Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01430
Entry Name
UniProt Accession
Theoretical PI
9.33
Molecular Weight
45472.32
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Synaptotagmin-7
Protein Synonyms/Alias
Synaptotagmin VII; SytVII;
Gene Name
Syt7
Gene Synonyms/Alias
Created Date
18-OCT-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
35
Canonical
LSVTIVLCGLCHWCQ
[1]
S-Palmitoylation
38
Canonical
TIVLCGLCHWCQRKL
[1]
S-Palmitoylation
41
Canonical
LCGLCHWCQRKLGKR
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] 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 be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis.
Sequence Annotation
Topological domain: 1 16 Vesicular.
Transmembrane: 17 37 Helical.
Topological domain: 38 403 Cytoplasmic.
Domain: 137 239 C2 1.
Domain: 268 371 C2 2.
Metal binding site: 166 166 Calcium 1.
Metal binding site: 166 166 Calcium 2.
Metal binding site: 172 172 Calcium 1.
Metal binding site: 225 225 Calcium 1.
Metal binding site: 225 225 Calcium 2.
Metal binding site: 227 227 Calcium 1.
Metal binding site: 227 227 Calcium 2.
Metal binding site: 227 227 Calcium 3.
Metal binding site: 230 230 Calcium 3.
Metal binding site: 233 233 Calcium 2.
Metal binding site: 233 233 Calcium 3.
Protein Length
403 AA.
Protein Sequence
(Canonical)
MYRDPEAASP GAPTRDVLLV SAIITVSLSV TIVLCGLCHW CQRKLGKRYK NSLETVGTPD  60
SGRGRGEKKA IKLPAGGKAV NTAPVPGQTP HDESDRRTET RSSVSDLVNS LTSEMLMLSP  120
GSEEDEAHEG CSRENLGRIQ FSVGYNFQES TLTVKVMKAQ ELPAKDFSGT SDPFVKIYLL  180
PDKKHKLETK VKRKNLNPHW NETFLFEGFP YEKVVQRVLY LQVLDYDRFS RNDPIGEVSI  240
PLNKVDLTQM QTFWKDLKPC SDGSGSRGEL LLSLCYNPSA NSIIVNIIKA RNLKAMDIGG  300
TSDPYVKVWL MYKDKRVEKK KTVTKKRNLN PIFNESFAFD IPTEKLRETT IIITVMDKDK  360
LSRNDVIGKI YLSWKSGPGE VKHWKDMIAR PRQPVAQWHQ LKA                    403
FASTA
(Canonical)
>LipidDB-10090-01430|Q9R0N7
MYRDPEAASPGAPTRDVLLVSAIITVSLSVTIVLCGLCHWCQRKLGKRYKNSLETVGTPD
SGRGRGEKKAIKLPAGGKAVNTAPVPGQTPHDESDRRTETRSSVSDLVNSLTSEMLMLSP
GSEEDEAHEGCSRENLGRIQFSVGYNFQESTLTVKVMKAQELPAKDFSGTSDPFVKIYLL
PDKKHKLETKVKRKNLNPHWNETFLFEGFPYEKVVQRVLYLQVLDYDRFSRNDPIGEVSI
PLNKVDLTQMQTFWKDLKPCSDGSGSRGELLLSLCYNPSANSIIVNIIKARNLKAMDIGG
TSDPYVKVWLMYKDKRVEKKKTVTKKRNLNPIFNESFAFDIPTEKLRETTIIITVMDKDK
LSRNDVIGKIYLSWKSGPGEVKHWKDMIARPRQPVAQWHQLKA
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005764; C:lysosome; IDA:MGI
GO:0008021; C:synaptic vesicle; IEA:InterPro
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0005215; F:transporter activity; IEA:InterPro
GO:0006887; P:exocytosis; IEA:InterPro
GO:0001778; P:plasma membrane repair; IDA:MGI
Interpro
InterPro; IPR000008; C2_dom
InterPro; IPR001565; Synaptotagmin
InterPro; IPR015427; Synaptotagmin7
Pfam
Pfam; PF00168; C2;
SMART
SMART; SM00239; C2;
PROSITE
PROSITE; PS50004; C2;
PRINTS
PRINTS; PR00360; C2DOMAIN;
PRINTS; PR00399; SYNAPTOTAGMN;