Syt7
entrez
59267
canonical
uniprot
Q62747
canonical
ensembl
ENSRNOG00000026432
resolver
ensembl
ENSRNOG00055017972
resolver
ensembl
ENSRNOG00060023249
resolver
ensembl
ENSRNOG00065024873
resolver
ensp
ENSRNOP00000031195
resolver
ensp
ENSRNOP00000031890
resolver
ensp
ENSRNOP00000031944
resolver
ensp
ENSRNOP00000032388
resolver
ensp
ENSRNOP00000040667
resolver
ensp
ENSRNOP00000049360
resolver
ensp
ENSRNOP00000085392
resolver
enst
ENSRNOT00000099494
resolver
genesymbol
Syt7
resolver
uniprot
A0A8I6A1J0
resolver
uniprot
F1M262
resolver
uniprot
Q99J98
resolver
uniprot
Q99P33
resolver
uniprot
Q99P34
resolver
uniprot
Q99P35
resolver
uniprot
Q99P36
resolver
uniprot
Q99P37
resolver
uniprot
Q99P38
resolver
uniprot_entry
A0A8I6A1J0_RAT
resolver
uniprot_entry
SYT7_RAT
resolver
uniprot_sec
F1M262
resolver
uniprot_sec
Q99J98
resolver
uniprot_sec
Q99P33
resolver
uniprot_sec
Q99P34
resolver
uniprot_sec
Q99P35
resolver
uniprot_sec
Q99P36
resolver
uniprot_sec
Q99P37
resolver
uniprot_sec
Q99P38
resolver
amino_acid_sequence
MYRDPEAASPGAPTRDVLLVSAIITVSLSVTIVLCGLCHWCQRKLGKRYKNSLETVGTPDSGRGRGEKKAIKLPAGGKAVNTAPVPGQTPHDESDRRTEPRSSVSDLVNSLTSEMLMLSPGSEEDEAHEGCSRENLGRIQFSVGYNFQESTLTVKVMKAQELPAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETFLFEGFPYEKVVQRILYLQVLDYDRFSRNDPIGEVSIPLNKVDLTQMQTFWKDLKPCSDGSGSRGELLLSLCYNPSANSIIVNIIKARNLKAMDIGGTSDPYVKVWLMYKDKRVEKKKTVTKKRNLNPIFNESFAFDIPTEKLRETTIIITVMDKDKLSRNDVIGKIYLSWKSGPGEVKHWKDMIARPRQPVAQWHQLKA
uniprot
proteins
function
FUNCTION: Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory and synaptic vesicles through Ca(2+) and phospholipid binding to the C2 domain (PubMed:10725327, PubMed:11395007, PubMed:11511344). Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (PubMed:11395007). SYT7 binds Ca(2+) with high affinity and slow kinetics compared to other synaptotagmins (By similarity). Involved in Ca(2+)-triggered lysosomal exocytosis, a major component of the plasma membrane repair (PubMed:10725327, PubMed:11511344). Ca(2+)-regulated delivery of lysosomal membranes to the cell surface is also involved in the phagocytic uptake of particles by macrophages. Ca(2+)-triggered lysosomal exocytosis also plays a role in bone remodeling by regulating secretory pathways in osteoclasts and osteoblasts. Involved in cholesterol transport from lysosome to peroxisome by promoting membrane contacts between lysosomes and peroxisomes: probably acts by promoting vesicle fusion by binding phosphatidylinositol-4,5-bisphosphate on peroxisomal membranes. Acts as a key mediator of synaptic facilitation, a process also named short-term synaptic potentiation: synaptic facilitation takes place at synapses with a low initial release probability and is caused by influx of Ca(2+) into the axon terminal after spike generation, increasing the release probability of neurotransmitters. Probably mediates synaptic facilitation by directly increasing the probability of release. May also contribute to synaptic facilitation by regulating synaptic vesicle replenishment, a process required to ensure that synaptic vesicles are ready for the arrival of the next action potential: SYT7 is required for synaptic vesicle replenishment by acting as a sensor for Ca(2+) and by forming a complex with calmodulin. Also acts as a regulator of Ca(2+)-dependent insulin and glucagon secretion in beta-cells. Triggers exocytosis by promoting fusion pore opening and fusion pore expansion in chromaffin cells (By similarity). Also regulates the secretion of some non-synaptic secretory granules of specialized cells (PubMed:15456748). {ECO:0000250|UniProtKB:Q9R0N7, ECO:0000269|PubMed:10725327, ECO:0000269|PubMed:11395007, ECO:0000269|PubMed:11511344, ECO:0000269|PubMed:15456748}.
uniprot
proteins
mass_dalton
45482
uniprot
proteins
mutagenesis
MUTAGEN 172; /note="D->N: Loss of Ca(2+)-binding in the first C2 domain; when associated with N-225."; /evidence="ECO:0000269|PubMed:11395007"; MUTAGEN 225; /note="D->N: Loss of Ca(2+)-binding in the first C2 domain; when associated with N-172."; /evidence="ECO:0000269|PubMed:11395007
uniprot
proteins
post_translational_modification
PTM: Palmitoylated at its vesicular N-terminus; palmitoylation is required for localization to lysosome and phagocytosis in macrophages. {ECO:0000250|UniProtKB:Q9R0N7}.
uniprot
proteins
protein_family
Synaptotagmin family
uniprot
proteins
pubmed
10725327
uniprot
proteins
pubmed
11395007
uniprot
proteins
pubmed
11511344
uniprot
proteins
pubmed
11823420
uniprot
proteins
pubmed
12071850
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15456748
uniprot
proteins
pubmed
17190793
uniprot
proteins
pubmed
18508778
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
7791877
uniprot
proteins
sequence_length
403
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11823420}; Single-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:17190793}; Single-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:10725327}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:15456748}; Single-pass membrane protein {ECO:0000255}. Note=Localization to lysosomes is dependent on N-terminal palmitoylation and interaction with CD63. {ECO:0000250|UniProtKB:Q9R0N7}.
uniprot
proteins
transmembrane_region
TRANSMEM 17..37; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins