Reviewed, UniProtKB/Swiss-Prot P32851 (STX1A_RAT)

Names and origin

Protein names

Recommended name:
    Syntaxin-1A
Alternative name(s):
    Synaptotagmin-associated 35 kDa protein
      Short name=P35A
    Neuron-specific antigen HPC-1

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.
Subunit structure	Interacts with OTOF, SYTL4, VAPA, SYBU and LGI3. Found in a complex with VAMP8 and SNAP23 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. Ref.6
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.
Sequence similarities	Belongs to the syntaxin family. Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
Biological process	Exocytosis Neurotransmitter transport Transport
Cellular component	Cell junction Cytoplasmic vesicle Membrane Synapse Synaptosome
Domain	Coiled coil Transmembrane
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
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 during exocytosis Ref.3 Inferred from expression pattern. Source: UniProtKB
Cellular component	actomyosin Inferred from direct assay. Source: RGD cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Ref.3 Non-traceable author statement. Source: UniProtKB secretory granule Inferred from direct assay. Source: UniProtKB 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
Sept5	Q9JJM9	1	EBI-539720,EBI-539712
Stxbp1	P61765	1	EBI-539720,EBI-1029097
Vamp2	P63045	2	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

23

Anchor for type IV membrane protein Potential

Domain

192 – 254

63

t-SNARE coiled-coil homology

Coiled coil

68 – 109

42

Potential

Compositional bias

13 – 19

7

Asp-rich (acidic)

Amino acid modifications

Modified residue

14

1

Phosphoserine By similarity

Secondary structure

1

.

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288

Helix Strand Turn

Details...

Turn

6 – 8

3

Helix

28 – 63

36

Helix

69 – 104

36

Helix

111 – 146

36

Helix

151 – 156

6

Helix

162 – 170

9

Turn

178 – 180

3

Helix

192 – 254

63

Sequences

	Sequence		Length	Mass (Da)
	P32851-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 8F929F489E323CAA	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

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]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.

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	[»]

DisProt

DP00155.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-108N.

IntAct

P32851. 11 interactions.

STRING

P32851.

PTM databases

PhosphoSite

P32851.

Genome annotation databases

Ensembl

ENSRNOT00000049601; ENSRNOP00000040699; ENSRNOG00000029165; Rattus norvegicus. [Genome view]

GeneID

116470.

KEGG

rno:116470.

UCSC

NM_053788. rat.

Organism-specific databases

CTD

116470.

RGD

69430. Stx1a.

Phylogenomic databases

eggNOG

roNOG09503.

HOVERGEN

P32851.

InParanoid

P32851.

OMA

GIEQSIE.

OrthoDB

EOG9FN73Q.

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]

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]

PROSITE

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

ProtoNet

Search...

Other Resources

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:	January 19, 2010
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)