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Protein

Syntaxin-1A

Gene

Syx1A

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a critical role in several secretory processes, including cuticle secretion and neurotransmitter release, and probably assists in neuronal membrane maturation or the final stages of neuronal differentiation. Essential for embryonic viability and development. Required for coordinated peristaltic contractions.

GO - Molecular functioni

  • SNAP receptor activity Source: FlyBase
  • SNARE binding Source: FlyBase

GO - Biological processi

  • cellularization Source: FlyBase
  • cuticle development Source: FlyBase
  • exocytosis Source: FlyBase
  • haltere development Source: FlyBase
  • intracellular protein transport Source: GO_Central
  • mitotic cytokinesis Source: FlyBase
  • muscle contraction Source: FlyBase
  • neuromuscular synaptic transmission Source: FlyBase
  • neurotransmitter secretion Source: FlyBase
  • regulation of exocytosis Source: InterPro
  • regulation of pole plasm oskar mRNA localization Source: FlyBase
  • synaptic transmission Source: FlyBase
  • synaptic vesicle docking Source: FlyBase
  • synaptic vesicle fusion to presynaptic active zone membrane Source: FlyBase
  • vesicle docking Source: GO_Central
  • vesicle fusion Source: FlyBase
  • vesicle-mediated transport Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Neurotransmitter transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Syntaxin-1A
Alternative name(s):
dSynt1
Gene namesi
Name:Syx1A
Synonyms:syx-1A
ORF Names:CG31136
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0013343. Syx1A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 268268CytoplasmicSequence analysisAdd
BLAST
Transmembranei269 – 28921Helical; Anchor for type IV membrane proteinSequence analysisAdd
BLAST
Topological domaini290 – 2912VesicularSequence analysis

GO - Cellular componenti

  • integral component of membrane Source: GO_Central
  • membrane Source: FlyBase
  • plasma membrane Source: FlyBase
  • SNARE complex Source: FlyBase
  • synaptic vesicle Source: FlyBase
  • terminal bouton Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291Syntaxin-1APRO_0000210235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ24547.
PRIDEiQ24547.

PTM databases

iPTMnetiQ24547.

Expressioni

Tissue specificityi

Prior to embryonic stage 12 expression is ubiquitous, then it becomes concentrated in the neuropil. In third instar larvae, expression is seen at the synaptic boutons of the ventral muscles. In adult brain, expression is seen in the optic lobe neuropils.1 Publication

Developmental stagei

Expressed throughout development.

Gene expression databases

BgeeiQ24547.
ExpressionAtlasiQ24547. differential.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
alphaSnapQ239834EBI-135062,EBI-195132

GO - Molecular functioni

  • SNAP receptor activity Source: FlyBase
  • SNARE binding Source: FlyBase

Protein-protein interaction databases

BioGridi67788. 36 interactions.
DIPiDIP-19389N.
IntActiQ24547. 10 interactions.
MINTiMINT-957003.
STRINGi7227.FBpp0292260.

Structurei

3D structure databases

ProteinModelPortaliQ24547.
SMRiQ24547. Positions 30-286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 25763t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili33 – 11785Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the syntaxin family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0810. Eukaryota.
COG5074. LUCA.
GeneTreeiENSGT00760000119200.
InParanoidiQ24547.
KOiK04560.
OrthoDBiEOG7X9G7R.
PhylomeDBiQ24547.

Family and domain databases

InterProiIPR028669. STX1A/1B.
IPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR19957:SF84. PTHR19957:SF84. 1 hit.
PfamiPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q24547-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKDRLAALH AAQSDDEEET EVAVNVDGHD SYMDDFFAQV EEIRGMIDKV
60 70 80 90 100
QDNVEEVKKK HSAILSAPQT DEKTKQELED LMADIKKNAN RVRGKLKGIE
110 120 130 140 150
QNIEQEEQQN KSSADLRIRK TQHSTLSRKF VEVMTEYNRT QTDYRERCKG
160 170 180 190 200
RIQRQLEITG RPTNDDELEK MLEEGNSSVF TQGIIMETQQ AKQTLADIEA
210 220 230 240 250
RHQDIMKLET SIKELHDMFM DMAMLVESQG EMIDRIEYHV EHAMDYVQTA
260 270 280 290
TQDTKKALKY QSKARRKKIM ILICLTVLGI LAASYVSSYF M
Length:291
Mass (Da):33,648
Last modified:November 1, 1996 - v1
Checksum:iBD0AB88ABC5DD7B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221Q → E (PubMed:7609612).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37732 mRNA. Translation: AAA75649.1.
AE014297 Genomic DNA. Translation: AAF56232.1.
AY061472 mRNA. Translation: AAL29020.1.
PIRiA55673.
RefSeqiNP_001303545.1. NM_001316616.1.
NP_524475.1. NM_079751.5.
UniGeneiDm.2366.

Genome annotation databases

EnsemblMetazoaiFBtr0084588; FBpp0083973; FBgn0013343.
GeneIDi42854.
KEGGidme:Dmel_CG31136.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37732 mRNA. Translation: AAA75649.1.
AE014297 Genomic DNA. Translation: AAF56232.1.
AY061472 mRNA. Translation: AAL29020.1.
PIRiA55673.
RefSeqiNP_001303545.1. NM_001316616.1.
NP_524475.1. NM_079751.5.
UniGeneiDm.2366.

3D structure databases

ProteinModelPortaliQ24547.
SMRiQ24547. Positions 30-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67788. 36 interactions.
DIPiDIP-19389N.
IntActiQ24547. 10 interactions.
MINTiMINT-957003.
STRINGi7227.FBpp0292260.

PTM databases

iPTMnetiQ24547.

Proteomic databases

PaxDbiQ24547.
PRIDEiQ24547.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084588; FBpp0083973; FBgn0013343.
GeneIDi42854.
KEGGidme:Dmel_CG31136.

Organism-specific databases

CTDi42854.
FlyBaseiFBgn0013343. Syx1A.

Phylogenomic databases

eggNOGiKOG0810. Eukaryota.
COG5074. LUCA.
GeneTreeiENSGT00760000119200.
InParanoidiQ24547.
KOiK04560.
OrthoDBiEOG7X9G7R.
PhylomeDBiQ24547.

Miscellaneous databases

GenomeRNAii42854.
PROiQ24547.

Gene expression databases

BgeeiQ24547.
ExpressionAtlasiQ24547. differential.

Family and domain databases

InterProiIPR028669. STX1A/1B.
IPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR19957:SF84. PTHR19957:SF84. 1 hit.
PfamiPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic and electrophysiological studies of Drosophila syntaxin-1A demonstrate its role in nonneuronal secretion and neurotransmission."
    Schulze K.L., Broadie K., Perin M.S., Bellen H.J.
    Cell 80:311-320(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Head.
  2. "Characterization and gene cloning of Drosophila syntaxin 1 (Dsynt1): the fruit fly homologue of rat syntaxin 1."
    Cerezo J.R., Jimenez F., Moya F.
    Brain Res. Mol. Brain Res. 29:245-252(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, TISSUE SPECIFICITY.
    Tissue: Embryo.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiSTX1A_DROME
AccessioniPrimary (citable) accession number: Q24547
Secondary accession number(s): Q9TX14, Q9VCD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.