Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00770
Entry Name
UniProt Accession
Theoretical PI
8.68
Molecular Weight
47418.0
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Synaptotagmin-1
Protein Synonyms/Alias
Synaptotagmin I; SytI; p65;
Gene Name
Syt1
Gene Synonyms/Alias
Created Date
01-NOV-1995
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
74
Canonical
AVLLVVTCCFCVCKK
[1][2]
S-Palmitoylation
75
Canonical
VLLVVTCCFCVCKKC
[1][2]
S-Palmitoylation
77
Canonical
LVVTCCFCVCKKCLF
[1][2]
S-Palmitoylation
79
Canonical
VTCCFCVCKKCLFKK
[1][2]
S-Palmitoylation
82
Canonical
CFCVCKKCLFKKKNK
[1][2]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Heindel U, Schmidt MF, Veit M. Palmitoylation sites and processing ofsynaptotagmin I, the putative calcium sensor for neurosecretion. FEBS Lett. 2003 Jun 5;544(1-3):57-62.[PMID:12782290]
[2] Kang R, Swayze R, Lise MF, Gerrow K, Mullard A, Honer WG, El-Husseini A.Presynaptic trafficking of synaptotagmin I is regulated by proteinpalmitoylation. J Biol Chem. 2004 Nov 26;279(48):50524-36. Epub 2004 Sep 7.[PMID:15355980]
Functional Description
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.
Sequence Annotation
Topological domain: 1 57 Vesicular.
Transmembrane: 58 79 Helical.
Topological domain: 80 421 Cytoplasmic.
Domain: 143 244 C2 1.
Domain: 274 377 C2 2.
Region: 135 381 Phospholipid binding.
Metal binding site: 171 171 Calcium 2; via carbonyl oxygen.
Metal binding site: 172 172 Calcium 1.
Metal binding site: 172 172 Calcium 2.
Metal binding site: 178 178 Calcium 1.
Metal binding site: 230 230 Calcium 1.
Metal binding site: 230 230 Calcium 2.
Metal binding site: 231 231 Calcium 1; via carbonyl oxygen.
Metal binding site: 232 232 Calcium 1.
Metal binding site: 232 232 Calcium 2.
Metal binding site: 232 232 Calcium 3.
Metal binding site: 235 235 Calcium 3.
Metal binding site: 236 236 Calcium 3; via carbonyl oxygen.
Metal binding site: 238 238 Calcium 2.
Metal binding site: 238 238 Calcium 3.
Modified residue: 128 128 Phosphothreonine.
Modified residue: 229 229 Phosphotyrosine.
Protein Length
421 AA.
Protein Sequence
(Canonical)
MVSASRPEAL AAPVTTVATL VPHNATEPAS PGEGKEDAFS KLKQKFMNEL HKIPLPPWAL  60
IAIAIVAVLL VVTCCFCVCK KCLFKKKNKK KGKEKGGKNA INMKDVKDLG KTMKDQALKD  120
DDAETGLTDG EEKEEPKEEE KLGKLQYSLD YDFQNNQLLV GIIQAAELPA LDMGGTSDPY  180
VKVFLLPDKK KKFETKVHRK TLNPVFNEQF TFKVPYSELG GKTLVMAVYD FDRFSKHDII  240
GEFKVPMNTV DFGHVTEEWR DLQSAEKEEQ EKLGDICFSL RYVPTAGKLT VVILEAKNLK  300
KMDVGGLSDP YVKIHLMQNG KRLKKKKTTI KKNTLNPYYN ESFSFEVPFE QIQKVQVVVT  360
VLDYDKIGKN DAIGKVFVGY NSTGAELRHW SDMLANPRRP IAQWHTLQVE EEVDAMLAVK  420
K                                                                  421
FASTA
(Canonical)
>LipidDB-10090-00770|P46096
MVSASRPEALAAPVTTVATLVPHNATEPASPGEGKEDAFSKLKQKFMNELHKIPLPPWAL
IAIAIVAVLLVVTCCFCVCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKD
DDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPY
VKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDII
GEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLK
KMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVT
VLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVK
K
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0031045; C:dense core granule; IEA:Ensembl
GO:0060076; C:excitatory synapse; IEA:Ensembl
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL
GO:0005886; C:plasma membrane; TAS:UniProtKB
GO:0042734; C:presynaptic membrane; IDA:MGI
GO:0030141; C:secretory granule; IDA:MGI
GO:0008021; C:synaptic vesicle; TAS:UniProtKB
GO:0030672; C:synaptic vesicle membrane; IDA:MGI
GO:0005509; F:calcium ion binding; IDA:MGI
GO:0005544; F:calcium-dependent phospholipid binding; ISS:ParkinsonsUK-UCL
GO:0048306; F:calcium-dependent protein binding; IPI:HGNC
GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI
GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl
GO:0001786; F:phosphatidylserine binding; IEA:Ensembl
GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL
GO:0017075; F:syntaxin-1 binding; ISS:ParkinsonsUK-UCL
GO:0005215; F:transporter activity; IEA:InterPro
GO:0048791; P:calcium ion-dependent exocytosis of neurotransmitter; IDA:ParkinsonsUK-UCL
GO:0007269; P:neurotransmitter secretion; IDA:MGI
GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IEA:Ensembl
GO:0050806; P:positive regulation of synaptic transmission; IMP:ParkinsonsUK-UCL
GO:0031340; P:positive regulation of vesicle fusion; IEA:Ensembl
GO:1903305; P:regulation of regulated secretory pathway; ISS:ParkinsonsUK-UCL
GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:ParkinsonsUK-UCL
GO:0051592; P:response to calcium ion; IEA:Ensembl
GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI
GO:0048278; P:vesicle docking; IEA:Ensembl
Interpro
InterPro; IPR000008; C2_dom
InterPro; IPR001565; Synaptotagmin
InterPro; IPR015428; Synaptotagmin1
Pfam
Pfam; PF00168; C2;
SMART
SMART; SM00239; C2;
PROSITE
PROSITE; PS50004; C2;
PRINTS
PRINTS; PR00360; C2DOMAIN;
PRINTS; PR00399; SYNAPTOTAGMN;