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Synaptotagmin-7 (Synaptotagmin VII) (SytVII)

 SYT7_MOUSE              Reviewed;         403 AA.
Q9R0N7; A4QPF1; E9PZA8; Q0D2K7; Q8CF95; Q8CF96;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 137.
RecName: Full=Synaptotagmin-7 {ECO:0000305};
AltName: Full=Synaptotagmin VII {ECO:0000303|PubMed:10531343};
Short=SytVII {ECO:0000303|PubMed:10531343};
Name=Syt7 {ECO:0000312|MGI:MGI:1859545};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=ICR; TISSUE=Cerebellum;
PubMed=10531343; DOI=10.1074/jbc.274.44.31421;
Fukuda M., Kanno E., Mikoshiba K.;
"Conserved N-terminal cysteine motif is essential for homo- and
heterodimer formation of synaptotagmins III, V, VI, and X.";
J. Biol. Chem. 274:31421-31427(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=12071850; DOI=10.1042/BJ20011877;
Fukuda M., Ogata Y., Saegusa C., Kanno E., Mikoshiba K.;
"Alternative splicing isoforms of synaptotagmin VII in the mouse, rat
and human.";
Biochem. J. 365:173-180(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBUNIT.
PubMed=10871604; DOI=10.1074/jbc.M001376200;
Fukuda M., Mikoshiba K.;
"Distinct self-oligomerization activities of synaptotagmin family.
Unique calcium-dependent oligomerization properties of synaptotagmin
VII.";
J. Biol. Chem. 275:28180-28185(2000).
[6]
SUBCELLULAR LOCATION.
PubMed=11395007; DOI=10.1016/S0896-6273(01)00290-2;
Sugita S., Han W., Butz S., Liu X., Fernandez-Chacon R., Lao Y.,
Sudhof T.C.;
"Synaptotagmin VII as a plasma membrane Ca(2+) sensor in exocytosis.";
Neuron 30:459-473(2001).
[7]
DISRUPTION PHENOTYPE.
PubMed=12925704; DOI=10.1083/jcb.200305131;
Chakrabarti S., Kobayashi K.S., Flavell R.A., Marks C.B., Miyake K.,
Liston D.R., Fowler K.T., Gorelick F.S., Andrews N.W.;
"Impaired membrane resealing and autoimmune myositis in synaptotagmin
VII-deficient mice.";
J. Cell Biol. 162:543-549(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 225-ASP--ASP-227
AND 357-ASP--ASP-359.
PubMed=16982801; DOI=10.1083/jcb.200605004;
Czibener C., Sherer N.M., Becker S.M., Pypaert M., Hui E.,
Chapman E.R., Mothes W., Andrews N.W.;
"Ca2+ and synaptotagmin VII-dependent delivery of lysosomal membrane
to nascent phagosomes.";
J. Cell Biol. 174:997-1007(2006).
[9]
DISRUPTION PHENOTYPE.
PubMed=17720139; DOI=10.1016/j.bbrc.2007.08.023;
Li Y., Wang P., Xu J., Gorelick F., Yamazaki H., Andrews N.,
Desir G.V.;
"Regulation of insulin secretion and GLUT4 trafficking by the calcium
sensor synaptotagmin VII.";
Biochem. Biophys. Res. Commun. 362:658-664(2007).
[10]
FUNCTION.
PubMed=18539119; DOI=10.1016/j.devcel.2008.03.022;
Zhao H., Ito Y., Chappel J., Andrews N.W., Teitelbaum S.L., Ross F.P.;
"Synaptotagmin VII regulates bone remodeling by modulating osteoclast
and osteoblast secretion.";
Dev. Cell 14:914-925(2008).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=18308938; DOI=10.1073/pnas.0711700105;
Gustavsson N., Lao Y., Maximov A., Chuang J.C., Kostromina E.,
Repa J.J., Li C., Radda G.K., Suedhof T.C., Han W.;
"Impaired insulin secretion and glucose intolerance in synaptotagmin-7
null mutant mice.";
Proc. Natl. Acad. Sci. U.S.A. 105:3992-3997(2008).
[12]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=19171650; DOI=10.1113/jphysiol.2008.168005;
Gustavsson N., Wei S.H., Hoang D.N., Lao Y., Zhang Q., Radda G.K.,
Rorsman P., Suedhof T.C., Han W.;
"Synaptotagmin-7 is a principal Ca2+ sensor for Ca2+ -induced glucagon
exocytosis in pancreas.";
J. Physiol. (Lond.) 587:1169-1178(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; THR-58; SER-61 AND
SER-122, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
FUNCTION, PALMITOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH CD63,
AND MUTAGENESIS OF 35-CYS--CYS-43.
PubMed=21041449; DOI=10.1083/jcb.201003021;
Flannery A.R., Czibener C., Andrews N.W.;
"Palmitoylation-dependent association with CD63 targets the Ca2+
sensor synaptotagmin VII to lysosomes.";
J. Cell Biol. 191:599-613(2010).
[15]
FUNCTION.
PubMed=20956309; DOI=10.1073/pnas.1014070107;
Segovia M., Ales E., Montes M.A., Bonifas I., Jemal I., Lindau M.,
Maximov A., Suedhof T.C., Alvarez de Toledo G.;
"Push-and-pull regulation of the fusion pore by synaptotagmin-7.";
Proc. Natl. Acad. Sci. U.S.A. 107:19032-19037(2010).
[16]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH
CALMODULIN, AND MUTAGENESIS OF 225-ASP--ASP-227 AND 357-ASP--ASP-359.
PubMed=24569478; DOI=10.7554/eLife.01524;
Liu H., Bai H., Hui E., Yang L., Evans C.S., Wang Z., Kwon S.E.,
Chapman E.R.;
"Synaptotagmin 7 functions as a Ca2+-sensor for synaptic vesicle
replenishment.";
Elife 3:E01524-E01524(2014).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-169 AND ARG-171 (ISOFORM 4),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=25860611; DOI=10.1016/j.cell.2015.02.019;
Chu B.B., Liao Y.C., Qi W., Xie C., Du X., Wang J., Yang H.,
Miao H.H., Li B.L., Song B.L.;
"Cholesterol transport through lysosome-peroxisome membrane
contacts.";
Cell 161:291-306(2015).
[19]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 225-ASP--ASP-232.
PubMed=26738595; DOI=10.1038/nature16507;
Jackman S.L., Turecek J., Belinsky J.E., Regehr W.G.;
"The calcium sensor synaptotagmin 7 is required for synaptic
facilitation.";
Nature 529:88-91(2016).
[20] {ECO:0000244|PDB:3N5A}
X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 266-403 IN COMPLEX WITH
CALCIUM, AND COFACTOR.
PubMed=20824061; DOI=10.1371/journal.pone.0012544;
Xue M., Craig T.K., Shin O.H., Li L., Brautigam C.A., Tomchick D.R.,
Sudhof T.C., Rosenmund C., Rizo J.;
"Structural and mutational analysis of functional differentiation
between synaptotagmins-1 and -7.";
PLoS ONE 5:E12544-E12544(2010).
-!- 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. Ca(2+) induces binding of the C2-domains
to phospholipid membranes and to assembled SNARE-complexes; both
actions contribute to triggering exocytosis. SYT7 binds Ca(2+)
with high affinity and slow kinetics compared to other
synaptotagmins (PubMed:26738595). Involved in Ca(2+)-triggered
lysosomal exocytosis, a major component of the plasma membrane
repair (By similarity). Ca(2+)-regulated delivery of lysosomal
membranes to the cell surface is also involved in the phagocytic
uptake of particles by macrophages (PubMed:16982801,
PubMed:21041449). Ca(2+)-triggered lysosomal exocytosis also plays
a role in bone remodeling by regulating secretory pathways in
osteoclasts and osteoblasts (PubMed:18539119). 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 (PubMed:25860611). 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
(PubMed:24569478, PubMed:26738595). Probably mediates synaptic
facilitation by directly increasing the probability of release
(PubMed:26738595). 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 (PubMed:24569478). Also acts as a
regulator of Ca(2+)-dependent insulin and glucagon secretion in
beta-cells (PubMed:18308938, PubMed:19171650). Triggers exocytosis
by promoting fusion pore opening and fusion pore expansion in
chromaffin cells (PubMed:20956309). Also regulates the secretion
of some non-synaptic secretory granules of specialized cells (By
similarity). {ECO:0000250|UniProtKB:Q62747,
ECO:0000269|PubMed:16982801, ECO:0000269|PubMed:18308938,
ECO:0000269|PubMed:18539119, ECO:0000269|PubMed:19171650,
ECO:0000269|PubMed:20956309, ECO:0000269|PubMed:21041449,
ECO:0000269|PubMed:24569478, ECO:0000269|PubMed:25860611,
ECO:0000269|PubMed:26738595}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:20824061};
Note=Binds 3 Ca(2+) ions per C2 domain.
{ECO:0000269|PubMed:20824061};
-!- SUBUNIT: Homodimer (PubMed:10871604). Can also form heterodimers
with SYT6, SYT9 and SYT10 (PubMed:10871604). Interacts with
calmodulin (CALM1, CALM2 or CALM3) (PubMed:24569478). Interacts
with CD63; required for localization to lysosomes
(PubMed:21041449). {ECO:0000269|PubMed:10871604,
ECO:0000269|PubMed:21041449, ECO:0000269|PubMed:24569478}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q62747}; Single-pass membrane protein
{ECO:0000255}. Cell junction, synapse, presynaptic cell membrane
{ECO:0000269|PubMed:11395007}; Single-pass membrane protein
{ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic
vesicle membrane {ECO:0000269|PubMed:24569478}; Single-pass
membrane protein {ECO:0000255}. Lysosome membrane
{ECO:0000269|PubMed:21041449, ECO:0000269|PubMed:25860611};
Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle,
phagosome membrane {ECO:0000269|PubMed:16982801}; Single-pass
membrane protein {ECO:0000255}. Peroxisome membrane
{ECO:0000269|PubMed:25860611}; Single-pass membrane protein
{ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane
{ECO:0000250|UniProtKB:Q62747}; Single-pass membrane protein
{ECO:0000255}. Note=Localization to lysosomes is dependent on N-
terminal palmitoylation and interaction with CD63.
{ECO:0000269|PubMed:21041449}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Synaptotagmin VIIalpha
{ECO:0000303|PubMed:12071850}, Syt7alpha {ECO:0000305};
IsoId=Q9R0N7-1; Sequence=Displayed;
Note=Major isoform. {ECO:0000269|PubMed:12071850};
Name=2; Synonyms=Synaptotagmin VIIgamma
{ECO:0000303|PubMed:12071850}, Syt7gamma {ECO:0000305};
IsoId=Q9R0N7-2; Sequence=VSP_058236;
Name=3; Synonyms=Synaptotagmin VIIbeta
{ECO:0000303|PubMed:12071850}, Syt7beta {ECO:0000305};
IsoId=Q9R0N7-3; Sequence=VSP_058235;
Name=4;
IsoId=Q9R0N7-4; Sequence=VSP_058237;
Note=Contains a asymmetric dimethylarginine at position 169.
Contains a asymmetric dimethylarginine at position 171.
{ECO:0000244|PubMed:24129315};
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in insulin-
secreting cells (PubMed:18308938). Present in glucagon-secreting
cells (at protein level) (PubMed:19171650).
{ECO:0000269|PubMed:18308938, ECO:0000269|PubMed:19171650}.
-!- DOMAIN: The C2 domains bind Ca(2+) and membranes. Binding to
membranes involves Ca(2+)-dependent phospholipid binding. Compared
to other members of the family, the C2 domains of SYT7 dock and
insert into cellular membranes in response to intracellular Ca(2+)
concentrations that are lower than those required for other
synaptotagmins. The two C2 domains bind independently to planar
membranes, without interdomain cooperativity. Moreover, SYT7 C2
domains insert more deeply into membranes compared to other
synaptotagmins. {ECO:0000250|UniProtKB:O43581}.
-!- PTM: Palmitoylated at its vesicular N-terminus; palmitoylation is
required for localization to lysosome and phagocytosis in
macrophages. {ECO:0000269|PubMed:21041449}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Mice were born at the
expected Mendelian ratio and do not show gross abnormalities
and/or obvious neurological defects. Mice have a normal life span
and are fertile, although reproductive capacity is declining
faster with age (PubMed:12925704). Embryonic fibroblasts from Syt7
deficient mice are less susceptible to Trypanosoma cruzi invasion,
and display impaired lysosomal exocytosis and resealing after
wounding (PubMed:12925704). Mutant mice display impaired insulin
secretion: they exhibit normal insulin sensitivity and normal
metabolic and Ca(2+) responses but impaired insulin release, due
to Ca(2+)-sensing defects (PubMed:18308938). Impaired glucagon
secretion (PubMed:19171650). Neurons show enhanced synaptic
depression: spontaneous synaptic vesicle release is unaffected,
while replenishment is impaired (PubMed:24569478). Abolished
synaptic facilitation at all synapses except for mossy fiber
synapses, where the remaining enhancement is consistent with use-
dependent spike broadening that occurs at this synapse
(PubMed:26738595). The loss of facilitation is not due to slowed
recovery from depression. The initial probability of release and
the presynaptic residual Ca(2+) signals are not affected
(PubMed:26738595). {ECO:0000269|PubMed:12925704,
ECO:0000269|PubMed:18308938, ECO:0000269|PubMed:19171650,
ECO:0000269|PubMed:24569478, ECO:0000269|PubMed:26738595}.
-!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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EMBL; AB026804; BAA85776.1; -; mRNA.
EMBL; AB075900; BAC44832.1; -; mRNA.
EMBL; AB075901; BAC44833.1; -; mRNA.
EMBL; AC124169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC105660; AAI05661.1; -; mRNA.
EMBL; BC139806; AAI39807.1; -; mRNA.
CCDS; CCDS29575.1; -. [Q9R0N7-1]
CCDS; CCDS29576.1; -. [Q9R0N7-3]
CCDS; CCDS50388.1; -. [Q9R0N7-4]
RefSeq; NP_061271.1; NM_018801.3. [Q9R0N7-1]
RefSeq; NP_775090.1; NM_173067.3. [Q9R0N7-3]
RefSeq; NP_775091.2; NM_173068.2. [Q9R0N7-4]
UniGene; Mm.182654; -.
PDB; 3N5A; X-ray; 1.44 A; A=266-403.
PDBsum; 3N5A; -.
ProteinModelPortal; Q9R0N7; -.
SMR; Q9R0N7; -.
IntAct; Q9R0N7; 1.
STRING; 10090.ENSMUSP00000127973; -.
iPTMnet; Q9R0N7; -.
PhosphoSitePlus; Q9R0N7; -.
SwissPalm; Q9R0N7; -.
MaxQB; Q9R0N7; -.
PaxDb; Q9R0N7; -.
PRIDE; Q9R0N7; -.
Ensembl; ENSMUST00000073899; ENSMUSP00000073560; ENSMUSG00000024743. [Q9R0N7-1]
Ensembl; ENSMUST00000169121; ENSMUSP00000127973; ENSMUSG00000024743. [Q9R0N7-4]
Ensembl; ENSMUST00000223586; ENSMUSP00000153482; ENSMUSG00000024743. [Q9R0N7-3]
GeneID; 54525; -.
KEGG; mmu:54525; -.
UCSC; uc008gpp.2; mouse.
UCSC; uc008gpq.2; mouse. [Q9R0N7-1]
UCSC; uc012bin.1; mouse.
CTD; 9066; -.
MGI; MGI:1859545; Syt7.
eggNOG; ENOG410IT3N; Eukaryota.
eggNOG; ENOG410XS7N; LUCA.
GeneTree; ENSGT00760000118973; -.
HOGENOM; HOG000232126; -.
HOVERGEN; HBG005010; -.
InParanoid; Q9R0N7; -.
KO; K19907; -.
OMA; TGEPKCQ; -.
OrthoDB; EOG091G08NG; -.
PhylomeDB; Q9R0N7; -.
ChiTaRS; Syt7; mouse.
PRO; PR:Q9R0N7; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024743; -.
CleanEx; MM_SYT7; -.
Genevisible; Q9R0N7; MM.
GO; GO:0043679; C:axon terminus; IDA:ParkinsonsUK-UCL.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
GO; GO:0031045; C:dense core granule; IEA:Ensembl.
GO; GO:0032009; C:early phagosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:ParkinsonsUK-UCL.
GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0008021; C:synaptic vesicle; IMP:UniProtKB.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; IDA:ParkinsonsUK-UCL.
GO; GO:0000149; F:SNARE binding; IDA:ParkinsonsUK-UCL.
GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
GO; GO:1990927; P:calcium ion regulated lysosome exocytosis; IMP:UniProtKB.
GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IMP:UniProtKB.
GO; GO:0006909; P:phagocytosis; IMP:UniProtKB.
GO; GO:0090385; P:phagosome-lysosome fusion; IMP:UniProtKB.
GO; GO:0001778; P:plasma membrane repair; IDA:MGI.
GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
GO; GO:0046850; P:regulation of bone remodeling; IMP:UniProtKB.
GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IMP:ParkinsonsUK-UCL.
GO; GO:0014059; P:regulation of dopamine secretion; IMP:ParkinsonsUK-UCL.
GO; GO:0070092; P:regulation of glucagon secretion; IMP:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; IMP:UniProtKB.
GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
GO; GO:1990926; P:short-term synaptic potentiation; IDA:UniProtKB.
GO; GO:0036465; P:synaptic vesicle recycling; IMP:UniProtKB.
GO; GO:0090119; P:vesicle-mediated cholesterol transport; IDA:UniProtKB.
CDD; cd08386; C2A_Synaptotagmin-7; 1.
CDD; cd08405; C2B_Synaptotagmin-7; 1.
Gene3D; 2.60.40.150; -; 2.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR037732; C2A_Synaptotagmin-7.
InterPro; IPR037741; C2B_Synaptotagmin-7.
InterPro; IPR001565; Synaptotagmin.
InterPro; IPR015427; Synaptotagmin7.
PANTHER; PTHR10024:SF206; PTHR10024:SF206; 1.
Pfam; PF00168; C2; 2.
PRINTS; PR00360; C2DOMAIN.
PRINTS; PR00399; SYNAPTOTAGMN.
SMART; SM00239; C2; 2.
PROSITE; PS50004; C2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Calmodulin-binding;
Cell junction; Cell membrane; Complete proteome; Cytoplasmic vesicle;
Exocytosis; Lipoprotein; Lysosome; Membrane; Metal-binding;
Methylation; Palmitate; Peroxisome; Phosphoprotein;
Reference proteome; Repeat; Synapse; Transmembrane;
Transmembrane helix.
CHAIN 1 403 Synaptotagmin-7.
/FTId=PRO_0000183958.
TOPO_DOM 1 16 Vesicular. {ECO:0000255}.
TRANSMEM 17 37 Helical. {ECO:0000255}.
TOPO_DOM 38 403 Cytoplasmic. {ECO:0000255}.
DOMAIN 137 239 C2 1. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 268 371 C2 2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
METAL 166 166 Calcium 1.
{ECO:0000250|UniProtKB:P40748}.
METAL 166 166 Calcium 2.
{ECO:0000250|UniProtKB:P40748}.
METAL 172 172 Calcium 1.
{ECO:0000250|UniProtKB:P40748}.
METAL 225 225 Calcium 1. {ECO:0000305|PubMed:26738595}.
METAL 225 225 Calcium 2. {ECO:0000305|PubMed:26738595}.
METAL 227 227 Calcium 1. {ECO:0000305|PubMed:26738595}.
METAL 227 227 Calcium 2. {ECO:0000305|PubMed:26738595}.
METAL 227 227 Calcium 3. {ECO:0000305|PubMed:26738595}.
METAL 230 230 Calcium 3.
{ECO:0000250|UniProtKB:P40748}.
METAL 233 233 Calcium 2. {ECO:0000305|PubMed:26738595}.
METAL 233 233 Calcium 3. {ECO:0000305|PubMed:26738595}.
METAL 297 297 Calcium 4. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 297 297 Calcium 5. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 303 303 Calcium 5. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 357 357 Calcium 4. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 357 357 Calcium 5. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 359 359 Calcium 4. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 359 359 Calcium 5. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 359 359 Calcium 6. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 362 362 Calcium 6. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 365 365 Calcium 4. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
METAL 365 365 Calcium 6. {ECO:0000244|PDB:3N5A,
ECO:0000269|PubMed:20824061}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 58 58 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000250|UniProtKB:Q62747}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 71 71 I -> INDLDRDFWNNNESTVQQKWSSYPPKEFILNISPYA
PYGDPRLSL (in isoform 3).
/FTId=VSP_058235.
VAR_SEQ 72 72 K -> NFEDSTLSTATTLESIPSSAGEPKCQRPRTLMRQQS
LQQPLSQNQRGRQPSQPTTSWDHVVGQIRNRGLDMKSFLEG
RMVVLSLVLGLSEQDDFANIPDLQNPGTQQNQNAQGDKR
(in isoform 2).
/FTId=VSP_058236.
VAR_SEQ 72 72 K -> NFEDSTLSTATTLESIPSSAGEPKCQRPRTLMRQQS
LQQPLSQNQQGRQPSQPTTSQSLGQLQAHAASAPGSNPRAY
GRGQARQGTSAGSKYRAAGGRSRSNPGSWDHVVGQIRNRGL
DMKSFLEGRMVVLSLVLGLSEQDDFANIPDLQNPGTQQNQN
AQGDKR (in isoform 4).
/FTId=VSP_058237.
MUTAGEN 35 41 CGLCHWC->SGLSHWS: Abolishes
palmitoylation. Impaired phagocytosis and
localization to lysosomes.
{ECO:0000269|PubMed:21041449}.
MUTAGEN 225 233 DYDRFSRND->AYARFSRNA: In C2A*; loss of
function due to abolished Ca(2+)-binding
to the first C2 domain. Impaired ability
to mediate synaptic facilitation.
{ECO:0000269|PubMed:26738595}.
MUTAGEN 225 227 DYD->NYN: Loss of Ca(2+)-binding in the
first C2 domain. Impaired delivery of
lysosomal membrane to nascent phagosomes;
when associated with 357-N--N-359.
Impaired synaptic vesicle replenishment;
when associated with 357-N--N-359.
{ECO:0000269|PubMed:16982801,
ECO:0000269|PubMed:24569478}.
MUTAGEN 357 359 DKD->NKN: Loss of Ca(2+)-binding in the
second C2 domain. Impaired delivery of
lysosomal membrane to nascent phagosomes;
when associated with 225-N--N-227.
Impaired synaptic vesicle replenishment;
when associated with 225-N--N-227.
{ECO:0000269|PubMed:16982801,
ECO:0000269|PubMed:24569478}.
STRAND 269 277 {ECO:0000244|PDB:3N5A}.
TURN 278 281 {ECO:0000244|PDB:3N5A}.
STRAND 282 292 {ECO:0000244|PDB:3N5A}.
TURN 298 300 {ECO:0000244|PDB:3N5A}.
STRAND 304 312 {ECO:0000244|PDB:3N5A}.
STRAND 315 321 {ECO:0000244|PDB:3N5A}.
STRAND 332 340 {ECO:0000244|PDB:3N5A}.
HELIX 343 348 {ECO:0000244|PDB:3N5A}.
STRAND 349 357 {ECO:0000244|PDB:3N5A}.
STRAND 360 362 {ECO:0000244|PDB:3N5A}.
STRAND 365 376 {ECO:0000244|PDB:3N5A}.
HELIX 378 389 {ECO:0000244|PDB:3N5A}.
STRAND 395 400 {ECO:0000244|PDB:3N5A}.
SEQUENCE 403 AA; 45472 MW; 4E63C5779C2ED43E CRC64;
MYRDPEAASP GAPTRDVLLV SAIITVSLSV TIVLCGLCHW CQRKLGKRYK NSLETVGTPD
SGRGRGEKKA IKLPAGGKAV NTAPVPGQTP HDESDRRTET RSSVSDLVNS LTSEMLMLSP
GSEEDEAHEG CSRENLGRIQ FSVGYNFQES TLTVKVMKAQ ELPAKDFSGT SDPFVKIYLL
PDKKHKLETK VKRKNLNPHW NETFLFEGFP YEKVVQRVLY LQVLDYDRFS RNDPIGEVSI
PLNKVDLTQM QTFWKDLKPC SDGSGSRGEL LLSLCYNPSA NSIIVNIIKA RNLKAMDIGG
TSDPYVKVWL MYKDKRVEKK KTVTKKRNLN PIFNESFAFD IPTEKLRETT IIITVMDKDK
LSRNDVIGKI YLSWKSGPGE VKHWKDMIAR PRQPVAQWHQ LKA


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