STX1A_RAT
ID STX1A_RAT Reviewed; 288 AA.
AC P32851;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Syntaxin-1A;
DE AltName: Full=Neuron-specific antigen HPC-1;
DE AltName: Full=Synaptotagmin-associated 35 kDa protein;
DE Short=P35A;
GN Name=Stx1a; Synonyms=Sap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 8-37 AND 44-102.
RC TISSUE=Brain;
RX PubMed=1587842; DOI=10.1016/s0021-9258(19)50061-8;
RA Inoue A., Obata K., Akagawa K.;
RT "Cloning and sequence analysis of cDNA for a neuronal cell membrane
RT antigen, HPC-1.";
RL J. Biol. Chem. 267:10613-10619(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-288, AND PROTEIN SEQUENCE OF 1-15 AND
RP 95-113.
RC TISSUE=Brain;
RX PubMed=1334074; DOI=10.1016/s0021-9258(19)73984-2;
RA Yoshida A., Oho C., Omori A., Kuwahara R., Ito T., Takahashi M.;
RT "HPC-1 is associated with synaptotagmin and omega-conotoxin receptor.";
RL J. Biol. Chem. 267:24925-24928(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-288, AND PROTEIN SEQUENCE OF 4-16 AND
RP 31-56.
RC TISSUE=Brain;
RX PubMed=1321498; DOI=10.1126/science.1321498;
RA Bennett M.K., Calakos N., Scheller R.H.;
RT "Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at
RT presynaptic active zones.";
RL Science 257:255-259(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7690687; DOI=10.1016/0092-8674(93)90466-4;
RA Bennett M.K., Garcia-Arraras J.E., Elferink L.A., Peterson K.E.,
RA Fleming A.M., Hazuka C.D., Scheller R.H.;
RT "The syntaxin family of vesicular transport receptors.";
RL Cell 74:863-873(1993).
RN [5]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM
RP NEUROTOXIN TYPE C.
RX PubMed=7901002; DOI=10.1002/j.1460-2075.1993.tb06171.x;
RA Blasi J., Chapman E.R., Yamasaki S., Binz T., Niemann H., Jahn R.;
RT "Botulinum neurotoxin C1 blocks neurotransmitter release by means of
RT cleaving HPC-1/syntaxin.";
RL EMBO J. 12:4821-4828(1993).
RN [6]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM
RP NEUROTOXIN TYPE C.
RX PubMed=7737992; DOI=10.1074/jbc.270.18.10566;
RA Schiavo G., Shone C.C., Bennett M.K., Scheller R.H., Montecucco C.;
RT "Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the
RT carboxyl-terminal region of syntaxins.";
RL J. Biol. Chem. 270:10566-10570(1995).
RN [7]
RP INTERACTION WITH SNAP23.
RX PubMed=9507000; DOI=10.1074/jbc.273.12.6944;
RA Tang B.L., Tan A.E., Lim L.K., Lee S.S., Low D.Y., Hong W.;
RT "Syntaxin 12, a member of the syntaxin family localized to the endosome.";
RL J. Biol. Chem. 273:6944-6950(1998).
RN [8]
RP IDENTIFICATION IN A TERNARY COMPLEX WITH VAMP8 AND SNAP25.
RX PubMed=10336434; DOI=10.1074/jbc.274.22.15440;
RA Fasshauer D., Antonin W., Margittai M., Pabst S., Jahn R.;
RT "Mixed and non-cognate SNARE complexes. Characterization of assembly and
RT biophysical properties.";
RL J. Biol. Chem. 274:15440-15446(1999).
RN [9]
RP INTERACTION WITH SLC6A4.
RX PubMed=11709063; DOI=10.1042/0300-5127:0290722;
RA Haase J., Killian A.M., Magnani F., Williams C.;
RT "Regulation of the serotonin transporter by interacting proteins.";
RL Biochem. Soc. Trans. 29:722-728(2001).
RN [10]
RP INTERACTION WITH STXBP6.
RX PubMed=12145319; DOI=10.1074/jbc.m204929200;
RA Scales S.J., Hesser B.A., Masuda E.S., Scheller R.H.;
RT "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex
RT assembly.";
RL J. Biol. Chem. 277:28271-28279(2002).
RN [11]
RP PHOSPHORYLATION AT SER-188, AND INTERACTION WITH STXBP1.
RX PubMed=12730201; DOI=10.1074/jbc.m300492200;
RA Tian J.H., Das S., Sheng Z.H.;
RT "Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated
RT protein (DAP) kinase regulates its interaction with Munc18.";
RL J. Biol. Chem. 278:26265-26274(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH VAMP2 AND SNAP25.
RX PubMed=14665625; DOI=10.1074/jbc.m312064200;
RA Fasshauer D., Margittai M.;
RT "A transient N-terminal interaction of SNAP-25 and syntaxin nucleates SNARE
RT assembly.";
RL J. Biol. Chem. 279:7613-7621(2004).
RN [13]
RP FUNCTION, AND INTERACTION WITH VAMP2 AND SNAP25.
RX PubMed=16888141; DOI=10.1126/science.1129486;
RA Pobbati A.V., Stein A., Fasshauer D.;
RT "N- to C-terminal SNARE complex assembly promotes rapid membrane fusion.";
RL Science 313:673-676(2006).
RN [14]
RP FUNCTION, INTERACTION WITH KCNB1, AND SUBCELLULAR LOCATION.
RX PubMed=17301173; DOI=10.1523/jneurosci.4006-06.2007;
RA Singer-Lahat D., Sheinin A., Chikvashvili D., Tsuk S., Greitzer D.,
RA Friedrich R., Feinshreiber L., Ashery U., Benveniste M., Levitan E.S.,
RA Lotan I.;
RT "K+ channel facilitation of exocytosis by dynamic interaction with
RT syntaxin.";
RL J. Neurosci. 27:1651-1658(2007).
RN [15]
RP FUNCTION, INTERACTION WITH KCNB1, AND SUBCELLULAR LOCATION.
RX PubMed=18167541; DOI=10.1371/journal.pone.0001381;
RA Singer-Lahat D., Chikvashvili D., Lotan I.;
RT "Direct interaction of endogenous Kv channels with syntaxin enhances
RT exocytosis by neuroendocrine cells.";
RL PLoS ONE 3:E1381-E1381(2008).
RN [16]
RP INTERACTION WITH VAMP2 AND SEPT8.
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 [17]
RP FUNCTION, INTERACTION WITH KCNB1, AND SUBCELLULAR LOCATION.
RX PubMed=20484665; DOI=10.1242/jcs.063719;
RA Feinshreiber L., Singer-Lahat D., Friedrich R., Matti U., Sheinin A.,
RA Yizhar O., Nachman R., Chikvashvili D., Rettig J., Ashery U., Lotan I.;
RT "Non-conducting function of the Kv2.1 channel enables it to recruit
RT vesicles for release in neuroendocrine and nerve cells.";
RL J. Cell Sci. 123:1940-1947(2010).
RN [18]
RP FUNCTION, INTERACTION WITH KCNB1, AND SUBCELLULAR LOCATION.
RX PubMed=22411134; DOI=10.1007/s00125-012-2512-6;
RA Dai X.Q., Manning Fox J.E., Chikvashvili D., Casimir M., Plummer G.,
RA Hajmrle C., Spigelman A.F., Kin T., Singer-Lahat D., Kang Y., Shapiro A.M.,
RA Gaisano H.Y., Lotan I., Macdonald P.E.;
RT "The voltage-dependent potassium channel subunit Kv2.1 regulates insulin
RT secretion from rodent and human islets independently of its electrical
RT function.";
RL Diabetologia 55:1709-1720(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-64 AND SER-95, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [20]
RP INTERACTION WITH PLCL1, AND SUBCELLULAR LOCATION.
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 [21]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 180-262 IN COMPLEX WITH SNAP25 AND
RP VAMP2.
RX PubMed=9759724; DOI=10.1038/26412;
RA Sutton R.B., Fasshauer D., Jahn R., Brunger A.T.;
RT "Crystal structure of a SNARE complex involved in synaptic exocytosis at
RT 2.4 A resolution.";
RL Nature 395:347-353(1998).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-150.
RX PubMed=10913252; DOI=10.1021/bi0003994;
RA Lerman J.C., Robblee J., Fairman R., Hughson F.M.;
RT "Structural analysis of the neuronal SNARE protein syntaxin-1A.";
RL Biochemistry 39:8470-8479(2000).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-248 IN COMPLEX WITH STXBP1.
RX PubMed=10746715; DOI=10.1038/35006120;
RA Misura K.M.S., Scheller R.H., Weis W.I.;
RT "Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex.";
RL Nature 404:355-362(2000).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 191-267.
RX PubMed=11118447; DOI=10.1074/jbc.m009636200;
RA Misura K.M.S., Scheller R.H., Weis W.I.;
RT "Self-association of the H3 region of syntaxin 1A. Implications for
RT intermediates in SNARE complex assembly.";
RL J. Biol. Chem. 276:13273-13282(2001).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 191-267 IN COMPLEX WITH SNAP25.
RX PubMed=11533035; DOI=10.1074/jbc.m106853200;
RA Misura K.M.S., Gonzalez L.C. Jr., May A.P., Scheller R.H., Weis W.I.;
RT "Crystal structure and biophysical properties of a complex between the N-
RT terminal SNARE region of SNAP25 and syntaxin 1a.";
RL J. Biol. Chem. 276:41301-41309(2001).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 191-253 IN COMPLEX WITH CPLX1;
RP SNAP25 AND VAMP2, AND STRUCTURE BY NMR.
RX PubMed=11832227; DOI=10.1016/s0896-6273(02)00583-4;
RA Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., Suedhof T.C.,
RA Rizo J.;
RT "Three-dimensional structure of the complexin/SNARE complex.";
RL Neuron 33:397-409(2002).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 191-256 IN COMPLEX WITH SNAP25
RP AND VAMP2.
RX PubMed=12496247; DOI=10.1074/jbc.m211889200;
RA Ernst J.A., Brunger A.T.;
RT "High resolution structure, stability, and synaptotagmin binding of a
RT truncated neuronal SNARE complex.";
RL J. Biol. Chem. 278:8630-8636(2003).
RN [28]
RP STRUCTURE BY NMR OF 27-146.
RX PubMed=9753330; DOI=10.1016/s0092-8674(00)81742-0;
RA Fernandez I., Ubach J., Dulubova I., Zhang X., Suedhof T.C., Rizo J.;
RT "Three-dimensional structure of an evolutionarily conserved N-terminal
RT domain of syntaxin 1A.";
RL Cell 94:841-849(1998).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-267 IN COMPLEX WITH STXBP1 AND
RP SNAP25.
RX PubMed=18337752; DOI=10.1038/emboj.2008.37;
RA Burkhardt P., Hattendorf D.A., Weis W.I., Fasshauer D.;
RT "Munc18a controls SNARE assembly through its interaction with the syntaxin
RT N-peptide.";
RL EMBO J. 27:923-933(2008).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 183-288 IN COMPLEX WITH SNAP25
RP AND VAMP2, AND FUNCTION.
RX PubMed=19571812; DOI=10.1038/nature08156;
RA Stein A., Weber G., Wahl M.C., Jahn R.;
RT "Helical extension of the neuronal SNARE complex into the membrane.";
RL Nature 460:525-528(2009).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 191-253 IN COMPLEX WITH HUMAN
RP CPLX1; SNAP25 AND VAMP2.
RX PubMed=21785414; DOI=10.1038/nsmb.2101;
RA Kummel D., Krishnakumar S.S., Radoff D.T., Li F., Giraudo C.G., Pincet F.,
RA Rothman J.E., Reinisch K.M.;
RT "Complexin cross-links prefusion SNAREs into a zigzag array.";
RL Nat. Struct. Mol. Biol. 18:927-933(2011).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 191-256, AND INTERACTION WITH
RP SYT1; SNAP25 AND VAMP2.
RX PubMed=26280336; DOI=10.1038/nature14975;
RA Zhou Q., Lai Y., Bacaj T., Zhao M., Lyubimov A.Y., Uervirojnangkoorn M.,
RA Zeldin O.B., Brewster A.S., Sauter N.K., Cohen A.E., Soltis S.M.,
RA Alonso-Mori R., Chollet M., Lemke H.T., Pfuetzner R.A., Choi U.B.,
RA Weis W.I., Diao J., Suedhof T.C., Brunger A.T.;
RT "Architecture of the synaptotagmin-SNARE machinery for neuronal
RT exocytosis.";
RL Nature 525:62-67(2015).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 190-256, INTERACTION WITH SYT1;
RP CPLX1; VAMP2 AND SNAP25, AND FUNCTION.
RX PubMed=28813412; DOI=10.1038/nature23484;
RA Zhou Q., Zhou P., Wang A.L., Wu D., Zhao M., Suedhof T.C., Brunger A.T.;
RT "The primed SNARE-complexin-synaptotagmin complex for neuronal
RT exocytosis.";
RL Nature 548:420-425(2017).
CC -!- FUNCTION: Plays an essential role in hormone and neurotransmitter
CC calcium-dependent exocytosis and endocytosis (PubMed:7901002,
CC PubMed:17301173, PubMed:18167541, PubMed:20484665, PubMed:22411134,
CC PubMed:28813412). Part of the SNARE (Soluble NSF Attachment Receptor)
CC complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion
CC of synaptic vesicles with the presynaptic plasma membrane
CC (PubMed:14665625, PubMed:16888141, PubMed:19571812). STX1A and SNAP25
CC are localized on the plasma membrane while VAMP2 resides in synaptic
CC vesicles. The pairing of the three SNAREs from the N-terminal SNARE
CC motifs to the C-terminal anchors leads to the formation of the SNARE
CC complex, which brings membranes into close proximity and results in
CC final fusion (PubMed:14665625, PubMed:16888141, PubMed:19571812).
CC Participates in the calcium-dependent regulation of acrosomal
CC exocytosis in sperm (By similarity). Also plays an important role in
CC the exocytosis of hormones such as insulin or glucagon-like peptide 1
CC (GLP-1) (By similarity). {ECO:0000250|UniProtKB:O35526,
CC ECO:0000269|PubMed:14665625, ECO:0000269|PubMed:16888141,
CC ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:18167541,
CC ECO:0000269|PubMed:19571812, ECO:0000269|PubMed:20484665,
CC ECO:0000269|PubMed:22411134, ECO:0000269|PubMed:28813412,
CC ECO:0000269|PubMed:7901002}.
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:14665625,
CC PubMed:16888141, PubMed:19196426, PubMed:9759724, PubMed:11533035,
CC PubMed:11832227, PubMed:12496247, PubMed:19571812, PubMed:28813412,
CC PubMed:18337752, PubMed:21785414, PubMed:26280336). The SNARE complex
CC interacts with CPLX1 (PubMed:21785414, PubMed:28813412). Interacts with
CC STXBP1 (PubMed:10746715, PubMed:12730201, PubMed:18337752). Interacts
CC (via C-terminus) with KCNB1 (via C-terminus); the interaction increases
CC in a calcium-dependent manner and induces a pore-independent
CC enhancement of exocytosis in neuroendocrine cells, chromaffin cells,
CC pancreatic beta cells and from the soma of dorsal root ganglia (DRG)
CC neurons (PubMed:17301173, PubMed:18167541, PubMed:20484665,
CC PubMed:22411134). Interacts with SYTL4 (By similarity). Interacts with
CC STXBP6 (PubMed:12145319). Interacts with PLCL1 (via C2 domain)
CC (PubMed:23341457). Interacts with OTOF (By similarity). Interacts with
CC LGI3 (By similarity). Interacts with SLC6A4 (PubMed:11709063).
CC Interacts with SYT6 and SYT8; the interaction is Ca(2+)-dependent (By
CC similarity). Interacts with VAMP8 (PubMed:10336434). Interacts with
CC SNAP23 (PubMed:9507000). Interacts with VAPA and SYBU (By similarity).
CC Interacts with PRRT2 (By similarity). Interacts with SEPT8
CC (PubMed:19196426). Interacts with STXBP5L (By similarity). Interacts
CC with synaptotagmin-1/SYT1 (PubMed:26280336, PubMed:28813412). Interacts
CC with SEPTIN5; in the cerebellar cortex (By similarity). Interacts with
CC SEPTIN4; in the striatum (By similarity).
CC {ECO:0000250|UniProtKB:O35526, ECO:0000250|UniProtKB:Q16623,
CC ECO:0000269|PubMed:10336434, ECO:0000269|PubMed:10746715,
CC ECO:0000269|PubMed:11533035, ECO:0000269|PubMed:11709063,
CC ECO:0000269|PubMed:11832227, ECO:0000269|PubMed:12145319,
CC ECO:0000269|PubMed:12496247, ECO:0000269|PubMed:12730201,
CC ECO:0000269|PubMed:14665625, ECO:0000269|PubMed:16888141,
CC ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:18167541,
CC ECO:0000269|PubMed:18337752, ECO:0000269|PubMed:19196426,
CC ECO:0000269|PubMed:19571812, ECO:0000269|PubMed:20484665,
CC ECO:0000269|PubMed:21785414, ECO:0000269|PubMed:22411134,
CC ECO:0000269|PubMed:23341457, ECO:0000269|PubMed:26280336,
CC ECO:0000269|PubMed:28813412, ECO:0000269|PubMed:9507000,
CC ECO:0000269|PubMed:9759724}.
CC -!- INTERACTION:
CC P32851; O35430: Apba1; NbExp=3; IntAct=EBI-539720, EBI-704760;
CC P32851; Q62717: Cadps; NbExp=3; IntAct=EBI-539720, EBI-15804323;
CC P32851; P60881: Snap25; NbExp=29; IntAct=EBI-539720, EBI-1027214;
CC P32851; P60881-2: Snap25; NbExp=6; IntAct=EBI-539720, EBI-15685612;
CC P32851; P61765: Stxbp1; NbExp=22; IntAct=EBI-539720, EBI-1029097;
CC P32851; P63045: Vamp2; NbExp=8; IntAct=EBI-539720, EBI-520880;
CC P32851; P60879: Snap25; Xeno; NbExp=7; IntAct=EBI-539720, EBI-445270;
CC P32851; P60880-2: SNAP25; Xeno; NbExp=4; IntAct=EBI-539720, EBI-12177361;
CC P32851; Q5SQN1: SNAP47; Xeno; NbExp=3; IntAct=EBI-539720, EBI-10244848;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:O35526}; Single-pass type IV
CC membrane protein {ECO:0000250|UniProtKB:O35526}. Cell membrane
CC {ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:18167541,
CC ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:22411134,
CC ECO:0000269|PubMed:23341457}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:O35526}. Note=Colocalizes with KCNB1 at the cell
CC membrane (PubMed:17301173). Colocalizes with PLCL1 at the cell membrane
CC (PubMed:22673903). {ECO:0000269|PubMed:17301173}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in cerebral cortex,
CC hippocampus, cerebellum, adrenal medulla and retina with weak
CC expression detected in non-neuronal tissues.
CC -!- PTM: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1
CC significantly decreases its interaction with STXBP1.
CC {ECO:0000269|PubMed:12730201}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type C (BoNT/C), which hydrolyzes the 253-Lys-|-Ala-254 bond
CC (PubMed:7737992). Cleavage inhibits neurotransmitter release
CC (PubMed:7901002). {ECO:0000269|PubMed:7737992,
CC ECO:0000269|PubMed:7901002}.
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 -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01231.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D10392; BAA01231.1; ALT_INIT; mRNA.
DR EMBL; D12519; BAA02089.1; -; mRNA.
DR EMBL; M95734; AAA42195.1; -; mRNA.
DR PIR; A38141; A38141.
DR RefSeq; NP_446240.2; NM_053788.2.
DR PDB; 1BR0; NMR; -; A=27-144.
DR PDB; 1EZ3; X-ray; 1.90 A; A/B/C=24-150.
DR PDB; 1HVV; X-ray; 2.40 A; A/B/C/D=190-264.
DR PDB; 1JTH; X-ray; 2.00 A; B/D=191-267.
DR PDB; 1KIL; X-ray; 2.30 A; B=191-250.
DR PDB; 1N7S; X-ray; 1.45 A; B=191-256.
DR PDB; 1SFC; X-ray; 2.40 A; B/F/J=180-262.
DR PDB; 1URQ; X-ray; 2.00 A; B=188-259.
DR PDB; 2M8R; NMR; -; A=183-288.
DR PDB; 2N1T; NMR; -; B=188-259.
DR PDB; 3C98; X-ray; 2.60 A; B=1-267.
DR PDB; 3HD7; X-ray; 3.40 A; B/F=183-288.
DR PDB; 3IPD; X-ray; 4.80 A; B/F=183-288.
DR PDB; 3J96; EM; 7.60 A; L=191-256.
DR PDB; 3J97; EM; 7.80 A; L=191-256.
DR PDB; 3J98; EM; 8.40 A; L=191-256.
DR PDB; 3J99; EM; 8.20 A; L=191-256.
DR PDB; 3RK2; X-ray; 2.20 A; B/F=191-253.
DR PDB; 3RK3; X-ray; 3.50 A; B=191-253.
DR PDB; 3RL0; X-ray; 3.80 A; B/F/J/N/R/V/Z/d=191-253.
DR PDB; 4JEH; X-ray; 2.50 A; B=25-266.
DR PDB; 4JEU; X-ray; 3.20 A; B=2-243.
DR PDB; 5CCG; X-ray; 3.50 A; B/H=191-256.
DR PDB; 5CCH; X-ray; 3.60 A; B=191-256.
DR PDB; 5CCI; X-ray; 4.10 A; B=191-256.
DR PDB; 5KJ7; X-ray; 3.50 A; B/H=191-256.
DR PDB; 5KJ8; X-ray; 4.10 A; B/H=191-256.
DR PDB; 5W5C; X-ray; 1.85 A; B=190-256.
DR PDB; 5W5D; X-ray; 2.50 A; B=190-256.
DR PDB; 6IP1; EM; 3.90 A; B=2-253.
DR PDB; 6MDM; EM; 4.40 A; I=1-256.
DR PDB; 6MDN; EM; 4.40 A; I=1-256.
DR PDB; 6MTI; EM; 10.40 A; B/F/J/N/R/V=190-256.
DR PDB; 6WVW; X-ray; 2.11 A; B/F=191-256.
DR PDB; 7UDB; EM; 3.50 A; B=2-253.
DR PDB; 7UDC; EM; 3.70 A; B=2-253.
DR PDBsum; 1BR0; -.
DR PDBsum; 1EZ3; -.
DR PDBsum; 1HVV; -.
DR PDBsum; 1JTH; -.
DR PDBsum; 1KIL; -.
DR PDBsum; 1N7S; -.
DR PDBsum; 1SFC; -.
DR PDBsum; 1URQ; -.
DR PDBsum; 2M8R; -.
DR PDBsum; 2N1T; -.
DR PDBsum; 3C98; -.
DR PDBsum; 3HD7; -.
DR PDBsum; 3IPD; -.
DR PDBsum; 3J96; -.
DR PDBsum; 3J97; -.
DR PDBsum; 3J98; -.
DR PDBsum; 3J99; -.
DR PDBsum; 3RK2; -.
DR PDBsum; 3RK3; -.
DR PDBsum; 3RL0; -.
DR PDBsum; 4JEH; -.
DR PDBsum; 4JEU; -.
DR PDBsum; 5CCG; -.
DR PDBsum; 5CCH; -.
DR PDBsum; 5CCI; -.
DR PDBsum; 5KJ7; -.
DR PDBsum; 5KJ8; -.
DR PDBsum; 5W5C; -.
DR PDBsum; 5W5D; -.
DR PDBsum; 6IP1; -.
DR PDBsum; 6MDM; -.
DR PDBsum; 6MDN; -.
DR PDBsum; 6MTI; -.
DR PDBsum; 6WVW; -.
DR PDBsum; 7UDB; -.
DR PDBsum; 7UDC; -.
DR AlphaFoldDB; P32851; -.
DR BMRB; P32851; -.
DR SMR; P32851; -.
DR BioGRID; 250448; 18.
DR CORUM; P32851; -.
DR DIP; DIP-108N; -.
DR IntAct; P32851; 25.
DR MINT; P32851; -.
DR STRING; 10116.ENSRNOP00000040699; -.
DR iPTMnet; P32851; -.
DR PhosphoSitePlus; P32851; -.
DR SwissPalm; P32851; -.
DR jPOST; P32851; -.
DR PaxDb; P32851; -.
DR PRIDE; P32851; -.
DR GeneID; 116470; -.
DR KEGG; rno:116470; -.
DR UCSC; RGD:69430; rat.
DR CTD; 6804; -.
DR RGD; 69430; Stx1a.
DR VEuPathDB; HostDB:ENSRNOG00000029165; -.
DR eggNOG; KOG0810; Eukaryota.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; P32851; -.
DR OMA; RWICFIL; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; P32851; -.
DR TreeFam; TF313763; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-449836; Other interleukin signaling.
DR Reactome; R-RNO-5682910; LGI-ADAM interactions.
DR Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; P32851; -.
DR PRO; PR:P32851; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000029165; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; P32851; baseline and differential.
DR Genevisible; P32851; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0042641; C:actomyosin; IDA:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0043229; C:intracellular organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IDA:RGD.
DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IDA:MGI.
DR GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; IDA:RGD.
DR GO; GO:0043008; F:ATP-dependent protein binding; IPI:RGD.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:RGD.
DR GO; GO:0019869; F:chloride channel inhibitor activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0017022; F:myosin binding; IPI:RGD.
DR GO; GO:0032028; F:myosin head/neck binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:RGD.
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; IPI:UniProtKB.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0046879; P:hormone secretion; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006836; P:neurotransmitter transport; TAS:RGD.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IDA:UniProtKB.
DR GO; GO:0033605; P:positive regulation of catecholamine secretion; IDA:UniProtKB.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; IDA:RGD.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:RGD.
DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; IDA:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016925; P:protein sumoylation; ISO:RGD.
DR GO; GO:0045055; P:regulated exocytosis; ISO:RGD.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:RGD.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; ISO:RGD.
DR GO; GO:0009629; P:response to gravity; IDA:RGD.
DR GO; GO:0032940; P:secretion by cell; ISO:RGD.
DR GO; GO:0035493; P:SNARE complex assembly; IMP:CAFA.
DR GO; GO:0016081; P:synaptic vesicle docking; IEP:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IGI:SynGO.
DR GO; GO:0048278; P:vesicle docking; ISO:RGD.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR DisProt; DP00155; -.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR028669; STX1.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR PANTHER; PTHR19957:SF84; PTHR19957:SF84; 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; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW Direct protein sequencing; Exocytosis; Isopeptide bond; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..288
FT /note="Syntaxin-1A"
FT /id="PRO_0000210189"
FT TOPO_DOM 1..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..288
FT /note="Helical; Anchor for type IV membrane protein"
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 SITE 253..254
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type C (BoNT/C)"
FT /evidence="ECO:0000269|PubMed:7737992"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 188
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000269|PubMed:12730201"
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"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:3C98"
FT HELIX 28..63
FT /evidence="ECO:0007829|PDB:1EZ3"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4JEU"
FT HELIX 69..104
FT /evidence="ECO:0007829|PDB:1EZ3"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3C98"
FT HELIX 111..146
FT /evidence="ECO:0007829|PDB:1EZ3"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:4JEH"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4JEH"
FT HELIX 192..254
FT /evidence="ECO:0007829|PDB:1N7S"
FT HELIX 261..284
FT /evidence="ECO:0007829|PDB:2M8R"
SQ SEQUENCE 288 AA; 33067 MW; 8F929F489E323CAA CRC64;
MKDRTQELRT AKDSDDDDDV TVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA
ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH
STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG
IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHA
VDYVERAVSD TKKAVKYQSK ARRKKIMIII CCVILGIIIA STIGGIFG
