Syt2
entrez
20980
canonical
uniprot
P46097
canonical
ensembl
ENSMUSG00000026452
resolver
ensp
ENSMUSP00000112438
resolver
ensp
ENSMUSP00000140081
resolver
ensp
ENSMUSP00000314390
resolver
enst
ENSMUST00000121990
resolver
enst
ENSMUST00000188842
resolver
genesymbol
Syt2
resolver
uniprot
A0A0R4J2C2
resolver
uniprot
Q8R0E1
resolver
uniprot_entry
A0A0R4J2C2_MOUSE
resolver
uniprot_entry
SYT2_MOUSE
resolver
uniprot_sec
Q8R0E1
resolver
amino_acid_sequence
MRNIFKRNQEPNVAPATTTATMPLAPVAPADNSTESTGPGESQEDMFAKLKEKFFNEINKIPLPPWALIAMAVVAGLLLLTCCFCICKKCCCKKKKNKKEKGKGMKNAMNMKDMKGGQDDDDAETGLTEGEGEGEEEKEPENLGKLQFSLDYDFQANQLTVGVLQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPAFNETFTFKVPYQELAGKTLVMAIYDFDRFSKHDIIGEVKVPMNTVDLGQPIEEWRDLQGGEKEEPEKLGDICTSLRYVPTAGKLTVCILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTVKKKTLNPYFNESFSFEIPFEQIQKVQVVVTVLDYDKLGKNEAIGKIFVGSNATGTELRHWSDMLANPRRPIAQWHSLKPEEEVDALLGKNK
uniprot
proteins
function
FUNCTION: Exhibits calcium-dependent phospholipid and inositol polyphosphate binding properties (PubMed:7961887). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse (PubMed:7961887). Plays a role in dendrite formation by melanocytes (By similarity). {ECO:0000250|UniProtKB:Q8N9I0, ECO:0000269|PubMed:7961887}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type B (BoNT/B, botB); interaction is improved in the presence of gangliosides (PubMed:14504267). The toxin binds via the vesicular domain (residues 47-60) (PubMed:14504267, PubMed:17167418, PubMed:23807078). {ECO:0000269|PubMed:14504267, ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:23807078}.; FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin type G (BoNT/G, botG); gangliosides are not required for (or only very slightly improve) binding to a membrane-anchored receptor fragment (PubMed:20219474). The toxin binds via the vesicular domain (residues 47-55) (PubMed:20219474). {ECO:0000269|PubMed:20219474}.
uniprot
proteins
mass_dalton
47263
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="F->A: No binding to C.botulinum neurotoxin type B (BoNT/B, botB). Requires gangliosides to bind BoNT/B, wild-type binding to BoNT/G."; /evidence="ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:20219474"; MUTAGEN 48..52; /note="AKLKE->SKLKQ: Wild-type binding to BoNT/B."; /evidence="ECO:0000269|PubMed:17167418"; MUTAGEN 50; /note="L->A: Wild-type in binding to C.botulinum neurotoxin type G (BoNT/G, botG)."; /evidence="ECO:0000269|PubMed:20219474"; MUTAGEN 52..55; /note="EKFF->QKFM: Wild-type binding to BoNT/B. Wild-type in binding to BoNT/G."; /evidence="ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:20219474"; MUTAGEN 52; /note="E->A: Wild-type binding to BoNT/B."; /evidence="ECO:0000269|PubMed:17167418"; MUTAGEN 54; /note="F->A: No binding to BoNT/B. No binding to BoNT/G."; /evidence="ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:20219474"; MUTAGEN 54; /note="F->M: Requires gangliosides to bind BoNT/B, no binding to BoNT/G with or without gangliosides."; /evidence="ECO:0000269|PubMed:20219474"; MUTAGEN 55; /note="F->A: No binding to BoNT/B. Wild-type binding to BoNT/G."; /evidence="ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:20219474"; MUTAGEN 58..59; /note="IN->LH: Only binds to BoNT/B in presence of gangliosides."; /evidence="ECO:0000269|PubMed:17167418
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-202 by WNK1, changes the calcium requirement for SYT2-binding to phospholipid membranes. {ECO:0000250|UniProtKB:P29101}.
uniprot
proteins
protein_family
Synaptotagmin family
uniprot
proteins
pubmed
14504267
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17167418
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
20219474
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23807078
uniprot
proteins
pubmed
27052163
uniprot
proteins
pubmed
7961887
uniprot
proteins
sequence_length
422
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P29101}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein {ECO:0000250|UniProtKB:P29101}. Cytoplasm {ECO:0000250|UniProtKB:P29101}.
uniprot
proteins
transmembrane_region
TRANSMEM 61..87; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins