STX1A_DROME
ID STX1A_DROME Reviewed; 291 AA.
AC Q24547; Q9TX14; Q9VCD7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Syntaxin-1A;
DE AltName: Full=dSynt1;
GN Name=Syx1A; Synonyms=syx-1A; ORFNames=CG31136;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Head;
RX PubMed=7834751; DOI=10.1016/0092-8674(95)90414-x;
RA Schulze K.L., Broadie K., Perin M.S., Bellen H.J.;
RT "Genetic and electrophysiological studies of Drosophila syntaxin-1A
RT demonstrate its role in nonneuronal secretion and neurotransmission.";
RL Cell 80:311-320(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=7609612; DOI=10.1016/0169-328x(94)00254-c;
RA Cerezo J.R., Jimenez F., Moya F.;
RT "Characterization and gene cloning of Drosophila syntaxin 1 (Dsynt1): the
RT fruit fly homologue of rat syntaxin 1.";
RL Brain Res. Mol. Brain Res. 29:245-252(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27323327; DOI=10.1038/ncb3374;
RA Caviglia S., Brankatschk M., Fischer E.J., Eaton S., Luschnig S.;
RT "Staccato/Unc-13-4 controls secretory lysosome-mediated lumen fusion during
RT epithelial tube anastomosis.";
RL Nat. Cell Biol. 18:727-739(2016).
CC -!- FUNCTION: Plays a critical role in several secretory processes,
CC including cuticle secretion and neurotransmitter release, and probably
CC assists in neuronal membrane maturation or the final stages of neuronal
CC differentiation (PubMed:7834751). Essential for embryonic viability and
CC development (PubMed:7834751). Required for coordinated peristaltic
CC contractions (PubMed:7834751). Recruited by Unc-13-4B to secretory
CC lysosome-related organelles (SLs) that are essential for tracheal lumen
CC fusion between previously separate tracheal branches (anastomosis).
CC Possibly promotes the intracellular fusion of the extending tracheal
CC stalk cell lumens in tracheal fusion cells (Fcs) by interacting with
CC complementary SNAREs (such as Syb) present in the apical membrane of
CC the FC-FC interface and the membranes of the separate tracheal stalk
CC cells (PubMed:27323327). {ECO:0000269|PubMed:27323327,
CC ECO:0000269|PubMed:7834751}.
CC -!- INTERACTION:
CC Q24547; Q23983: alphaSnap; NbExp=4; IntAct=EBI-135062, EBI-195132;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:7834751}; Single-pass type IV
CC membrane protein {ECO:0000305}. Lysosome membrane
CC {ECO:0000269|PubMed:27323327}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Prior to embryonic stage 12 expression is
CC ubiquitous, then it becomes concentrated in the neuropil. In third
CC instar larvae, expression is seen at the synaptic boutons of the
CC ventral muscles. In adult brain, expression is seen in the optic lobe
CC neuropils. {ECO:0000269|PubMed:7609612}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; L37732; AAA75649.1; -; mRNA.
DR EMBL; AE014297; AAF56232.1; -; Genomic_DNA.
DR EMBL; AY061472; AAL29020.1; -; mRNA.
DR PIR; A55673; A55673.
DR RefSeq; NP_001303545.1; NM_001316616.1.
DR RefSeq; NP_524475.1; NM_079751.5.
DR AlphaFoldDB; Q24547; -.
DR SMR; Q24547; -.
DR BioGRID; 67788; 59.
DR DIP; DIP-19389N; -.
DR IntAct; Q24547; 10.
DR STRING; 7227.FBpp0292260; -.
DR iPTMnet; Q24547; -.
DR PaxDb; Q24547; -.
DR PRIDE; Q24547; -.
DR EnsemblMetazoa; FBtr0084588; FBpp0083973; FBgn0013343.
DR EnsemblMetazoa; FBtr0392904; FBpp0352246; FBgn0013343.
DR GeneID; 42854; -.
DR KEGG; dme:Dmel_CG31136; -.
DR CTD; 42854; -.
DR FlyBase; FBgn0013343; Syx1A.
DR VEuPathDB; VectorBase:FBgn0013343; -.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; Q24547; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; Q24547; -.
DR Reactome; R-DME-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-DME-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-DME-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-DME-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-DME-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-DME-449836; Other interleukin signaling.
DR Reactome; R-DME-888590; GABA synthesis, release, reuptake and degradation.
DR Reactome; R-DME-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR BioGRID-ORCS; 42854; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42854; -.
DR PRO; PR:Q24547; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0013343; Expressed in brain and 32 other tissues.
DR ExpressionAtlas; Q24547; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IDA:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; IDA:FlyBase.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0000149; F:SNARE binding; IPI:FlyBase.
DR GO; GO:0007349; P:cellularization; TAS:FlyBase.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0007482; P:haltere development; IGI:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:FlyBase.
DR GO; GO:0017157; P:regulation of exocytosis; IEA:InterPro.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0016081; P:synaptic vesicle docking; ISS:FlyBase.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IDA:FlyBase.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IDA:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:FlyBase.
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 Coiled coil; Cytoplasmic vesicle; Lysosome; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..291
FT /note="Syntaxin-1A"
FT /id="PRO_0000210235"
FT TOPO_DOM 1..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..291
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 195..257
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 33..117
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 122
FT /note="Q -> E (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 33648 MW; BD0AB88ABC5DD7B3 CRC64;
MTKDRLAALH AAQSDDEEET EVAVNVDGHD SYMDDFFAQV EEIRGMIDKV QDNVEEVKKK
HSAILSAPQT DEKTKQELED LMADIKKNAN RVRGKLKGIE QNIEQEEQQN KSSADLRIRK
TQHSTLSRKF VEVMTEYNRT QTDYRERCKG RIQRQLEITG RPTNDDELEK MLEEGNSSVF
TQGIIMETQQ AKQTLADIEA RHQDIMKLET SIKELHDMFM DMAMLVESQG EMIDRIEYHV
EHAMDYVQTA TQDTKKALKY QSKARRKKIM ILICLTVLGI LAASYVSSYF M
