STX1A

STX1A
Identifikatori
Aliasi	STX1A
Vanjski ID-jevi	OMIM: 186590 MGI: 109355 HomoloGene: 37941 GeneCards: STX1A
Lokacija gena (čovjek)
Hrom.	Hromosom 7 (čovjek)
Kraj	73,719,672 bp
Lokacija gena (miš)
Hrom.	Hromosom 5 (miš)
Kraj	135,079,954 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• calcium channel inhibitor activity; • transmembrane transporter binding; • protein N-terminus binding; • SNAP receptor activity; • kinase binding; • chloride channel inhibitor activity; • protein heterodimerization activity; • SNARE binding; • GO:0001948, GO:0016582 vezivanje za proteine; • myosin binding; • protein domain specific binding; • protein-macromolecule adaptor activity; • myosin head/neck binding; • ATP-dependent protein binding; • calcium-dependent protein binding;
Ćelijska komponenta	• integral component of membrane; • citosol; • membrana; • Sinapsna vezikula; • synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; • voltage-gated potassium channel complex; • ćelijska membrana; • sinapsa; • synaptic vesicle membrane; • secretory granule; • extracellular region; • synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; • međućelijske veze; • SNARE complex; • intracellular organelle; • neuron projection; • synaptobrevin 2-SNAP-25-syntaxin-1a complex; • actomyosin; • GO:0016023 citoplazmatska vezikula; • presynaptic membrane; • GO:0097483, GO:0097481 postsynaptic density; • presynaptic active zone membrane; • Jedarna membrana; • integral component of plasma membrane; • Akson; • GO:0009327 makromolekulani kompleks; • Akrozom; • integral component of synaptic vesicle membrane; • glutamatergic synapse; • integral component of presynaptic membrane; • Endomembranski sistem; • intracellular anatomical structure;
Biološki proces	• Egzocitoza; • positive regulation of norepinephrine secretion; • synaptic vesicle docking; • secretion by cell; • regulation of insulin secretion; • positive regulation of catecholamine secretion; • positive regulation of neurotransmitter secretion; • positive regulation of calcium ion-dependent exocytosis; • regulation of exocytosis; • response to gravity; • vesicle docking; • positive regulation of excitatory postsynaptic potential; • positive regulation of exocytosis; • intracellular protein transport; • neurotransmitter transport; • vesicle-mediated transport; • calcium-ion regulated exocytosis; • regulation of synaptic vesicle priming; • protein localization to membrane; • modulation of excitatory postsynaptic potential; • synaptic vesicle fusion to presynaptic active zone membrane; • SNARE complex assembly; • cytokine-mediated signaling pathway; • synaptic vesicle exocytosis; • Fuzija vezikula; • GO:0010554 neurotransmitter secretion; • glutamate secretion; • protein sumoylation; • insulin secretion; • regulated exocytosis; • hormone secretion; • synaptic vesicle endocytosis; • membrane fusion;
	Izvori:Amigo / QuickGO
Ortolozi
	6804
	20907
	ENSG00000106089
	ENSMUSG00000007207
	Q16623; Q75ME0
	O35526
	NM_001165903; NM_004603
	NM_016801; NM_001359179
	NP_001159375; NP_004594; NP_004594.1
	NP_058081; NP_001346108
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Sintaksin-1A jest protein koji je kod ljudi kodiran genom STX1A sa hromosoma 7.^[5]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 288 aminokiselina, a molekulska težina 33.023 Da ^[6]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MKDRTQELRT	AKDSDDDDDV	AVTVDRDRFM	DEFFEQVEEI	RGFIDKIAEN
VEEVKRKHSA	ILASPNPDEK	TKEELEELMS	DIKKTANKVR	SKLKSIEQSI
EQEEGLNRSS	ADLRIRKTQH	STLSRKFVEV	MSEYNATQSD	YRERCKGRIQ
RQLEITGRTT	TSEELEDMLE	SGNPAIFASG	IIMDSSISKQ	ALSEIETRHS
EIIKLENSIR	ELHDMFMDMA	MLVESQGEMI	DRIEYNVEHA	VDYVERAVSD
TKKAVKYQSK	ARRKKIMIII	CCVILGIVIA	STVGGIFA

Funkcija

Sinapsne vezikule skladište neurotransmiter koji se oslobađa tokom kalcijem regulisane egzocitoze. Specifičnost oslobađanja neurotransmitera zahteva lokalizaciju sinapsnih vezikula i kalcijskih kanala u aktivnu presinapsnu zonu. Sintaksini funkcionišu u ovom procesu fuzije vezikula.

Sintaksin-1A je član natšprodice sintaksin. Sintaksini su proteini specifični za nervni sistem uključeni u spajanje sinapsnih vezikula sa presinapsnom plazmamembranom. Sintaksini posjeduju jedan C-terminalni transmembranski domen, SNARE (Soluble NSF N-etilmaleimid-sensitive fuzion protein)-Attachment protein Receptor) domen (poznat kao H3), i N-terminalni regulatorni domen (Habc). Sintaksini se vezuju za sinaptotagmin na način ovisan o kalciju i stupaju u interakciju sa naponskim zavisnim kalcijevim i kalijevim kanalima preko C-terminalnog H3 domena. Sintaksin-1A je ključni protein u regulaciji ionskih kanala i sinapsnoj egzocitozi.^[7]

Klinički značaj

Sintaksini služe kao supstrat za botulinumski neurotoksin tipa C, metaloproteazu koja blokira egzocitozu i ima visok afinitet za molekulski kompleks koji uključuje alfa-latrotoksinski receptor koji proizvodi eksplozivnu egzocitozu.^[8]

Nivo ekspresije STX1A je u direktnoj korelaciji sa inteligencijom u Williamsovom sindromu.^[9]

Interaktivna mapa puta

Šablon:NicotineDopaminergicActivity WP1602

Interakcije

Pokazalo se da STX1A reaguje sa:

CPLX1,^[10]^[11]^[12]
CFTR,^[13]^[14]
NAPA,^[15]^[16]
RNF40,^[17]
SCNN1G,^[18]
SLC6A1,^[19]^[20]^[21]
SNAP-25,^[10]^[11]^[15]^[22]^[23]^[24]^[25]^[26]^[27]^[28]^[29]
SNAP23,^[27]^[29]^[30]^[31]^[32]
STXBP1,^[10]^[15]^[23]^[33]^[34]
STXBP5,^[35]^[36]
SYT1^[37]^[38]
UNC13B,^[39]
VAMP2,^[10]^[11]^[15]^[34]^[40]^[41] i
VAMP8.^[42]

Također pogledajte

Sintaksin

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000106089 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000007207 - Ensembl, maj 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.
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^ "UniProt, Q16623" (jezik: engleski). Pristupljeno 12. 4. 2022.
^ "Entrez Gene: STX1A syntaxin 1A (brain)".
^ Zhang R, Maksymowych AB, Simpson LL (juli 1995). "Cloning and sequence analysis of a cDNA encoding human syntaxin 1A, a polypeptide essential for exocytosis". Gene. 159 (2): 293–4. doi:10.1016/0378-1119(95)00152-V. PMID 7622072.
^
Gao MC, Bellugi U, Dai L, Mills DL, Sobel EM, Lange K, Korenberg JR (2010). Toland AE (ured.). "Intelligence in Williams Syndrome is related to STX1A, which encodes a component of the presynaptic SNARE complex". PLOS ONE. 5 (4): e10292. Bibcode:2010PLoSO...510292G. doi:10.1371/journal.pone.0010292. PMC 2858212. PMID 20422020.
- Brian Maffly (22. 4. 2010). "U. scientist links one gene to intelligence". The Salt Lake Tribune. Arhivirano s originala, 25. 4. 2010.
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^ Naren AP, Nelson DJ, Xie W, Jovov B, Pevsner J, Bennett MK, Benos DJ, Quick MW, Kirk KL (novembar 1997). "Regulation of CFTR chloride channels by syntaxin and Munc18 isoforms". Nature. 390 (6657): 302–5. Bibcode:1997Natur.390..302N. doi:10.1038/36882. PMID 9384384. S2CID 4395005.
^ Cormet-Boyaka E, Di A, Chang SY, Naren AP, Tousson A, Nelson DJ, Kirk KL (septembar 2002). "CFTR chloride channels are regulated by a SNAP-23/syntaxin 1A complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (19): 12477–82. Bibcode:2002PNAS...9912477C. doi:10.1073/pnas.192203899. PMC 129470. PMID 12209004.
^ ^a ^b ^c ^d McMahon HT, Missler M, Li C, Südhof TC (oktobar 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell. 83 (1): 111–9. doi:10.1016/0092-8674(95)90239-2. PMID 7553862. S2CID 675343.
^ Hanson PI, Otto H, Barton N, Jahn R (juli 1995). "The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin". The Journal of Biological Chemistry. 270 (28): 16955–61. doi:10.1074/jbc.270.28.16955. PMID 7622514.
^ Chin LS, Vavalle JP, Li L (septembar 2002). "Staring, a novel E3 ubiquitin-protein ligase that targets syntaxin 1 for degradation". The Journal of Biological Chemistry. 277 (38): 35071–9. doi:10.1074/jbc.M203300200. PMID 12121982.
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^ Quick MW (april 2002). "Substrates regulate gamma-aminobutyric acid transporters in a syntaxin 1A-dependent manner". Proceedings of the National Academy of Sciences of the United States of America. 99 (8): 5686–91. Bibcode:2002PNAS...99.5686Q. doi:10.1073/pnas.082712899. PMC 122832. PMID 11960023.
^ Deken SL, Beckman ML, Boos L, Quick MW (oktobar 2000). "Transport rates of GABA transporters: regulation by the N-terminal domain and syntaxin 1A". Nature Neuroscience. 3 (10): 998–1003. doi:10.1038/79939. PMID 11017172. S2CID 11312913.
^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (septembar 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
^ ^a ^b Hata Y, Südhof TC (juni 1995). "A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic". The Journal of Biological Chemistry. 270 (22): 13022–8. doi:10.1074/jbc.270.22.13022. PMID 7768895.
^ Gonelle-Gispert C, Molinete M, Halban PA, Sadoul K (septembar 2000). "Membrane localization and biological activity of SNAP-25 cysteine mutants in insulin-secreting cells". Journal of Cell Science. 113 ( Pt 18) (18): 3197–205. doi:10.1242/jcs.113.18.3197. PMID 10954418.
^ Ilardi JM, Mochida S, Sheng ZH (februar 1999). "Snapin: a SNARE-associated protein implicated in synaptic transmission". Nature Neuroscience. 2 (2): 119–24. doi:10.1038/5673. PMID 10195194. S2CID 25524692.
^ Li Y, Chin LS, Weigel C, Li L (novembar 2001). "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". The Journal of Biological Chemistry. 276 (44): 40824–33. doi:10.1074/jbc.M106141200. PMID 11524423.
^ ^a ^b Ravichandran V, Chawla A, Roche PA (juni 1996). "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues". The Journal of Biological Chemistry. 271 (23): 13300–3. doi:10.1074/jbc.271.23.13300. PMID 8663154.
^ Chapman ER, An S, Barton N, Jahn R (novembar 1994). "SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils". The Journal of Biological Chemistry. 269 (44): 27427–32. doi:10.1016/S0021-9258(18)47003-2. PMID 7961655.
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^ Imai A, Nashida T, Yoshie S, Shimomura H (august 2003). "Intracellular localisation of SNARE proteins in rat parotid acinar cells: SNARE complexes on the apical plasma membrane". Archives of Oral Biology. 48 (8): 597–604. doi:10.1016/S0003-9969(03)00116-X. PMID 12828989.
^ Li G, Alexander EA, Schwartz JH (maj 2003). "Syntaxin isoform specificity in the regulation of renal H+-ATPase exocytosis". The Journal of Biological Chemistry. 278 (22): 19791–7. doi:10.1074/jbc.M212250200. PMID 12651853.
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^ ^a ^b Pérez-Brangulí F, Muhaisen A, Blasi J (juni 2002). "Munc 18a binding to syntaxin 1A and 1B isoforms defines its localization at the plasma membrane and blocks SNARE assembly in a three-hybrid system assay". Molecular and Cellular Neurosciences. 20 (2): 169–80. doi:10.1006/mcne.2002.1122. PMID 12093152. S2CID 23927545.
^ Widberg CH, Bryant NJ, Girotti M, Rea S, James DE (septembar 2003). "Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation". The Journal of Biological Chemistry. 278 (37): 35093–101. doi:10.1074/jbc.M304261200. PMID 12832401.
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^ Shao X, Li C, Fernandez I, Zhang X, Südhof TC, Rizo J (januar 1997). "Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch". Neuron. 18 (1): 133–42. doi:10.1016/S0896-6273(01)80052-0. PMID 9010211. S2CID 17947552.
^ Thomas DM, Ferguson GD, Herschman HR, Elferink LA (juli 1999). "Functional and biochemical analysis of the C2 domains of synaptotagmin IV". Molecular Biology of the Cell. 10 (7): 2285–95. doi:10.1091/mbc.10.7.2285. PMC 25443. PMID 10397765.
^ Betz A, Okamoto M, Benseler F, Brose N (januar 1997). "Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin". The Journal of Biological Chemistry. 272 (4): 2520–6. doi:10.1074/jbc.272.4.2520. PMID 8999968.
^ Margittai M, Otto H, Jahn R (mart 1999). "A stable interaction between syntaxin 1a and synaptobrevin 2 mediated by their transmembrane domains". FEBS Letters. 446 (1): 40–4. doi:10.1016/S0014-5793(99)00028-9. PMID 10100611. S2CID 9115709.
^ Hao JC, Salem N, Peng XR, Kelly RB, Bennett MK (mart 1997). "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes". The Journal of Neuroscience. 17 (5): 1596–603. doi:10.1523/JNEUROSCI.17-05-01596.1997. PMC 6573372. PMID 9030619.
^ Nagamatsu S, Nakamichi Y, Watanabe T, Matsushima S, Yamaguchi S, Ni J, Itagaki E, Ishida H (januar 2001). "Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules". Journal of Cell Science. 114 (Pt 1): 219–227. doi:10.1242/jcs.114.1.219. PMID 11112705.

Dopunska literatura

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McMahon HT, Missler M, Li C, Südhof TC (oktobar 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell. 83 (1): 111–9. doi:10.1016/0092-8674(95)90239-2. PMID 7553862. S2CID 675343.
Zhang R, Maksymowych AB, Simpson LL (juli 1995). "Cloning and sequence analysis of a cDNA encoding human syntaxin 1A, a polypeptide essential for exocytosis". Gene. 159 (2): 293–4. doi:10.1016/0378-1119(95)00152-V. PMID 7622072.
Hanson PI, Otto H, Barton N, Jahn R (juli 1995). "The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin". The Journal of Biological Chemistry. 270 (28): 16955–61. doi:10.1074/jbc.270.28.16955. PMID 7622514.
Hata Y, Südhof TC (juni 1995). "A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic". The Journal of Biological Chemistry. 270 (22): 13022–8. doi:10.1074/jbc.270.22.13022. PMID 7768895.
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Vanjski linkovi

P32851

Šablon:Proteini vezikulskog transporta Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000106089 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000007207 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

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