UniProt functional annotation for P32851



	UniProt functional annotation for P32851

UniProt code: P32851.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

Function: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis (PubMed:7901002, PubMed:17301173, PubMed:18167541, PubMed:20484665, PubMed:22411134, PubMed:28813412). Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane (PubMed:14665625, PubMed:16888141, PubMed:19571812). STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion (PubMed:14665625, PubMed:16888141, PubMed:19571812). Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm (By similarity). Plays also an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity). {ECO:0000250|UniProtKB:O35526, ECO:0000269|PubMed:14665625, ECO:0000269|PubMed:16888141, ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:18167541, ECO:0000269|PubMed:19571812, ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:22411134, ECO:0000269|PubMed:28813412, ECO:0000269|PubMed:7901002}.

Subunit: Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A; this complex constitutes the basic catalytic machinery of the complex neurotransmitter release apparatus (PubMed:14665625, PubMed:16888141, PubMed:19196426, PubMed:9759724, PubMed:11533035, PubMed:11832227, PubMed:12496247, PubMed:19571812, PubMed:28813412, PubMed:18337752, PubMed:21785414, PubMed:26280336). The SNARE complex interacts with CPLX1 (PubMed:21785414, PubMed:28813412). Interacts with STXBP1 (PubMed:10746715, PubMed:12730201, PubMed:18337752). Interacts (via C-terminus) with KCNB1 (via C-terminus); the interaction increases in a calcium-dependent manner and induces a pore-independent enhancement of exocytosis in neuroendocrine cells, chromaffin cells, pancreatic beta cells and from the soma of dorsal root ganglia (DRG) neurons (PubMed:17301173, PubMed:18167541, PubMed:20484665, PubMed:22411134). Interacts with SYTL4 (By similarity). Interacts with STXBP6 (PubMed:12145319). Interacts with PLCL1 (via C2 domain) (PubMed:23341457). Interacts with OTOF (By similarity). Interacts with LGI3 (By similarity). Interacts with SLC6A4 (PubMed:11709063). Interacts with SYT6 and SYT8; the interaction is Ca(2+)-dependent (By similarity). Interacts with VAMP8 (PubMed:10336434). Interacts with SNAP23 (PubMed:9507000). Interacts with VAPA and SYBU (By similarity). Interacts with PRRT2 (By similarity). Interacts with SEPT8 (PubMed:19196426). Interacts with STXBP5L (By similarity). Interacts with synaptotagmin-1/SYT1 (PubMed:26280336, PubMed:28813412). {ECO:0000250|UniProtKB:O35526, ECO:0000250|UniProtKB:Q16623, ECO:0000269|PubMed:10336434, ECO:0000269|PubMed:10746715, ECO:0000269|PubMed:11533035, ECO:0000269|PubMed:11709063, ECO:0000269|PubMed:11832227, ECO:0000269|PubMed:12145319, ECO:0000269|PubMed:12496247, ECO:0000269|PubMed:12730201, ECO:0000269|PubMed:14665625, ECO:0000269|PubMed:16888141, ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:18167541, ECO:0000269|PubMed:18337752, ECO:0000269|PubMed:19196426, ECO:0000269|PubMed:19571812, ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:21785414, ECO:0000269|PubMed:22411134, ECO:0000269|PubMed:23341457, ECO:0000269|PubMed:26280336, ECO:0000269|PubMed:28813412, ECO:0000269|PubMed:9507000, ECO:0000269|PubMed:9759724}.

Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:O35526}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:O35526}. Cell membrane {ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:18167541, ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:22411134, ECO:0000269|PubMed:23341457}. Cell junction, synapse, synaptosome {ECO:0000250|UniProtKB:O35526}. Note=Colocalizes with KCNB1 at the cell membrane (PubMed:17301173). Colocalizes with PLCL1 at the cell membrane (PubMed:22673903). {ECO:0000269|PubMed:17301173}.

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

Ptm: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1. {ECO:0000269|PubMed:12730201}.

Ptm: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type C (BoNT/C), which hydrolyzes the 253-Lys-|-Ala-254 bond (PubMed:7737992). Cleavage inhibits neurotransmitter release (PubMed:7901002). {ECO:0000269|PubMed:7737992, ECO:0000269|PubMed:7901002}.

Ptm: Phosphorylated by CK2 (By similarity). Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16623}.

Ptm: Sumoylated, sumoylation is required for regulation of synaptic vesicle endocytosis. {ECO:0000250|UniProtKB:Q16623}.

Similarity: Belongs to the syntaxin family. {ECO:0000305}.

Sequence caution: Sequence=BAA01231.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



Function:		Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis (PubMed:7901002, PubMed:17301173, PubMed:18167541, PubMed:20484665, PubMed:22411134, PubMed:28813412). Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane (PubMed:14665625, PubMed:16888141, PubMed:19571812). STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion (PubMed:14665625, PubMed:16888141, PubMed:19571812). Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm (By similarity). Plays also an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity). {ECO:0000250\|UniProtKB:O35526, ECO:0000269\|PubMed:14665625, ECO:0000269\|PubMed:16888141, ECO:0000269\|PubMed:17301173, ECO:0000269\|PubMed:18167541, ECO:0000269\|PubMed:19571812, ECO:0000269\|PubMed:20484665, ECO:0000269\|PubMed:22411134, ECO:0000269\|PubMed:28813412, ECO:0000269\|PubMed:7901002}.


Subunit:		Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A; this complex constitutes the basic catalytic machinery of the complex neurotransmitter release apparatus (PubMed:14665625, PubMed:16888141, PubMed:19196426, PubMed:9759724, PubMed:11533035, PubMed:11832227, PubMed:12496247, PubMed:19571812, PubMed:28813412, PubMed:18337752, PubMed:21785414, PubMed:26280336). The SNARE complex interacts with CPLX1 (PubMed:21785414, PubMed:28813412). Interacts with STXBP1 (PubMed:10746715, PubMed:12730201, PubMed:18337752). Interacts (via C-terminus) with KCNB1 (via C-terminus); the interaction increases in a calcium-dependent manner and induces a pore-independent enhancement of exocytosis in neuroendocrine cells, chromaffin cells, pancreatic beta cells and from the soma of dorsal root ganglia (DRG) neurons (PubMed:17301173, PubMed:18167541, PubMed:20484665, PubMed:22411134). Interacts with SYTL4 (By similarity). Interacts with STXBP6 (PubMed:12145319). Interacts with PLCL1 (via C2 domain) (PubMed:23341457). Interacts with OTOF (By similarity). Interacts with LGI3 (By similarity). Interacts with SLC6A4 (PubMed:11709063). Interacts with SYT6 and SYT8; the interaction is Ca(2+)-dependent (By similarity). Interacts with VAMP8 (PubMed:10336434). Interacts with SNAP23 (PubMed:9507000). Interacts with VAPA and SYBU (By similarity). Interacts with PRRT2 (By similarity). Interacts with SEPT8 (PubMed:19196426). Interacts with STXBP5L (By similarity). Interacts with synaptotagmin-1/SYT1 (PubMed:26280336, PubMed:28813412). {ECO:0000250\|UniProtKB:O35526, ECO:0000250\|UniProtKB:Q16623, ECO:0000269\|PubMed:10336434, ECO:0000269\|PubMed:10746715, ECO:0000269\|PubMed:11533035, ECO:0000269\|PubMed:11709063, ECO:0000269\|PubMed:11832227, ECO:0000269\|PubMed:12145319, ECO:0000269\|PubMed:12496247, ECO:0000269\|PubMed:12730201, ECO:0000269\|PubMed:14665625, ECO:0000269\|PubMed:16888141, ECO:0000269\|PubMed:17301173, ECO:0000269\|PubMed:18167541, ECO:0000269\|PubMed:18337752, ECO:0000269\|PubMed:19196426, ECO:0000269\|PubMed:19571812, ECO:0000269\|PubMed:20484665, ECO:0000269\|PubMed:21785414, ECO:0000269\|PubMed:22411134, ECO:0000269\|PubMed:23341457, ECO:0000269\|PubMed:26280336, ECO:0000269\|PubMed:28813412, ECO:0000269\|PubMed:9507000, ECO:0000269\|PubMed:9759724}.
Subcellular location:		Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250\|UniProtKB:O35526}; Single-pass type IV membrane protein {ECO:0000250\|UniProtKB:O35526}. Cell membrane {ECO:0000269\|PubMed:17301173, ECO:0000269\|PubMed:18167541, ECO:0000269\|PubMed:20484665, ECO:0000269\|PubMed:22411134, ECO:0000269\|PubMed:23341457}. Cell junction, synapse, synaptosome {ECO:0000250\|UniProtKB:O35526}. Note=Colocalizes with KCNB1 at the cell membrane (PubMed:17301173). Colocalizes with PLCL1 at the cell membrane (PubMed:22673903). {ECO:0000269\|PubMed:17301173}.
Tissue specificity:		Expressed predominantly in cerebral cortex, hippocampus, cerebellum, adrenal medulla and retina with weak expression detected in non-neuronal tissues.
Ptm:		Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1. {ECO:0000269\|PubMed:12730201}.
Ptm:		(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type C (BoNT/C), which hydrolyzes the 253-Lys-\|-Ala-254 bond (PubMed:7737992). Cleavage inhibits neurotransmitter release (PubMed:7901002). {ECO:0000269\|PubMed:7737992, ECO:0000269\|PubMed:7901002}.
Ptm:		Phosphorylated by CK2 (By similarity). Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1 (By similarity). {ECO:0000250, ECO:0000250\|UniProtKB:Q16623}.
Ptm:		Sumoylated, sumoylation is required for regulation of synaptic vesicle endocytosis. {ECO:0000250\|UniProtKB:Q16623}.
Similarity:		Belongs to the syntaxin family. {ECO:0000305}.
Sequence caution:		Sequence=BAA01231.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};