UniProt functional annotation for P21707



	UniProt functional annotation for P21707

UniProt code: P21707.

Organism: Rattus norvegicus (Rat).

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

Function: Calcium sensor that participates in triggering neurotransmitter release at the synapse (PubMed:30107533). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes. {ECO:0000250|UniProtKB:P21579, ECO:0000269|PubMed:30107533}.

Function: (Microbial infection) Receptor for C.botulinum neurotoxin type B (BoNT/B, botB); interaction is improved in the presence of gangliosides (PubMed:8144634, PubMed:14504267, PubMed:17167418). BoNT/B toxin binds to the membrane proximal vesicular domain of Syt1 (residues 32-51) (PubMed:14504267, PubMed:17167421). {ECO:0000269|PubMed:14504267, ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:17167421, ECO:0000269|PubMed:8144634}.

Function: (Microbial infection) Receptor for C.botulinum neurotoxin type G (BoNT/G, botG); unlike the case with BoNT/B, interaction is not improved in the presence of gangliosides (PubMed:15123599, PubMed:20219474). BoNT/G toxin binds to the vesicular domain of Syt1 (residues 32-53) (PubMed:15123599, PubMed:20219474). {ECO:0000269|PubMed:15123599, ECO:0000269|PubMed:20219474}.

Cofactor: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|PubMed:11823420, ECO:0000269|PubMed:9819203}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains. {ECO:0000269|PubMed:9819203};

Subunit: Homotetramer (Probable). Interacts with SCAMP5 (By similarity). Interacts with STON2 (By similarity). Forms a complex with SV2B, syntaxin 1 and SNAP25 (By similarity). Interacts with SV2A, SV2B and SV2C (PubMed:8910372, PubMed:15866046). Interacts with RIMS1 (PubMed:11438518). Interacts with PRRT2 (By similarity). Interacts with DNAJC5 in a phosphorylation-dependent manner (PubMed:11931641). Interacts (via N-terminus) with RAB3A (PubMed:28057568). Interacts with SYT12 (PubMed:17190793). Interacts with calmodulin (By similarity). {ECO:0000250|UniProtKB:P21579, ECO:0000250|UniProtKB:P46096, ECO:0000250|UniProtKB:P48018, ECO:0000269|PubMed:11438518, ECO:0000269|PubMed:11931641, ECO:0000269|PubMed:15866046, ECO:0000269|PubMed:17190793, ECO:0000269|PubMed:28057568, ECO:0000269|PubMed:8910372, ECO:0000305}.

Subunit: (Microbial infection) Interacts with C.botulinum neurotoxin type B (BoNT/B, botB). Has lower affinity for BoNT/B than Syt2; mutating its residues to match those in Syt2 increases its affinity (PubMed:17167421, PubMed:17167418). {ECO:0000269|PubMed:14504267, ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:17167421, ECO:0000269|PubMed:20219474, ECO:0000269|PubMed:8144634}.

Subunit: (Microbial infection) Interacts with C.botulinum neurotoxin type G (BoNT/G, botG). {ECO:0000269|PubMed:15123599, ECO:0000269|PubMed:20219474}.

Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:11823420}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:17190793}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Single-pass membrane protein. Cytoplasm.

Tissue specificity: Expressed in the brain (at protein level) (PubMed:17190793). Predominantly expressed in rostral, phylogenetically younger brain regions, and in some endocrine tissues. {ECO:0000269|PubMed:17190793}.

Domain: The first C2 domain mediates Ca(2+)-dependent phospholipid binding. {ECO:0000269|PubMed:11823420, ECO:0000269|PubMed:8910372}.

Domain: The second C2 domain mediates interaction with SV2A and probably with STN2. {ECO:0000269|PubMed:8910372}.

Ptm: Glycosylated. {ECO:0000269|PubMed:17190793}.

Similarity: Belongs to the synaptotagmin family. {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:		Calcium sensor that participates in triggering neurotransmitter release at the synapse (PubMed:30107533). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes. {ECO:0000250\|UniProtKB:P21579, ECO:0000269\|PubMed:30107533}.



Function:		(Microbial infection) Receptor for C.botulinum neurotoxin type B (BoNT/B, botB); interaction is improved in the presence of gangliosides (PubMed:8144634, PubMed:14504267, PubMed:17167418). BoNT/B toxin binds to the membrane proximal vesicular domain of Syt1 (residues 32-51) (PubMed:14504267, PubMed:17167421). {ECO:0000269\|PubMed:14504267, ECO:0000269\|PubMed:17167418, ECO:0000269\|PubMed:17167421, ECO:0000269\|PubMed:8144634}.



Function:		(Microbial infection) Receptor for C.botulinum neurotoxin type G (BoNT/G, botG); unlike the case with BoNT/B, interaction is not improved in the presence of gangliosides (PubMed:15123599, PubMed:20219474). BoNT/G toxin binds to the vesicular domain of Syt1 (residues 32-53) (PubMed:15123599, PubMed:20219474). {ECO:0000269\|PubMed:15123599, ECO:0000269\|PubMed:20219474}.


Cofactor:		Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255\|PROSITE-ProRule:PRU00041, ECO:0000269\|PubMed:11823420, ECO:0000269\|PubMed:9819203}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains. {ECO:0000269\|PubMed:9819203};
Subunit:		Homotetramer (Probable). Interacts with SCAMP5 (By similarity). Interacts with STON2 (By similarity). Forms a complex with SV2B, syntaxin 1 and SNAP25 (By similarity). Interacts with SV2A, SV2B and SV2C (PubMed:8910372, PubMed:15866046). Interacts with RIMS1 (PubMed:11438518). Interacts with PRRT2 (By similarity). Interacts with DNAJC5 in a phosphorylation-dependent manner (PubMed:11931641). Interacts (via N-terminus) with RAB3A (PubMed:28057568). Interacts with SYT12 (PubMed:17190793). Interacts with calmodulin (By similarity). {ECO:0000250\|UniProtKB:P21579, ECO:0000250\|UniProtKB:P46096, ECO:0000250\|UniProtKB:P48018, ECO:0000269\|PubMed:11438518, ECO:0000269\|PubMed:11931641, ECO:0000269\|PubMed:15866046, ECO:0000269\|PubMed:17190793, ECO:0000269\|PubMed:28057568, ECO:0000269\|PubMed:8910372, ECO:0000305}.
Subunit:		(Microbial infection) Interacts with C.botulinum neurotoxin type B (BoNT/B, botB). Has lower affinity for BoNT/B than Syt2; mutating its residues to match those in Syt2 increases its affinity (PubMed:17167421, PubMed:17167418). {ECO:0000269\|PubMed:14504267, ECO:0000269\|PubMed:17167418, ECO:0000269\|PubMed:17167421, ECO:0000269\|PubMed:20219474, ECO:0000269\|PubMed:8144634}.
Subunit:		(Microbial infection) Interacts with C.botulinum neurotoxin type G (BoNT/G, botG). {ECO:0000269\|PubMed:15123599, ECO:0000269\|PubMed:20219474}.
Subcellular location:		Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269\|PubMed:11823420}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269\|PubMed:17190793}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Single-pass membrane protein. Cytoplasm.
Tissue specificity:		Expressed in the brain (at protein level) (PubMed:17190793). Predominantly expressed in rostral, phylogenetically younger brain regions, and in some endocrine tissues. {ECO:0000269\|PubMed:17190793}.
Domain:		The first C2 domain mediates Ca(2+)-dependent phospholipid binding. {ECO:0000269\|PubMed:11823420, ECO:0000269\|PubMed:8910372}.
Domain:		The second C2 domain mediates interaction with SV2A and probably with STN2. {ECO:0000269\|PubMed:8910372}.
Ptm:		Glycosylated. {ECO:0000269\|PubMed:17190793}.
Similarity:		Belongs to the synaptotagmin family. {ECO:0000305}.