Syntaxin-1A - Rattus norvegicus (Rat)

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P32851 (STX1A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 136. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Protein existence	Evidence 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 vesicle › secretory vesicle › synaptic vesicle membrane; Single-pass type IV membrane protein By similarity. Cell junction › synapse › synaptosome 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 process	Exocytosis Neurotransmitter transport Transport
Cellular component	Cell junction Cytoplasmic vesicle Membrane Synapse Synaptosome
Domain	Coiled coil Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	calcium ion-dependent exocytosis Inferred from electronic annotation. Source: Compara intracellular protein transport Inferred from electronic annotation. Source: InterPro 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 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_component	actomyosin Inferred from direct assay PubMed 16030255. Source: RGD cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Non-traceable author statement Ref.3. Source: UniProtKB neuron projection Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay PubMed 11331586. 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_function	SNARE binding Inferred from direct assay PubMed 7553862. Source: MGI calcium channel inhibitor activity Inferred from electronic annotation. Source: Compara glycoprotein binding Inferred from direct assay PubMed 7553862. Source: MGI protein N-terminus binding Inferred from direct assay PubMed 19255244. Source: RGD protein heterodimerization activity Inferred from direct assay PubMed 16030255. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Vamp2	P63045	5	EBI-539720,EBI-520880

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 288

288

Syntaxin-1A

PRO_0000210189

Regions

Topological domain

1 – 265

265

Cytoplasmic Potential

Transmembrane

266 – 288

Helical; Anchor for type IV membrane protein; Potential

Domain

192 – 254

t-SNARE coiled-coil homology

Coiled coil

68 – 109

Potential

Compositional bias

13 – 19

Asp-rich (acidic)

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

188

Phosphoserine; by DAPK1 Ref.9

Secondary structure

288

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P32851 [UniParc].

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

FASTA

288

33,067

        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.

IPI

IPI00324381.

PIR

A38141.

RefSeq

NP_446240.2. NM_053788.2.

UniGene

Rn.9943.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BR0	NMR	-	A	27-144	[»]
1EZ3	X-ray	1.90	A/B/C	24-150	[»]
1HVV	X-ray	2.40	A/B/C/D	190-264	[»]
1JTH	X-ray	2.00	B/D	191-267	[»]
1KIL	X-ray	2.30	B	191-250	[»]
1N7S	X-ray	1.45	B	191-256	[»]
1SFC	X-ray	2.40	B/F/J	180-262	[»]
1URQ	X-ray	2.00	B	188-259	[»]
2BU0	model	-	B	191-258	[»]
3C98	X-ray	2.60	B	1-267	[»]
3HD7	X-ray	3.40	B/F	183-288	[»]
3IPD	X-ray	4.80	B/F	183-288	[»]
3RK2	X-ray	2.20	B/F	191-253	[»]
3RK3	X-ray	3.50	B	191-253	[»]
3RL0	X-ray	3.80	B/F/J/N/R/V/Z/d	191-253	[»]

DisProt

DP00155.

ProteinModelPortal

P32851.

SMR

P32851. Positions 2-259.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-108N.

IntAct

P32851. 10 interactions.

MINT

MINT-96097.

STRING

10116.ENSRNOP00000040699.

PTM databases

PhosphoSite

P32851.

Proteomic databases

PaxDb

P32851.

PRIDE

P32851.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000049601; ENSRNOP00000040699; ENSRNOG00000029165.

GeneID

116470.

KEGG

rno:116470.

UCSC

RGD:69430. rat.

Organism-specific databases

CTD

6804.

RGD

69430. Stx1a.

Phylogenomic databases

eggNOG

COG5074.

GeneTree

ENSGT00550000074334.

HOGENOM

HOG000286023.

HOVERGEN

HBG000497.

InParanoid

P32851.

K04560.

OMA

HVINASH.

OrthoDB

EOG4PC9SV.

Gene expression databases

Genevestigator

P32851.

GermOnline

ENSRNOG00000029165. Rattus norvegicus.

Family and domain databases

InterPro

IPR015709. Syntaxin-1.
IPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]

PANTHER

PTHR19957:SF35. PTHR19957:SF35. 1 hit.

Pfam

PF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]

SMART

SM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]

SUPFAM

SSF47661. t-snare. 1 hit.

PROSITE

PS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P32851.

NextBio

619018.

PMAP-CutDB

P32851.

Entry information

Entry name

STX1A_RAT

Accession

Primary (citable) accession number: P32851

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	April 3, 2013
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents