N-terminal domain bindsto 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

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000135823Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000026470Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^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.
  6. ^"Entrez Gene: STX6 syntaxin 6".
  7. ^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.
  8. ^abMallard 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.
  9. ^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.
  10. ^abMisura 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

[edit]

External links

[edit]
Synaptic vesicle
SNARE
Q-SNARE
R-SNARE
Synaptotagmin
Other
COPI
COPII
RME/Clathrin
Caveolae
Other/ungrouped
Vesicle formation
Adaptor protein complex 1:
Adaptor protein complex 2:
Adaptor protein complex 3:
Adaptor protein complex 4:
BLOC-1:
BLOC-2:
BLOC-3:
Coats:
Small GTPase
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