Syntaxin-1A - Rattus norvegicus (Rat)

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P32851 (STX1A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 125. 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)

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.6 Ref.7 Ref.8
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.8
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	intracellular protein transport Inferred from electronic annotation. Source: InterPro positive regulation of exocytosis Inferred from direct assay. Source: RGD positive regulation of neurotransmitter secretion Inferred from mutant phenotype. Source: RGD response to gravity Inferred from direct assay. Source: RGD synaptic vesicle docking involved in exocytosis Inferred from expression pattern Ref.3. Source: UniProtKB
Cellular component	actomyosin Inferred from direct assay. Source: RGD cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Non-traceable author statement Ref.3. Source: UniProtKB plasma membrane Inferred from direct assay. Source: RGD secretory granule Inferred from direct assay. Source: UniProtKB synaptic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synaptobrevin 2-SNAP-25-syntaxin-1a complex Inferred from direct assay. Source: MGI synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex Inferred from direct assay. Source: MGI synaptosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP-dependent protein binding Inferred from physical interaction. Source: RGD SNAP receptor activity Inferred from electronic annotation. Source: InterPro SNARE binding Inferred from direct assay. Source: MGI calcium-dependent protein binding Inferred from physical interaction. Source: RGD glycoprotein binding Inferred from direct assay. Source: MGI myosin head/neck binding Inferred from physical interaction. Source: RGD protein N-terminus binding Inferred from direct assay. Source: RGD protein binding, bridging Inferred from physical interaction. Source: RGD protein domain specific binding Inferred from physical interaction. Source: RGD protein heterodimerization activity Inferred from direct assay. 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.8

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: 1587842] [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: 1334074] [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: 1321498] [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: 7690687] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"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: 10336434] [Abstract] Cited for: IDENTIFICATION IN A TERNARY COMPLEX WITH VAMP8 AND SNAP25.
[6]	"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: 11709063] [Abstract] Cited for: INTERACTION WITH SLC6A4.
[7]	"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: 12145319] [Abstract] Cited for: INTERACTION WITH STXBP6.
[8]	"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: 12730201] [Abstract] Cited for: PHOSPHORYLATION AT SER-188, INTERACTION WITH DAPK1 AND STKB1.
[9]	"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: 9759724] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 180-262 IN COMPLEX WITH SNAP25 AND VAMP2.
[10]	"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: 10913252] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-150.
[11]	"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: 10746715] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-248 IN COMPLEX WITH STXBP1.
[12]	"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: 11118447] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 191-267.
[13]	"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: 11533035] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 191-267 IN COMPLEX WITH SNAP25.
[14]	"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: 11832227] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 191-253 IN COMPLEX WITH CPLX1; SNAP25 AND VAMP2, STRUCTURE BY NMR.
[15]	"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: 12496247] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 191-256 IN COMPLEX WITH SNAP25 AND VAMP2.
[16]	"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: 9753330] [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	[»]

ProteinModelPortal

P32851.

SMR

P32851. Positions 2-259.

DisProt

DP00155.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-108N.

IntAct

P32851. 9 interactions.

MINT

MINT-96097.

STRING

P32851.

PTM databases

PhosphoSite

P32851.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000049601; ENSRNOP00000040699; ENSRNOG00000029165.

GeneID

116470.

KEGG

rno:116470.

UCSC

NM_053788. rat.

Organism-specific databases

CTD

6804.

RGD

69430. Stx1a.

Phylogenomic databases

eggNOG

roNOG09503.

HOVERGEN

HBG000497.

InParanoid

P32851.

OMA

RDGFMDE.

OrthoDB

EOG4PC9SV.

PhylomeDB

P32851.

Gene expression databases

ArrayExpress

P32851.

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]

K04560.

PANTHER

PTHR19957:SF35. Syntaxin-1. 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

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:	December 14, 2011
This is version 125 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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents