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P32851 (STX1A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Syntaxin-1A
Alternative name(s):
Neuron-specific antigen HPC-1
Synaptotagmin-associated 35 kDa protein
Short name=P35A
Gene names
Name:Stx1a
Synonyms:Sap
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca2+-regulation of exocytosis acrosomal reaction in sperm.

Subunit structure

Interacts with OTOF, SYTL4, VAPA, SYBU and LGI3. Found in a complex with VAMP8 and SNAP23. Interacts with SYT6 and SYT8; the interaction is Ca2+-dependent By similarity. Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds to CPLX1. Binds STXBP6. Found in a ternary complex with STX1A and SNAP25. Interacts with SLC6A4. Interacts with STXBP1 and DAPK1. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Single-pass type IV membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity.

Tissue specificity

Expressed predominantly in cerebral cortex, hippocampus, cerebellum, adrenal medulla and retina with weak expression detected in non-neuronal tissues.

Post-translational modification

Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1. Ref.9

Sequence similarities

Belongs to the syntaxin family.

Contains 1 t-SNARE coiled-coil homology domain.

Sequence caution

The sequence BAA01231.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processExocytosis
Neurotransmitter transport
Transport
   Cellular componentCell junction
Cytoplasmic vesicle
Membrane
Synapse
Synaptosome
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion-dependent exocytosis

Inferred from electronic annotation. Source: Ensembl

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

neurotransmitter transport

Traceable author statement PubMed 11846792. Source: RGD

positive regulation of exocytosis

Inferred from direct assay PubMed 11331586. Source: RGD

positive regulation of neurotransmitter secretion

Inferred from mutant phenotype PubMed 12183029. Source: RGD

regulation of exocytosis

Inferred from mutant phenotype PubMed 16030255. Source: RGD

response to gravity

Inferred from direct assay PubMed 15076716. Source: RGD

synaptic vesicle docking involved in exocytosis

Inferred from expression pattern Ref.3. Source: UniProtKB

   Cellular_componentSNARE complex

Inferred from sequence or structural similarity. Source: UniProtKB

actomyosin

Inferred from direct assay PubMed 16030255. Source: RGD

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of membrane

Non-traceable author statement Ref.3. Source: UniProtKB

intracellular organelle

Inferred from direct assay PubMed 10340764. Source: RGD

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 11331586. Source: RGD

protein complex

Inferred from direct assay PubMed 19255244. Source: RGD

secretory granule

Inferred from direct assay PubMed 15537656. Source: UniProtKB

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synaptobrevin 2-SNAP-25-syntaxin-1a complex

Inferred from direct assay PubMed 7553862. Source: MGI

synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex

Inferred from direct assay PubMed 7553862. Source: MGI

synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex

Inferred from direct assay PubMed 19132534. Source: RGD

   Molecular_functionATP-dependent protein binding

Inferred from physical interaction PubMed 16030255. Source: RGD

SNARE binding

Inferred from direct assay PubMed 7553862. Source: MGI

calcium channel inhibitor activity

Inferred from electronic annotation. Source: Ensembl

calcium-dependent protein binding

Inferred from physical interaction PubMed 16030255. Source: RGD

glycoprotein binding

Inferred from direct assay PubMed 7553862. Source: MGI

myosin binding

Inferred from physical interaction PubMed 16030255. Source: RGD

myosin head/neck binding

Inferred from physical interaction PubMed 16030255. Source: RGD

protein N-terminus binding

Inferred from direct assay PubMed 19255244. Source: RGD

protein binding

Inferred from physical interaction Ref.7PubMed 14642278. Source: UniProtKB

protein binding, bridging

Inferred from physical interaction PubMed 16030255. Source: RGD

protein domain specific binding

Inferred from physical interaction PubMed 8999968. Source: RGD

protein heterodimerization activity

Inferred from direct assay PubMed 16030255. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288Syntaxin-1A
PRO_0000210189

Regions

Topological domain1 – 265265Cytoplasmic Potential
Transmembrane266 – 28823Helical; Anchor for type IV membrane protein; Potential
Domain192 – 25463t-SNARE coiled-coil homology
Coiled coil68 – 10942 Potential
Compositional bias13 – 197Asp-rich (acidic)

Amino acid modifications

Modified residue141Phosphoserine By similarity
Modified residue1881Phosphoserine; by DAPK1 Ref.9

Secondary structure

..................... 288
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32851 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 8F929F489E323CAA

FASTA28833,067
        10         20         30         40         50         60 
MKDRTQELRT AKDSDDDDDV TVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA 

        70         80         90        100        110        120 
ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH 

       130        140        150        160        170        180 
STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG 

       190        200        210        220        230        240 
IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHA 

       250        260        270        280 
VDYVERAVSD TKKAVKYQSK ARRKKIMIII CCVILGIIIA STIGGIFG 

« Hide

References

[1]"Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1."
Inoue A., Obata K., Akagawa K.
J. Biol. Chem. 267:10613-10619(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 8-37 AND 44-102.
Tissue: Brain.
[2]"HPC-1 is associated with synaptotagmin and omega-conotoxin receptor."
Yoshida A., Oho C., Omori A., Kuwahara R., Ito T., Takahashi M.
J. Biol. Chem. 267:24925-24928(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-288, PROTEIN SEQUENCE OF 1-15 AND 95-113.
Tissue: Brain.
[3]"Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones."
Bennett M.K., Calakos N., Scheller R.H.
Science 257:255-259(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-288, PROTEIN SEQUENCE OF 4-16 AND 31-56.
Tissue: Brain.
[4]"The syntaxin family of vesicular transport receptors."
Bennett M.K., Garcia-Arraras J.E., Elferink L.A., Peterson K.E., Fleming A.M., Hazuka C.D., Scheller R.H.
Cell 74:863-873(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Syntaxin 12, a member of the syntaxin family localized to the endosome."
Tang B.L., Tan A.E., Lim L.K., Lee S.S., Low D.Y., Hong W.
J. Biol. Chem. 273:6944-6950(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNAP23.
[6]"Mixed and non-cognate SNARE complexes. Characterization of assembly and biophysical properties."
Fasshauer D., Antonin W., Margittai M., Pabst S., Jahn R.
J. Biol. Chem. 274:15440-15446(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A TERNARY COMPLEX WITH VAMP8 AND SNAP25.
[7]"Regulation of the serotonin transporter by interacting proteins."
Haase J., Killian A.M., Magnani F., Williams C.
Biochem. Soc. Trans. 29:722-728(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC6A4.
[8]"Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly."
Scales S.J., Hesser B.A., Masuda E.S., Scheller R.H.
J. Biol. Chem. 277:28271-28279(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STXBP6.
[9]"Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18."
Tian J.H., Das S., Sheng Z.H.
J. Biol. Chem. 278:26265-26274(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-188, INTERACTION WITH DAPK1 AND STKB1.
[10]"Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution."
Sutton R.B., Fasshauer D., Jahn R., Brunger A.T.
Nature 395:347-353(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 180-262 IN COMPLEX WITH SNAP25 AND VAMP2.
[11]"Structural analysis of the neuronal SNARE protein syntaxin-1A."
Lerman J.C., Robblee J., Fairman R., Hughson F.M.
Biochemistry 39:8470-8479(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-150.
[12]"Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex."
Misura K.M.S., Scheller R.H., Weis W.I.
Nature 404:355-362(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-248 IN COMPLEX WITH STXBP1.
[13]"Self-association of the H3 region of syntaxin 1A. Implications for intermediates in SNARE complex assembly."
Misura K.M.S., Scheller R.H., Weis W.I.
J. Biol. Chem. 276:13273-13282(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 191-267.
[14]"Crystal structure and biophysical properties of a complex between the N-terminal SNARE region of SNAP25 and syntaxin 1a."
Misura K.M.S., Gonzalez L.C. Jr., May A.P., Scheller R.H., Weis W.I.
J. Biol. Chem. 276:41301-41309(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 191-267 IN COMPLEX WITH SNAP25.
[15]"Three-dimensional structure of the complexin/SNARE complex."
Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., Suedhof T.C., Rizo J.
Neuron 33:397-409(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 191-253 IN COMPLEX WITH CPLX1; SNAP25 AND VAMP2, STRUCTURE BY NMR.
[16]"High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex."
Ernst J.A., Brunger A.T.
J. Biol. Chem. 278:8630-8636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 191-256 IN COMPLEX WITH SNAP25 AND VAMP2.
[17]"Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A."
Fernandez I., Ubach J., Dulubova I., Zhang X., Suedhof T.C., Rizo J.
Cell 94:841-849(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 27-146.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10392 mRNA. Translation: BAA01231.1. Different initiation.
D12519 mRNA. Translation: BAA02089.1.
M95734 mRNA. Translation: AAA42195.1.
PIRA38141.
RefSeqNP_446240.2. NM_053788.2.
UniGeneRn.9943.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BR0NMR-A27-144[»]
1EZ3X-ray1.90A/B/C24-150[»]
1HVVX-ray2.40A/B/C/D190-264[»]
1JTHX-ray2.00B/D191-267[»]
1KILX-ray2.30B191-250[»]
1N7SX-ray1.45B191-256[»]
1SFCX-ray2.40B/F/J180-262[»]
1URQX-ray2.00B188-259[»]
2BU0model-B191-258[»]
2M8RNMR-A183-288[»]
3C98X-ray2.60B1-267[»]
3HD7X-ray3.40B/F183-288[»]
3IPDX-ray4.80B/F183-288[»]
3RK2X-ray2.20B/F191-253[»]
3RK3X-ray3.50B191-253[»]
3RL0X-ray3.80B/F/J/N/R/V/Z/d191-253[»]
4JEHX-ray2.50B25-266[»]
4JEUX-ray3.20B2-243[»]
DisProtDP00155.
ProteinModelPortalP32851.
SMRP32851. Positions 2-259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250448. 11 interactions.
DIPDIP-108N.
IntActP32851. 13 interactions.
MINTMINT-96097.
STRING10116.ENSRNOP00000040699.

PTM databases

PhosphoSiteP32851.

Proteomic databases

PaxDbP32851.
PRIDEP32851.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000049601; ENSRNOP00000040699; ENSRNOG00000029165.
GeneID116470.
KEGGrno:116470.
UCSCRGD:69430. rat.

Organism-specific databases

CTD6804.
RGD69430. Stx1a.

Phylogenomic databases

eggNOGCOG5074.
GeneTreeENSGT00730000110552.
HOGENOMHOG000286023.
HOVERGENHBG000497.
InParanoidP32851.
KOK04560.
OMAHEETKAV.
OrthoDBEOG7X9G7R.
PhylomeDBP32851.
TreeFamTF313763.

Gene expression databases

GenevestigatorP32851.

Family and domain databases

InterProIPR028669. STX1A/1B.
IPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERPTHR19957:SF84. PTHR19957:SF84. 1 hit.
PfamPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMSSF47661. SSF47661. 1 hit.
PROSITEPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32851.
NextBio619018.
PMAP-CutDBP32851.
PROP32851.

Entry information

Entry nameSTX1A_RAT
AccessionPrimary (citable) accession number: P32851
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references