##gff-version 3 P46097 UniProtKB Chain 1 422 . . . ID=PRO_0000183943;Note=Synaptotagmin-2 P46097 UniProtKB Topological domain 1 60 . . . Note=Vesicular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P46097 UniProtKB Transmembrane 61 87 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 P46097 UniProtKB Topological domain 88 422 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P46097 UniProtKB Domain 142 261 . . . Note=C2 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Domain 273 406 . . . Note=C2 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Region 1 43 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46097 UniProtKB Region 102 141 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46097 UniProtKB Region 136 382 . . . Note=Phospholipid binding;Ontology_term=ECO:0000305;evidence=ECO:0000305 P46097 UniProtKB Compositional bias 103 122 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46097 UniProtKB Compositional bias 123 137 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P46097 UniProtKB Binding site 172 172 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 173 173 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 173 173 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 179 179 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 231 231 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 231 231 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 232 232 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 233 233 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 233 233 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 233 233 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 236 236 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 237 237 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 239 239 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 239 239 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 304 304 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 310 310 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 364 364 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Binding site 366 366 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P46097 UniProtKB Modified residue 125 125 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29101 P46097 UniProtKB Modified residue 128 128 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P46097 UniProtKB Modified residue 202 202 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29101 P46097 UniProtKB Modified residue 230 230 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18034455;Dbxref=PMID:18034455 P46097 UniProtKB Modified residue 386 386 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P29101 P46097 UniProtKB Glycosylation 32 32 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P46097 UniProtKB Mutagenesis 47 47 . . . Note=No binding to C.botulinum neurotoxin type B (BoNT/B%2C botB). Requires gangliosides to bind BoNT/B%2C wild-type binding to BoNT/G. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17167418,ECO:0000269|PubMed:20219474;Dbxref=PMID:17167418,PMID:20219474 P46097 UniProtKB Mutagenesis 48 52 . . . Note=Wild-type binding to BoNT/B. AKLKE->SKLKQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17167418;Dbxref=PMID:17167418 P46097 UniProtKB Mutagenesis 50 50 . . . Note=Wild-type in binding to C.botulinum neurotoxin type G (BoNT/G%2C botG). L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20219474;Dbxref=PMID:20219474 P46097 UniProtKB Mutagenesis 52 55 . . . Note=Wild-type binding to BoNT/B. Wild-type in binding to BoNT/G. EKFF->QKFM;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17167418,ECO:0000269|PubMed:20219474;Dbxref=PMID:17167418,PMID:20219474 P46097 UniProtKB Mutagenesis 52 52 . . . Note=Wild-type binding to BoNT/B. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17167418;Dbxref=PMID:17167418 P46097 UniProtKB Mutagenesis 54 54 . . . Note=No binding to BoNT/B. No binding to BoNT/G. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17167418,ECO:0000269|PubMed:20219474;Dbxref=PMID:17167418,PMID:20219474 P46097 UniProtKB Mutagenesis 54 54 . . . Note=Requires gangliosides to bind BoNT/B%2C no binding to BoNT/G with or without gangliosides. F->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20219474;Dbxref=PMID:20219474 P46097 UniProtKB Mutagenesis 55 55 . . . Note=No binding to BoNT/B. Wild-type binding to BoNT/G. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17167418,ECO:0000269|PubMed:20219474;Dbxref=PMID:17167418,PMID:20219474 P46097 UniProtKB Mutagenesis 58 59 . . . Note=Only binds to BoNT/B in presence of gangliosides. IN->LH;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17167418;Dbxref=PMID:17167418 P46097 UniProtKB Sequence conflict 221 221 . . . Note=A->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P46097 UniProtKB Helix 46 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KBB