Syt1
entrez
25716
canonical
uniprot
P21707
canonical
ensembl
ENSRNOG00000006426
resolver
ensembl
ENSRNOG00055017023
resolver
ensembl
ENSRNOG00060003698
resolver
ensembl
ENSRNOG00065003237
resolver
ensp
ENSRNOP00000049624
resolver
ensp
ENSRNOP00055023267
resolver
ensp
ENSRNOP00060004535
resolver
ensp
ENSRNOP00065003286
resolver
enst
ENSRNOT00000048880
resolver
enst
ENSRNOT00055028911
resolver
enst
ENSRNOT00060006122
resolver
enst
ENSRNOT00065004587
resolver
genesymbol
Syt1
resolver
genesymbol_syn
syt1
resolver
uniprot
Q3S2E6
resolver
uniprot
Q707P0
resolver
uniprot
Q707P5
resolver
uniprot_entry
Q707P0_RAT
resolver
uniprot_entry
SYT1_RAT
resolver
uniprot_sec
Q3S2E6
resolver
uniprot_sec
Q707P5
resolver
amino_acid_sequence
MVSASHPEALAAPVTTVATLVPHNATEPASPGEGKEDAFSKLKQKFMNELHKIPLPPWALIAIAIVAVLLVVTCCFCVCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK
uniprot
proteins
function
FUNCTION: Calcium sensor that participates in triggering neurotransmitter release at the synapse (PubMed:2333096, 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:2333096, 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:14504267, PubMed:17167418, PubMed:8144634). 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}.
uniprot
proteins
mass_dalton
47399
uniprot
proteins
mutagenesis
MUTAGEN 47..50; /note="MNEL->FNEI: Greatly increased binding of fragment 1-53 to C.botulinum type B (BoNT/B, botB) heavy chain; increases its resemblance to Syt2."; /evidence="ECO:0000269|PubMed:17167421"; MUTAGEN 47; /note="M->F: Slightly increased binding of fragment 1-53 to BoNT/B heavy chain."; /evidence="ECO:0000269|PubMed:17167421"; MUTAGEN 50..51; /note="LH->IN: Binds to BoNT/B in the absence of gangliosides."; /evidence="ECO:0000269|PubMed:17167418"; MUTAGEN 50; /note="L->I: Increased binding of fragment 1-53 to BoNT/B heavy chain."; /evidence="ECO:0000269|PubMed:17167421"; MUTAGEN 233; /note="R->Q: Impaired Ca(2+)-affinity."; /evidence="ECO:0000269|PubMed:11823420"; MUTAGEN 302; /note="M->K: Fails to localize at nerve terminals."; /evidence="ECO:0000269|PubMed:30107533"; MUTAGEN 303; /note="D->G: Fails to relocalize to nerve terminals after stimulation of neurotransmitter release."; /evidence="ECO:0000269|PubMed:30107533"; MUTAGEN 365; /note="D->E: Fails to relocalize to nerve terminals after stimulation of neurotransmitter release."; /evidence="ECO:0000269|PubMed:30107533"; MUTAGEN 367; /note="I->T: Slows synaptic vesicle fusion kinetics and exocytosis. Impairs the kinetics of synaptic vesicle endocytosis."; /evidence="ECO:0000269|PubMed:25705886, ECO:0000269|PubMed:30107533"; MUTAGEN 370; /note="N->K: Slows synaptic vesicle fusion kinetics and exocytosis."; /evidence="ECO:0000269|PubMed:30107533
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:17190793}.
uniprot
proteins
protein_family
Synaptotagmin family
uniprot
proteins
pubmed
11438518
uniprot
proteins
pubmed
11754837
uniprot
proteins
pubmed
11823420
uniprot
proteins
pubmed
11931641
uniprot
proteins
pubmed
12782290
uniprot
proteins
pubmed
14504267
uniprot
proteins
pubmed
15123599
uniprot
proteins
pubmed
15238157
uniprot
proteins
pubmed
15866046
uniprot
proteins
pubmed
17167418
uniprot
proteins
pubmed
17167421
uniprot
proteins
pubmed
17190793
uniprot
proteins
pubmed
1985919
uniprot
proteins
pubmed
20219474
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2333096
uniprot
proteins
pubmed
25705886
uniprot
proteins
pubmed
25964652
uniprot
proteins
pubmed
28057568
uniprot
proteins
pubmed
30107533
uniprot
proteins
pubmed
7697723
uniprot
proteins
pubmed
8144634
uniprot
proteins
pubmed
8910372
uniprot
proteins
pubmed
9819203
uniprot
proteins
pubmed
9867811
uniprot
proteins
sequence_length
421
uniprot
proteins
subcellular_location
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, ECO:0000269|PubMed:9867811}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000269|PubMed:1985919}; Single-pass membrane protein. Cytoplasm.
uniprot
proteins
transmembrane_region
TRANSMEM 58..79; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins