STX1A_HUMAN
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 03-AUG-2022, entry version 212.
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). Interacts (via C-terminus) with
CC KCNB1 (via C-terminus); the interaction increases in a calcium-
CC 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 with SLC6A4 (By similarity). Interacts with
CC SYT6 and SYT8; the interaction is Ca(2+)-dependent (By similarity).
CC Interacts with VAMP8 (PubMed:12130530). Interacts with SNAP23
CC (PubMed:12130530). Interacts with VAPA and SYBU (PubMed:15459722).
CC Interacts with PRRT2 (By similarity). Interacts with SEPT8 (By
CC similarity). Interacts with STXBP5L (By similarity). Interacts with
CC synaptotagmin-1/SYT1 (By similarity). Interacts with SEPTIN5; in the
CC cerebellar cortex (By similarity). Interacts with SEPTIN4; in the
CC striatum (By similarity). {ECO:0000250|UniProtKB:O35526,
CC ECO:0000250|UniProtKB:P32851, ECO:0000269|PubMed:12130530,
CC ECO:0000269|PubMed:12730201, ECO:0000269|PubMed:15459722,
CC 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};
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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; 177.
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 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; Q16623; -.
DR PeptideAtlas; Q16623; -.
DR PRIDE; Q16623; -.
DR ProteomicsDB; 60963; -. [Q16623-1]
DR ProteomicsDB; 60964; -. [Q16623-2]
DR ProteomicsDB; 60965; -. [Q16623-3]
DR ProteomicsDB; 69314; -.
DR Antibodypedia; 3644; 722 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 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; 1033833at2759; -.
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 1078 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 112 other tissues.
DR ExpressionAtlas; Q16623; baseline and differential.
DR Genevisible; Q16623; HS.
DR GO; GO:0042641; C:actomyosin; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
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:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IEA:Ensembl.
DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IEA:Ensembl.
DR GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; IEA:Ensembl.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0043008; F:ATP-dependent protein binding; IEA:Ensembl.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; 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:0032028; F:myosin head/neck binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
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:0072657; P:protein localization to membrane; IEA:Ensembl.
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:0009629; P:response to gravity; IEA:Ensembl.
DR GO; GO:0032940; P:secretion by cell; IDA:UniProtKB.
DR GO; GO:0035493; P:SNARE complex assembly; IEA:Ensembl.
DR GO; GO:0016081; P:synaptic vesicle docking; IEA:Ensembl.
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 GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
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 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
