ID STX1A_MOUSE Reviewed; 288 AA.
AC O35526;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 3.
DT 27-MAR-2024, entry version 201.
DE RecName: Full=Syntaxin-1A;
DE AltName: Full=Neuron-specific antigen HPC-1;
GN Name=Stx1a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Fujiwara T., Genda M., Nagai A., Okazaki M., Watanabe T., Nagamatsu S.,
RA Akagawa K.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 29-41; 47-56; 58-84; 95-108; 126-142; 152-158 AND
RP 233-246, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP INTERACTION WITH SYTL4.
RX PubMed=12101244; DOI=10.1128/mcb.22.15.5518-5526.2002;
RA Torii S., Zhao S., Yi Z., Takeuchi T., Izumi T.;
RT "Granuphilin modulates the exocytosis of secretory granules through
RT interaction with syntaxin 1a.";
RL Mol. Cell. Biol. 22:5518-5526(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH SYT6 AND SYT8.
RX PubMed=15774481; DOI=10.1074/jbc.m412920200;
RA Hutt D.M., Baltz J.M., Ngsee J.K.;
RT "Synaptotagmin VI and VIII and syntaxin 2 are essential for the mouse sperm
RT acrosome reaction.";
RL J. Biol. Chem. 280:20197-20203(2005).
RN [5]
RP INTERACTION WITH OTOF.
RC STRAIN=BALB/cJ; TISSUE=Cochlea;
RX PubMed=17055430; DOI=10.1016/j.cell.2006.08.040;
RA Roux I., Safieddine S., Nouvian R., Grati M., Simmler M.-C., Bahloul A.,
RA Perfettini I., Le Gall M., Rostaing P., Hamard G., Triller A., Avan P.,
RA Moser T., Petit C.;
RT "Otoferlin, defective in a human deafness form, is essential for exocytosis
RT at the auditory ribbon synapse.";
RL Cell 127:277-289(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17502420; DOI=10.1083/jcb.200608132;
RA Ohara-Imaizumi M., Fujiwara T., Nakamichi Y., Okamura T., Akimoto Y.,
RA Kawai J., Matsushima S., Kawakami H., Watanabe T., Akagawa K.,
RA Nagamatsu S.;
RT "Imaging analysis reveals mechanistic differences between first- and
RT second-phase insulin exocytosis.";
RL J. Cell Biol. 177:695-705(2007).
RN [8]
RP INTERACTION WITH SEPTIN4 AND SEPTIN5, AND TISSUE SPECIFICITY.
RX PubMed=17296554; DOI=10.1016/j.neuron.2007.01.019;
RA Ihara M., Yamasaki N., Hagiwara A., Tanigaki A., Kitano A., Hikawa R.,
RA Tomimoto H., Noda M., Takanashi M., Mori H., Hattori N., Miyakawa T.,
RA Kinoshita M.;
RT "Sept4, a component of presynaptic scaffold and Lewy bodies, is required
RT for the suppression of alpha-synuclein neurotoxicity.";
RL Neuron 53:519-533(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH LGI3.
RX PubMed=18760330; DOI=10.1016/j.neulet.2008.08.044;
RA Park W.-J., Lee S.E., Kwon N.S., Baek K.J., Kim D.-S., Yun H.-Y.;
RT "Leucine-rich glioma inactivated 3 associates with syntaxin 1.";
RL Neurosci. Lett. 444:240-244(2008).
RN [10]
RP INTERACTION WITH VAMP2.
RX PubMed=19196426; DOI=10.1111/j.1471-4159.2008.05849.x;
RA Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I.,
RA Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., Nagata K.;
RT "Sept8 controls the binding of vesicle-associated membrane protein 2 to
RT synaptophysin.";
RL J. Neurochem. 108:867-880(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH STXBP5L.
RX PubMed=21998599; DOI=10.1371/journal.pgen.1002323;
RA Bhatnagar S., Oler A.T., Rabaglia M.E., Stapleton D.S., Schueler K.L.,
RA Truchan N.A., Worzella S.L., Stoehr J.P., Clee S.M., Yandell B.S.,
RA Keller M.P., Thurmond D.C., Attie A.D.;
RT "Positional cloning of a type 2 diabetes quantitative trait locus; tomosyn-
RT 2, a negative regulator of insulin secretion.";
RL PLoS Genet. 7:E1002323-E1002323(2011).
RN [13]
RP INTERACTION WITH STXBP1.
RX PubMed=21445306; DOI=10.1371/journal.pone.0017999;
RA Graham M.E., Prescott G.R., Johnson J.R., Jones M., Walmesley A.,
RA Haynes L.P., Morgan A., Burgoyne R.D., Barclay J.W.;
RT "Structure-function study of mammalian Munc18-1 and C. elegans UNC-18
RT implicates domain 3b in the regulation of exocytosis.";
RL PLoS ONE 6:e17999-e17999(2011).
RN [14]
RP INTERACTION WITH PLCL1.
RX PubMed=23341457; DOI=10.1074/jbc.m112.419317;
RA Zhang Z., Takeuchi H., Gao J., Wang D., James D.J., Martin T.F., Hirata M.;
RT "PRIP (phospholipase C-related but catalytically inactive protein) inhibits
RT exocytosis by direct interactions with syntaxin 1 and SNAP-25 through its
RT C2 domain.";
RL J. Biol. Chem. 288:7769-7780(2013).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28596237; DOI=10.2337/db16-1403;
RA Wheeler S.E., Stacey H.M., Nahaei Y., Hale S.J., Hardy A.B., Reimann F.,
RA Gribble F.M., Larraufie P., Gaisano H.Y., Brubaker P.L.;
RT "The SNARE protein syntaxin-1a Plays an essential role in biphasic
RT exocytosis of the incretin hormone glucagon-like peptide 1.";
RL Diabetes 66:2327-2338(2017).
RN [16]
RP FUNCTION, INTERACTION WITH VAMP2; VAMP8; SNAP23; SNAP25 AND STXBP1, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=28031464; DOI=10.1074/jbc.m116.769885;
RA Liang T., Qin T., Xie L., Dolai S., Zhu D., Prentice K.J., Wheeler M.,
RA Kang Y., Osborne L., Gaisano H.Y.;
RT "New Roles of Syntaxin-1A in Insulin Granule Exocytosis and
RT Replenishment.";
RL J. Biol. Chem. 292:2203-2216(2017).
RN [17]
RP IDENTIFICATION IN THE SNARE COMPLEX, AND INTERACTION WITH STXBP1.
RX PubMed=28821673; DOI=10.1523/jneurosci.0338-17.2017;
RA Park S., Bin N.R., Yu B., Wong R., Sitarska E., Sugita K., Ma K., Xu J.,
RA Tien C.W., Algouneh A., Turlova E., Wang S., Siriya P., Shahid W.,
RA Kalia L., Feng Z.P., Monnier P.P., Sun H.S., Zhen M., Gao S., Rizo J.,
RA Sugita S.;
RT "UNC-18 and Tomosyn Antagonistically Control Synaptic Vesicle Priming
RT Downstream of UNC-13 in Caenorhabditis elegans.";
RL J. Neurosci. 37:8797-8815(2017).
RN [18]
RP INTERACTION WITH PRRT2.
RX PubMed=29056747; DOI=10.1038/cr.2017.128;
RA Tan G.H., Liu Y.Y., Wang L., Li K., Zhang Z.Q., Li H.F., Yang Z.F., Li Y.,
RA Li D., Wu M.Y., Yu C.L., Long J.J., Chen R.C., Li L.X., Yin L.P., Liu J.W.,
RA Cheng X.W., Shen Q., Shu Y.S., Sakimura K., Liao L.J., Wu Z.Y., Xiong Z.Q.;
RT "PRRT2 deficiency induces paroxysmal kinesigenic dyskinesia by regulating
RT synaptic transmission in cerebellum.";
RL Cell Res. 28:90-110(2018).
CC -!- FUNCTION: Plays an essential role in hormone and neurotransmitter
CC calcium-dependent exocytosis and endocytosis (PubMed:17502420,
CC PubMed:28596237, PubMed:28031464). Part of the SNARE (Soluble NSF
CC Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which
CC mediates the fusion of synaptic vesicles with the presynaptic plasma
CC membrane. STX1A and SNAP25 are localized on the plasma membrane while
CC VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs
CC from the N-terminal SNARE motifs to the C-terminal anchors leads to the
CC formation of the SNARE complex, which brings membranes into close
CC proximity and results in final fusion. Participates in the calcium-
CC dependent regulation of acrosomal exocytosis in sperm
CC (PubMed:12101244). Also plays an important role in the exocytosis of
CC hormones such as insulin or glucagon-like peptide 1 (GLP-1)
CC (PubMed:17502420, PubMed:28596237, PubMed:28031464).
CC {ECO:0000269|PubMed:12101244, ECO:0000269|PubMed:17502420,
CC ECO:0000269|PubMed:28031464, ECO:0000269|PubMed:28596237}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A; this complex constitutes the basic catalytic machinery of the
CC complex neurotransmitter release apparatus (PubMed:28031464,
CC PubMed:19196426, PubMed:28821673). The SNARE complex interacts with
CC CPLX1 (By similarity). Interacts with STXBP1 (PubMed:28031464,
CC PubMed:21445306, PubMed:28821673). The interaction with STXBP1 promotes
CC assembly of the SNARE complex (PubMed:28821673). Interacts (via C-
CC terminus) with KCNB1 (via C-terminus); the interaction increases in a
CC calcium-dependent manner and induces a pore-independent enhancement of
CC exocytosis in neuroendocrine cells, chromaffin cells, pancreatic beta
CC cells and from the soma of dorsal root ganglia (DRG) neurons (By
CC similarity). Interacts with SYTL4 (PubMed:12101244). Interacts with
CC STXBP6 (By similarity). Interacts with PLCL1 (via C2 domain)
CC (PubMed:23341457). Interacts with OTOF (PubMed:17055430). Interacts
CC with LGI3 (PubMed:18760330). Interacts (via the H3 domain) with SLC6A4
CC (via the N-terminus); this interaction regulates SLC4A6 channel
CC conductance in thalamocortical neurons (By similarity). Interacts with
CC SYT6 and SYT8; the interaction is Ca(2+)-dependent (PubMed:15774481).
CC Interacts with VAMP8 (PubMed:28031464). Interacts with SNAP23
CC (PubMed:28031464). Interacts with VAPA and SYBU (By similarity).
CC Interacts with PRRT2 (PubMed:29056747). Interacts with SEPT8 (By
CC similarity). Interacts with STXBP5L (PubMed:21998599). Interacts with
CC synaptotagmin-1/SYT1 (By similarity).Interacts with SEPTIN5; in the
CC cerebellar cortex (PubMed:17296554). Interacts with SEPTIN4; in the
CC striatum (PubMed:17296554). {ECO:0000250|UniProtKB:P32851,
CC ECO:0000250|UniProtKB:Q16623, ECO:0000269|PubMed:12101244,
CC ECO:0000269|PubMed:15774481, ECO:0000269|PubMed:17055430,
CC ECO:0000269|PubMed:17296554, ECO:0000269|PubMed:18760330,
CC ECO:0000269|PubMed:19196426, ECO:0000269|PubMed:21445306,
CC ECO:0000269|PubMed:21998599, ECO:0000269|PubMed:23341457,
CC ECO:0000269|PubMed:28031464, ECO:0000269|PubMed:28821673,
CC ECO:0000269|PubMed:29056747}.
CC -!- INTERACTION:
CC O35526; O08547: Sec22b; NbExp=4; IntAct=EBI-400878, EBI-8400083;
CC O35526; P60879: Snap25; NbExp=4; IntAct=EBI-400878, EBI-445270;
CC O35526; P46097: Syt2; NbExp=2; IntAct=EBI-400878, EBI-457969;
CC O35526; P21707: Syt1; Xeno; NbExp=3; IntAct=EBI-400878, EBI-458098;
CC O35526; Q62747: Syt7; Xeno; NbExp=2; IntAct=EBI-400878, EBI-16179541;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:18760330}; Single-pass type IV
CC membrane protein {ECO:0000269|PubMed:18760330}. Synapse, synaptosome
CC {ECO:0000269|PubMed:18760330}. Cell membrane
CC {ECO:0000250|UniProtKB:P32851}. Note=Colocalizes with KCNB1 at the cell
CC membrane. {ECO:0000250|UniProtKB:P32851}.
CC -!- TISSUE SPECIFICITY: Expressed in the striatum (at protein level)
CC (PubMed:17296554). Expressed in the ileum (PubMed:28596237).
CC {ECO:0000269|PubMed:17296554, ECO:0000269|PubMed:28596237}.
CC -!- PTM: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1
CC significantly decreases its interaction with STXBP1 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by CK2 (By similarity). Phosphorylation at Ser-188
CC by DAPK1 significantly decreases its interaction with STXBP1 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16623}.
CC -!- PTM: Sumoylated, sumoylation is required for regulation of synaptic
CC vesicle endocytosis. {ECO:0000250|UniProtKB:Q16623}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show impaired glucose tolerance
CC without any marked hyperglycemia. {ECO:0000269|PubMed:17502420,
CC ECO:0000269|PubMed:28031464, ECO:0000269|PubMed:28596237}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D45208; BAA28865.2; -; mRNA.
DR CCDS; CCDS19731.1; -.
DR RefSeq; NP_058081.2; NM_016801.4.
DR AlphaFoldDB; O35526; -.
DR BMRB; O35526; -.
DR SMR; O35526; -.
DR BioGRID; 203561; 33.
DR CORUM; O35526; -.
DR DIP; DIP-31950N; -.
DR IntAct; O35526; 20.
DR MINT; O35526; -.
DR STRING; 10090.ENSMUSP00000005509; -.
DR GlyGen; O35526; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O35526; -.
DR MetOSite; O35526; -.
DR PhosphoSitePlus; O35526; -.
DR SwissPalm; O35526; -.
DR PaxDb; 10090-ENSMUSP00000005509; -.
DR PeptideAtlas; O35526; -.
DR ProteomicsDB; 258768; -.
DR Antibodypedia; 3644; 783 antibodies from 45 providers.
DR DNASU; 20907; -.
DR Ensembl; ENSMUST00000005509.11; ENSMUSP00000005509.5; ENSMUSG00000007207.11.
DR GeneID; 20907; -.
DR KEGG; mmu:20907; -.
DR UCSC; uc008zxk.1; mouse.
DR AGR; MGI:109355; -.
DR CTD; 6804; -.
DR MGI; MGI:109355; Stx1a.
DR VEuPathDB; HostDB:ENSMUSG00000007207; -.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; O35526; -.
DR OMA; RWICFIL; -.
DR OrthoDB; 2876074at2759; -.
DR PhylomeDB; O35526; -.
DR TreeFam; TF313763; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
DR Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR BioGRID-ORCS; 20907; 3 hits in 80 CRISPR screens.
DR ChiTaRS; Stx1a; mouse.
DR PRO; PR:O35526; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O35526; Protein.
DR Bgee; ENSMUSG00000007207; Expressed in barrel cortex and 217 other cell types or tissues.
DR ExpressionAtlas; O35526; baseline and differential.
DR Genevisible; O35526; MM.
DR GO; GO:0001669; C:acrosomal vesicle; EXP:MGI.
DR GO; GO:0042641; C:actomyosin; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:SynGO-UCL.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:SynGO-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IDA:MGI.
DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; ISO:MGI.
DR GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0043008; F:ATP-dependent protein binding; ISO:MGI.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IMP:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0017022; F:myosin binding; ISO:MGI.
DR GO; GO:0032028; F:myosin head/neck binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IDA:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0046879; P:hormone secretion; IMP:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR GO; GO:0033605; P:positive regulation of catecholamine secretion; ISS:UniProtKB.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IGI:ParkinsonsUK-UCL.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IGI:ParkinsonsUK-UCL.
DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; ISS:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; ISO:MGI.
DR GO; GO:0016925; P:protein sumoylation; ISO:MGI.
DR GO; GO:0045055; P:regulated exocytosis; IMP:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:MGI.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IGI:ParkinsonsUK-UCL.
DR GO; GO:0009629; P:response to gravity; ISO:MGI.
DR GO; GO:0032940; P:secretion by cell; ISO:MGI.
DR GO; GO:0035493; P:SNARE complex assembly; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0048278; P:vesicle docking; IMP:UniProtKB.
DR CDD; cd15880; SNARE_syntaxin1; 1.
DR CDD; cd00179; SynN; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; SYNTAXIN; 1.
DR PANTHER; PTHR19957:SF84; SYNTAXIN-1A; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasmic vesicle; Direct protein sequencing;
KW Exocytosis; Isopeptide bond; Membrane; Neurotransmitter transport;
KW Phosphoprotein; Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..288
FT /note="Syntaxin-1A"
FT /id="PRO_0000210187"
FT TOPO_DOM 1..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 192..254
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..109
FT /evidence="ECO:0000255"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32851"
FT MOD_RES 188
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
SQ SEQUENCE 288 AA; 33054 MW; 8F8255F2EEF886CA CRC64;
MKDRTQELRT AKDSDDDDDV TVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA
ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH
STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG
IIMDSSISKQ ALSEIETRHS EIIKLETSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHA
VDYVERAVSD TKKAVKYQSK ARRKKIMIII CCVILGIIIA STIGGIFG
//
