ID STX1A_HUMAN Reviewed; 288 AA. AC Q16623; O15447; O15448; Q12936; Q75MD9; Q7Z5K3; Q9BPZ6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 220. DE RecName: Full=Syntaxin-1A; DE AltName: Full=Neuron-specific antigen HPC-1; GN Name=STX1A; Synonyms=STX1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=7622072; DOI=10.1016/0378-1119(95)00152-v; RA Zhang R.-D., Maksymowych A.B., Simpson L.L.; RT "Cloning and sequence analysis of a cDNA encoding human syntaxin 1A, a RT polypeptide essential for exocytosis."; RL Gene 159:293-294(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2). RX PubMed=9311751; DOI=10.1086/514850; RA Osborne L.R., Soder S., Shi X.-M., Pober B., Costa T., Scherer S.W., RA Tsui L.-C.; RT "Hemizygous deletion of the syntaxin 1A gene in individuals with Williams RT syndrome."; RL Am. J. Hum. Genet. 61:449-452(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND SEQUENCE REVISION RP TO 144. RX PubMed=11977160; DOI=10.1002/ajmg.10321; RA Wu Y.-Q., Bejjani B.A., Tsui L.-C., Mandel A., Osborne L.R., Shaffer L.G.; RT "Refinement of the genomic structure of STX1A and mutation analysis in RT nondeletion Williams syndrome patients."; RL Am. J. Med. Genet. 109:121-124(2002). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Adipose tissue; RX PubMed=9003414; DOI=10.1042/bj3210151; RA Jagadish M.N., Tellam J.T., Macaulay S.L., Gough K.H., James D.E., RA Ward C.W.; RT "Novel isoform of syntaxin 1 is expressed in mammalian cells."; RL Biochem. J. 321:151-156(1997). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9177791; DOI=10.1006/geno.1997.4650; RA Nakayama T., Fujiwara T., Miyazawa A., Asakawa S., Shimizu N., Shimizu Y., RA Mikoshiba K., Akagawa K.; RT "Mapping of the human HPC-1/syntaxin 1A gene (STX1A) to chromosome 7 band RT q11.2."; RL Genomics 42:173-176(1997). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=12586365; DOI=10.1016/s0014-5793(03)00015-2; RA Nakayama T., Mikoshiba K., Yamamori T., Akagawa K.; RT "Expression of syntaxin 1C, an alternative splice variant of HPC-1/syntaxin RT 1A, is enhanced by phorbol-ester stimulation in astroglioma: participation RT of the PKC signaling pathway."; RL FEBS Lett. 536:209-214(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-288 (ISOFORM 1). RC TISSUE=Brain; RA Zhang R.-D., Simpson L.; RT "Human syntaxin is homologous with rat syntaxin A and digested by BoNT C."; RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases. RN [11] RP TISSUE SPECIFICITY. RX PubMed=10644452; DOI=10.1006/geno.1999.5987; RA Botta A., Calza L., Giardino L., Potenza S., Novelli G., Dallapiccola B.; RT "Expression analysis of the human HPC-1/syntaxin 1A, a gene deleted in RT Williams syndrome."; RL Genomics 62:525-528(1999). RN [12] RP INTERACTION WITH VAMP8 AND SNAP23. RX PubMed=12130530; DOI=10.1182/blood.v100.3.1081; RA Polgar J., Chung S.H., Reed G.L.; RT "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in RT human platelets and are required for granule secretion."; RL Blood 100:1081-1083(2002). RN [13] 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 [14] RP INTERACTION WITH SYBU. RX PubMed=15459722; DOI=10.1038/ncb1169; RA Su Q., Cai Q., Gerwin C., Smith C.L., Sheng Z.-H.; RT "Syntabulin is a microtubule-associated protein implicated in syntaxin RT transport in neurons."; RL Nat. Cell Biol. 6:941-953(2004). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=15822905; DOI=10.1021/pr0498436; RA DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., RA Pant H.C., Dosemeci A.; RT "Phosphoproteomic analysis of synaptosomes from human cerebral cortex."; RL J. Proteome Res. 4:306-315(2005). RN [16] RP FUNCTION. RX PubMed=23091057; DOI=10.1074/jbc.m112.409649; RA Rodriguez F., Zanetti M.N., Mayorga L.S., Tomes C.N.; RT "Munc18-1 controls SNARE protein complex assembly during human sperm RT acrosomal exocytosis."; RL J. Biol. Chem. 287:43825-43839(2012). RN [17] RP FUNCTION, SUMOYLATION, INTERACTION WITH VAMP2; SNAP25 AND STXBP1, AND RP MUTAGENESIS OF LYS-252; LYS-253 AND LYS-256. RX PubMed=26635000; DOI=10.1038/srep17669; RA Craig T.J., Anderson D., Evans A.J., Girach F., Henley J.M.; RT "SUMOylation of Syntaxin1A regulates presynaptic endocytosis."; RL Sci. Rep. 5:17669-17669(2015). CC -!- FUNCTION: Plays an essential role in hormone and neurotransmitter CC calcium-dependent exocytosis and endocytosis (PubMed:26635000). Part of CC the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, CC STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the CC presynaptic plasma membrane. STX1A and SNAP25 are localized on the CC plasma membrane while VAMP2 resides in synaptic vesicles. The pairing CC of the three SNAREs from the N-terminal SNARE motifs to the C-terminal CC anchors leads to the formation of the SNARE complex, which brings CC membranes into close proximity and results in final fusion. CC Participates in the calcium-dependent regulation of acrosomal CC exocytosis in sperm (PubMed:23091057). 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:23091057, ECO:0000269|PubMed:26635000}. 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:26635000). The SNARE CC complex interacts with CPLX1 (By similarity). Interacts with STXBP1 CC (PubMed:12730201, PubMed:26635000). The interaction with STXBP1 CC promotes assembly of the SNARE complex (By similarity). Interacts (via CC C-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 (By similarity). Interacts with CC STXBP6 (By similarity). Interacts with PLCL1 (via C2 domain) (By CC similarity). Interacts with OTOF (By similarity). Interacts with LGI3 CC (By similarity). Interacts (via the H3 domain) with SLC6A4 (via the N- CC terminus); this interaction regulates SLC4A6 channel conductance in CC thalamocortical neurons (By similarity). Interacts with SYT6 and SYT8; CC the interaction is Ca(2+)-dependent (By similarity). Interacts with CC VAMP8 (PubMed:12130530). Interacts with SNAP23 (PubMed:12130530). CC Interacts with VAPA and SYBU (PubMed:15459722). Interacts with PRRT2 CC (By similarity). Interacts with SEPT8 (By similarity). Interacts with CC STXBP5L (By similarity). Interacts with synaptotagmin-1/SYT1 (By CC similarity). Interacts with SEPTIN5; in the cerebellar cortex (By CC similarity). Interacts with SEPTIN4; in the striatum (By similarity). CC {ECO:0000250|UniProtKB:O35526, ECO:0000250|UniProtKB:P32851, CC ECO:0000269|PubMed:12130530, ECO:0000269|PubMed:12730201, CC ECO:0000269|PubMed:15459722, ECO:0000269|PubMed:26635000}. CC -!- INTERACTION: CC Q16623; Q4LEZ3: AARD; NbExp=3; IntAct=EBI-712466, EBI-5463075; CC Q16623; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-712466, EBI-742038; CC Q16623; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-712466, EBI-11522760; CC Q16623; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-712466, EBI-11957045; CC Q16623; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-712466, EBI-12109402; CC Q16623; Q16853: AOC3; NbExp=3; IntAct=EBI-712466, EBI-3921628; CC Q16623; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-712466, EBI-4290634; CC Q16623; O95236-2: APOL3; NbExp=3; IntAct=EBI-712466, EBI-11976321; CC Q16623; Q92482: AQP3; NbExp=3; IntAct=EBI-712466, EBI-2808854; CC Q16623; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-712466, EBI-11343438; CC Q16623; O15155: BET1; NbExp=3; IntAct=EBI-712466, EBI-749204; CC Q16623; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-712466, EBI-465781; CC Q16623; Q12981: BNIP1; NbExp=3; IntAct=EBI-712466, EBI-4402847; CC Q16623; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-712466, EBI-8648738; CC Q16623; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-712466, EBI-12003442; CC Q16623; P60033: CD81; NbExp=3; IntAct=EBI-712466, EBI-712921; CC Q16623; Q16543: CDC37; NbExp=3; IntAct=EBI-712466, EBI-295634; CC Q16623; Q8NC01: CLEC1A; NbExp=3; IntAct=EBI-712466, EBI-11996768; CC Q16623; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-712466, EBI-6165897; CC Q16623; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-712466, EBI-2807956; CC Q16623; O43169: CYB5B; NbExp=3; IntAct=EBI-712466, EBI-1058710; CC Q16623; Q9Y6V7: DDX49; NbExp=3; IntAct=EBI-712466, EBI-719274; CC Q16623; O00559: EBAG9; NbExp=3; IntAct=EBI-712466, EBI-8787095; CC Q16623; P50402: EMD; NbExp=3; IntAct=EBI-712466, EBI-489887; CC Q16623; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-712466, EBI-711490; CC Q16623; Q9NVF9: ETNK2; NbExp=3; IntAct=EBI-712466, EBI-751864; CC Q16623; Q92520: FAM3C; NbExp=3; IntAct=EBI-712466, EBI-2876774; CC Q16623; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-712466, EBI-11991950; CC Q16623; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-712466, EBI-6166686; CC Q16623; O14653: GOSR2; NbExp=6; IntAct=EBI-712466, EBI-4401517; CC Q16623; Q13491-3: GPM6B; NbExp=3; IntAct=EBI-712466, EBI-11992640; CC Q16623; P09601: HMOX1; NbExp=4; IntAct=EBI-712466, EBI-2806151; CC Q16623; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-712466, EBI-10266796; CC Q16623; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-712466, EBI-14069005; CC Q16623; P21145: MAL; NbExp=4; IntAct=EBI-712466, EBI-3932027; CC Q16623; Q13021: MALL; NbExp=3; IntAct=EBI-712466, EBI-750078; CC Q16623; P30301: MIP; NbExp=3; IntAct=EBI-712466, EBI-8449636; CC Q16623; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-712466, EBI-6163737; CC Q16623; Q9H115: NAPB; NbExp=4; IntAct=EBI-712466, EBI-3921185; CC Q16623; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-712466, EBI-10317425; CC Q16623; Q16617: NKG7; NbExp=4; IntAct=EBI-712466, EBI-3919611; CC Q16623; Q8IXM6: NRM; NbExp=3; IntAct=EBI-712466, EBI-10262547; CC Q16623; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-712466, EBI-12092917; CC Q16623; P26678: PLN; NbExp=3; IntAct=EBI-712466, EBI-692836; CC Q16623; P60201-2: PLP1; NbExp=3; IntAct=EBI-712466, EBI-12188331; CC Q16623; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-712466, EBI-10485931; CC Q16623; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-712466, EBI-11721828; CC Q16623; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-712466, EBI-8652812; CC Q16623; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-712466, EBI-743796; CC Q16623; Q96LZ7: RMDN2; NbExp=3; IntAct=EBI-712466, EBI-2806908; CC Q16623; P78317: RNF4; NbExp=3; IntAct=EBI-712466, EBI-2340927; CC Q16623; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-712466, EBI-10244780; CC Q16623; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-712466, EBI-8652744; CC Q16623; O75396: SEC22B; NbExp=3; IntAct=EBI-712466, EBI-1058865; CC Q16623; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-712466, EBI-10329948; CC Q16623; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-712466, EBI-749270; CC Q16623; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-712466, EBI-12188413; CC Q16623; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-712466, EBI-741850; CC Q16623; P60880: SNAP25; NbExp=3; IntAct=EBI-712466, EBI-524785; CC Q16623; P60880-2: SNAP25; NbExp=5; IntAct=EBI-712466, EBI-12177361; CC Q16623; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-712466, EBI-10244848; CC Q16623; P37840: SNCA; NbExp=2; IntAct=EBI-712466, EBI-985879; CC Q16623; Q6UX34: SNORC; NbExp=3; IntAct=EBI-712466, EBI-11957067; CC Q16623; P0DN84: STRIT1; NbExp=3; IntAct=EBI-712466, EBI-12200293; CC Q16623; O60499-2: STX10; NbExp=3; IntAct=EBI-712466, EBI-12094584; CC Q16623; O75558: STX11; NbExp=3; IntAct=EBI-712466, EBI-714135; CC Q16623; Q86Y82: STX12; NbExp=3; IntAct=EBI-712466, EBI-2691717; CC Q16623; O14662-5: STX16; NbExp=3; IntAct=EBI-712466, EBI-9089968; CC Q16623; Q16623: STX1A; NbExp=5; IntAct=EBI-712466, EBI-712466; CC Q16623; P32856-2: STX2; NbExp=3; IntAct=EBI-712466, EBI-11956649; CC Q16623; Q13277: STX3; NbExp=3; IntAct=EBI-712466, EBI-1394295; CC Q16623; Q12846: STX4; NbExp=3; IntAct=EBI-712466, EBI-744942; CC Q16623; Q13190: STX5; NbExp=3; IntAct=EBI-712466, EBI-714206; CC Q16623; O43752: STX6; NbExp=3; IntAct=EBI-712466, EBI-2695795; CC Q16623; O15400: STX7; NbExp=3; IntAct=EBI-712466, EBI-3221827; CC Q16623; Q9UNK0: STX8; NbExp=3; IntAct=EBI-712466, EBI-727240; CC Q16623; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-712466, EBI-11955057; CC Q16623; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-712466, EBI-8644968; CC Q16623; Q9BXJ8: TMEM120A; NbExp=3; IntAct=EBI-712466, EBI-727322; CC Q16623; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-712466, EBI-10694905; CC Q16623; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-712466, EBI-2339195; CC Q16623; Q8N511: TMEM199; NbExp=3; IntAct=EBI-712466, EBI-10265825; CC Q16623; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-712466, EBI-347385; CC Q16623; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-712466, EBI-11956809; CC Q16623; Q96HV5: TMEM41A; NbExp=3; IntAct=EBI-712466, EBI-10288884; CC Q16623; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-712466, EBI-2852148; CC Q16623; P01375: TNF; NbExp=4; IntAct=EBI-712466, EBI-359977; CC Q16623; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-712466, EBI-765817; CC Q16623; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-712466, EBI-10241197; CC Q16623; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-712466, EBI-12003468; CC Q16623; P40222: TXLNA; NbExp=4; IntAct=EBI-712466, EBI-359793; CC Q16623; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-712466, EBI-10180829; CC Q16623; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-712466, EBI-17208936; CC Q16623; O75841: UPK1B; NbExp=3; IntAct=EBI-712466, EBI-12237619; CC Q16623; Q9NZ43: USE1; NbExp=3; IntAct=EBI-712466, EBI-742842; CC Q16623; P23763-3: VAMP1; NbExp=3; IntAct=EBI-712466, EBI-12097582; CC Q16623; P63027: VAMP2; NbExp=5; IntAct=EBI-712466, EBI-520113; CC Q16623; Q15836: VAMP3; NbExp=3; IntAct=EBI-712466, EBI-722343; CC Q16623; O75379: VAMP4; NbExp=3; IntAct=EBI-712466, EBI-744953; CC Q16623; O95183: VAMP5; NbExp=3; IntAct=EBI-712466, EBI-10191195; CC Q16623; Q8IW00: VSTM4; NbExp=3; IntAct=EBI-712466, EBI-4311759; CC Q16623; Q9UEU0: VTI1B; NbExp=3; IntAct=EBI-712466, EBI-723716; CC Q16623; O95159: ZFPL1; NbExp=3; IntAct=EBI-712466, EBI-718439; CC Q16623; P17014: ZNF12; NbExp=3; IntAct=EBI-712466, EBI-11278550; CC Q16623; P52737: ZNF136; NbExp=3; IntAct=EBI-712466, EBI-749129; CC Q16623; P15622-3: ZNF250; NbExp=3; IntAct=EBI-712466, EBI-10177272; CC Q16623; Q8IYI8: ZNF440; NbExp=3; IntAct=EBI-712466, EBI-726439; CC Q16623; Q8N8Z8: ZNF441; NbExp=3; IntAct=EBI-712466, EBI-17216366; CC Q16623; Q96JC4: ZNF479; NbExp=3; IntAct=EBI-712466, EBI-10820574; CC Q16623; Q9ULM2: ZNF490; NbExp=3; IntAct=EBI-712466, EBI-1105370; CC Q16623; Q8N988-2: ZNF557; NbExp=3; IntAct=EBI-712466, EBI-10699005; CC Q16623; Q9H7X3: ZNF696; NbExp=3; IntAct=EBI-712466, EBI-11090299; CC Q16623; Q96C28: ZNF707; NbExp=3; IntAct=EBI-712466, EBI-748111; CC Q16623; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-712466, EBI-3925400; CC Q16623; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-712466, EBI-5667516; 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}. Synapse, synaptosome CC {ECO:0000250|UniProtKB:O35526}. Cell membrane CC {ECO:0000250|UniProtKB:P32851}. Note=Colocalizes with KCNB1 at the cell CC membrane. {ECO:0000250|UniProtKB:P32851}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q16623-1; Sequence=Displayed; CC Name=2; Synonyms=1C; CC IsoId=Q16623-2; Sequence=VSP_006338; CC Name=3; CC IsoId=Q16623-3; Sequence=VSP_006339; CC -!- TISSUE SPECIFICITY: [Isoform 1]: Highly expressed in embryonic spinal CC cord and ganglia and in adult cerebellum and cerebral cortex. CC {ECO:0000269|PubMed:10644452}. CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in heart, liver, fat, CC skeletal muscle, kidney and brain. {ECO:0000269|PubMed:10644452}. CC -!- PTM: Phosphorylated by CK2 (By similarity). Phosphorylation at Ser-188 CC by DAPK1 significantly decreases its interaction with STXBP1. CC {ECO:0000250, ECO:0000269|PubMed:12730201}. CC -!- PTM: Sumoylated, sumoylation is required for regulation of synaptic CC vesicle endocytosis. {ECO:0000269|PubMed:26635000}. CC -!- DISEASE: Note=STX1A is located in the Williams-Beuren syndrome (WBS) CC critical region. WBS results from a hemizygous deletion of several CC genes on chromosome 7q11.23, thought to arise as a consequence of CC unequal crossing over between highly homologous low-copy repeat CC sequences flanking the deleted region. {ECO:0000305|PubMed:9311751}. CC -!- MISCELLANEOUS: [Isoform 2]: Expression is up-regulated by phorbol 12- CC myristate 13-acetate (PMA), but not by forskolin. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA20940.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; L37792; AAA53519.1; -; mRNA. DR EMBL; U87315; AAK54507.2; -; Genomic_DNA. DR EMBL; AF297001; AAK54507.2; JOINED; Genomic_DNA. DR EMBL; AF297002; AAK54507.2; JOINED; Genomic_DNA. DR EMBL; U87310; AAK54507.2; JOINED; Genomic_DNA. DR EMBL; AF297003; AAK54507.2; JOINED; Genomic_DNA. DR EMBL; U87314; AAK54507.2; JOINED; Genomic_DNA. DR EMBL; U87315; AAB65500.2; -; Genomic_DNA. DR EMBL; AF297001; AAB65500.2; JOINED; Genomic_DNA. DR EMBL; AF297002; AAB65500.2; JOINED; Genomic_DNA. DR EMBL; U87310; AAB65500.2; JOINED; Genomic_DNA. DR EMBL; AF297003; AAB65500.2; JOINED; Genomic_DNA. DR EMBL; U87314; AAB65500.2; JOINED; Genomic_DNA. DR EMBL; D37932; BAA07151.1; -; mRNA. DR EMBL; AB086954; BAC78519.1; -; mRNA. DR EMBL; AC073846; AAS07470.1; -; Genomic_DNA. DR EMBL; CH471200; EAW69650.1; -; Genomic_DNA. DR EMBL; BC000444; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC003011; AAH03011.1; -; mRNA. DR EMBL; BC064644; AAH64644.1; -; mRNA. DR EMBL; U12918; AAA20940.1; ALT_INIT; mRNA. DR CCDS; CCDS34655.1; -. [Q16623-1] DR CCDS; CCDS55120.1; -. [Q16623-3] DR RefSeq; NP_001159375.1; NM_001165903.1. [Q16623-3] DR RefSeq; NP_004594.1; NM_004603.3. [Q16623-1] DR AlphaFoldDB; Q16623; -. DR BMRB; Q16623; -. DR SMR; Q16623; -. DR BioGRID; 112676; 179. DR CORUM; Q16623; -. DR DIP; DIP-390N; -. DR IntAct; Q16623; 135. DR MINT; Q16623; -. DR STRING; 9606.ENSP00000222812; -. DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family. DR TCDB; 8.A.91.1.4; the syntaxin (syntaxin) family. DR GlyCosmos; Q16623; 1 site, 1 glycan. DR GlyGen; Q16623; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q16623; -. DR PhosphoSitePlus; Q16623; -. DR BioMuta; STX1A; -. DR DMDM; 2501084; -. DR jPOST; Q16623; -. DR MassIVE; Q16623; -. DR PaxDb; 9606-ENSP00000222812; -. DR PeptideAtlas; Q16623; -. DR ProteomicsDB; 60963; -. [Q16623-1] DR ProteomicsDB; 60964; -. [Q16623-2] DR ProteomicsDB; 60965; -. [Q16623-3] DR ProteomicsDB; 69314; -. DR Pumba; Q16623; -. DR Antibodypedia; 3644; 783 antibodies from 45 providers. DR DNASU; 6804; -. DR Ensembl; ENST00000222812.8; ENSP00000222812.3; ENSG00000106089.12. [Q16623-1] DR Ensembl; ENST00000395156.7; ENSP00000378585.3; ENSG00000106089.12. [Q16623-3] DR GeneID; 6804; -. DR KEGG; hsa:6804; -. DR MANE-Select; ENST00000222812.8; ENSP00000222812.3; NM_004603.4; NP_004594.1. DR UCSC; uc003tyy.4; human. [Q16623-1] DR AGR; HGNC:11433; -. DR CTD; 6804; -. DR DisGeNET; 6804; -. DR GeneCards; STX1A; -. DR HGNC; HGNC:11433; STX1A. DR HPA; ENSG00000106089; Group enriched (brain, pituitary gland). DR MalaCards; STX1A; -. DR MIM; 186590; gene. DR neXtProt; NX_Q16623; -. DR OpenTargets; ENSG00000106089; -. DR Orphanet; 586; Cystic fibrosis. DR Orphanet; 904; Williams syndrome. DR PharmGKB; PA36233; -. DR VEuPathDB; HostDB:ENSG00000106089; -. DR eggNOG; KOG0810; Eukaryota. DR GeneTree; ENSGT01030000234627; -. DR HOGENOM; CLU_042423_2_2_1; -. DR InParanoid; Q16623; -. DR OMA; RWICFIL; -. DR OrthoDB; 2876074at2759; -. DR PhylomeDB; Q16623; -. DR TreeFam; TF313763; -. DR PathwayCommons; Q16623; -. DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle. DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle. DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle. DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle. DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle. DR Reactome; R-HSA-264876; Insulin processing. DR Reactome; R-HSA-422356; Regulation of insulin secretion. DR Reactome; R-HSA-449836; Other interleukin signaling. DR Reactome; R-HSA-5250971; Toxicity of botulinum toxin type C (botC). DR Reactome; R-HSA-5682910; LGI-ADAM interactions. DR Reactome; R-HSA-6794361; Neurexins and neuroligins. DR Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation. DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR SignaLink; Q16623; -. DR SIGNOR; Q16623; -. DR BioGRID-ORCS; 6804; 11 hits in 1156 CRISPR screens. DR ChiTaRS; STX1A; human. DR GeneWiki; STX1A; -. DR GenomeRNAi; 6804; -. DR Pharos; Q16623; Tbio. DR PRO; PR:Q16623; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q16623; Protein. DR Bgee; ENSG00000106089; Expressed in right frontal lobe and 114 other cell types or tissues. DR ExpressionAtlas; Q16623; baseline and differential. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0043005; C:neuron projection; IDA:MGI. DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central. DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB. DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IEA:Ensembl. DR GO; GO:0019855; F:calcium channel inhibitor activity; IEA:Ensembl. DR GO; GO:0019869; F:chloride channel inhibitor activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB. DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central. DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central. DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IEA:Ensembl. DR GO; GO:0006887; P:exocytosis; IBA:GO_Central. DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. 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; IEA:Ensembl. DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IEA:Ensembl. DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; ISS:UniProtKB. DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB. DR GO; GO:0050796; P:regulation of insulin secretion; TAS:UniProtKB. DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IEA:Ensembl. DR GO; GO:0032940; P:secretion by cell; IDA:UniProtKB. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:UniProtKB. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:UniProtKB. DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central. DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central. 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. DR Genevisible; Q16623; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasmic vesicle; KW Exocytosis; Isopeptide bond; Membrane; Neurotransmitter transport; KW Phosphoprotein; Reference proteome; Secreted; Synapse; Synaptosome; KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation; KW Williams-Beuren syndrome. FT CHAIN 1..288 FT /note="Syntaxin-1A" FT /id="PRO_0000210186" 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 COILED 68..109 FT /evidence="ECO:0000255" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15822905" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35526" 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:0000269|PubMed:12730201" FT CROSSLNK 252 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:26635000" FT CROSSLNK 253 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:26635000" FT CROSSLNK 256 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:26635000" FT VAR_SEQ 227..288 FT /note="GEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIV FT IASTVGGIFA -> PQGAFLKSCPEPQPNREEGALWSSGAPGPAGRDD (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:12586365, FT ECO:0000303|PubMed:9003414" FT /id="VSP_006338" FT VAR_SEQ 227..288 FT /note="GEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIV FT IASTVGGIFA -> TMWRGPCLTPRRPSSTRARRAGRKS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_006339" FT MUTAGEN 252 FT /note="K->R: Complete loss of sumoylation; when associated FT with R-253 and R-256." FT /evidence="ECO:0000269|PubMed:26635000" FT MUTAGEN 253 FT /note="K->R: Complete loss of sumoylation; when associated FT with R-252 and R-256." FT /evidence="ECO:0000269|PubMed:26635000" FT MUTAGEN 256 FT /note="K->R: Complete loss of sumoylation; when associated FT with R-252 and R-253." FT /evidence="ECO:0000269|PubMed:26635000" FT CONFLICT 73 FT /note="E -> V (in Ref. 10; AAA20940)" FT /evidence="ECO:0000305" FT CONFLICT 140 FT /note="D -> V (in Ref. 10; AAA20940)" FT /evidence="ECO:0000305" SQ SEQUENCE 288 AA; 33023 MW; 8AC787EFCE65ACA1 CRC64; 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 //