[1]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/345260a0; PubMed=2333096 [NCBI, ExPASy, EBI, Israel, Japan]
Perin M.S.,
Fried V.A.,
Mignery G.A.,
Jahn R.,
Suedhof T.C.;
"Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C.";
Nature 345:260-263(1990).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1186/1471-2164-5-43; PubMed=15238157 [NCBI, ExPASy, EBI, Israel, Japan]
Craxton M.A.;
"Synaptotagmin gene content of the sequenced genomes.";
BMC Genomics 5:43-43(2004).
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[3]
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NUCLEOTIDE SEQUENCE.
STRAIN=Wistar;
Sunitha S.S.,
Thekkuveettil A.;
"Functional analysis of synaptotagmin.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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[4]
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PROTEIN SEQUENCE OF 214-233; 289-297; 355-366 AND 376-388, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus;
Lubec G.,
Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
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[5]
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INTERACTION WITH SV2A, AND DOMAIN.
DOI=10.1074/jbc.271.44.27770; PubMed=8910372 [NCBI, ExPASy, EBI, Israel, Japan]
Schivell A.E.,
Batchelor R.H.,
Bajjalieh S.M.;
"Isoform-specific, calcium-regulated interaction of the synaptic vesicle proteins SV2 and synaptotagmin.";
J. Biol. Chem. 271:27770-27775(1996).
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[6]
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INTERACTION WITH RIMS1.
TISSUE=Brain;
DOI=10.1074/jbc.M100929200; PubMed=11438518 [NCBI, ExPASy, EBI, Israel, Japan]
Coppola T.,
Magnin-Luethi S.,
Perret-Menoud V.,
Gattesco S.,
Schiavo G.,
Regazzi R.;
"Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin.";
J. Biol. Chem. 276:32756-32762(2001).
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[7]
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PALMITOYLATION AT CYS-74; CYS-75; CYS-77; CYS-79 AND CYS-82.
DOI=10.1016/S0014-5793(03)00449-6; PubMed=12782290 [NCBI, ExPASy, EBI, Israel, Japan]
Heindel U.,
Schmidt M.F.,
Veit M.;
"Palmitoylation sites and processing of synaptotagmin I, the putative calcium sensor for neurosecretion.";
FEBS Lett. 544:57-62(2003).
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[8]
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INTERACTION WITH SV2A; SV2B AND SV2C.
DOI=10.1016/j.mcn.2004.12.011; PubMed=15866046 [NCBI, ExPASy, EBI, Israel, Japan]
Schivell A.E.,
Mochida S.,
Kensel-Hammes P.,
Custer K.L.,
Bajjalieh S.M.;
"SV2A and SV2C contain a unique synaptotagmin-binding site.";
Mol. Cell. Neurosci. 29:56-64(2005).
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[9]
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X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 132-266.
DOI=10.1016/0092-8674(95)90296-1; PubMed=7697723 [NCBI, ExPASy, EBI, Israel, Japan]
Sutton R.B.,
Davletov B.A.,
Berghuis A.M.,
Suedhof T.C.,
Sprang S.R.;
"Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold.";
Cell 80:929-938(1995).
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[10]
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STRUCTURE BY NMR OF 140-267.
DOI=10.1021/bi981789h; PubMed=9819203 [NCBI, ExPASy, EBI, Israel, Japan]
Shao X.,
Fernandez I.,
Suedhof T.C.,
Rizo J.;
"Solution structures of the Ca2+-free and Ca2+-bound C2A domain of synaptotagmin I: does Ca2+ induce a conformational change?";
Biochemistry 37:16106-16115(1998).
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[11]
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STRUCTURE BY NMR OF 270-421.
DOI=10.1016/S0896-6273(01)00548-7; PubMed=11754837 [NCBI, ExPASy, EBI, Israel, Japan]
Fernandez I.,
Arac D.,
Ubach J.,
Gerber S.H.,
Shin O.,
Gao Y.,
Anderson R.G.,
Suedhof T.C.,
Rizo J.;
"Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine.";
Neuron 32:1057-1069(2001).
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- FUNCTION: 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.
- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to the C2 domains.
- SUBUNIT: Homotetramer (Probable). Interacts with SCAMP5 and STN2. Forms a complex with SV2B, syntaxin 1 and SNAP25 (By similarity). Interacts with RIMS1. Interacts with SV2A, SV2B and SV2C.
- INTERACTION:
Self; NbExp=1; IntAct=EBI-458098, EBI-458098;
P18484:Ap2a2; NbExp=2; IntAct=EBI-458098, EBI-539360;
Q02294:Cacna1b; NbExp=1; IntAct=EBI-458098, EBI-540038;
Q8WXE9:STON2 (xeno); NbExp=1; IntAct=EBI-458098, EBI-539742;
Q8BZ60:Ston2 (xeno); NbExp=1; IntAct=EBI-458098, EBI-539385;
Q02563:Sv2a; NbExp=1; IntAct=EBI-458098, EBI-466194;
P40748:Syt3; NbExp=1; IntAct=EBI-458098, EBI-458106;
P50232:Syt4; NbExp=1; IntAct=EBI-458098, EBI-540118;
- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Single-pass membrane protein. Cytoplasm. Note=Synaptic vesicles and chromaffin granules.
- TISSUE SPECIFICITY: Predominantly expressed in rostral, phylogenetically younger brain regions, and in some endocrine tissues.
- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid binding.
- DOMAIN: The second C2 domain mediates interaction with SV2A and probably with STN2.
- SIMILARITY: Belongs to the synaptotagmin family.
- SIMILARITY: Contains 2 C2 domains.
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