SYT7_RAT
ID SYT7_RAT Reviewed; 403 AA.
AC Q62747; F1M262; Q99J98; Q99P33; Q99P34; Q99P35; Q99P36; Q99P37; Q99P38;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Synaptotagmin-7 {ECO:0000305};
DE AltName: Full=Protein Syt7 {ECO:0000312|Ensembl:ENSRNOP00000040667};
DE AltName: Full=Synaptotagmin VII {ECO:0000303|PubMed:11395007};
DE Short=SytVII {ECO:0000303|PubMed:11395007};
GN Name=Syt7 {ECO:0000312|RGD:62013};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Intestine;
RX PubMed=7791877; DOI=10.1038/375594a0;
RA Li C., Ullrich B., Zhang J.Z., Anderson R.G.W., Brose N., Suedhof T.C.;
RT "Ca(2+)-dependent and -independent activities of neural and non-neural
RT synaptotagmins.";
RL Nature 375:594-599(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION,
RP COFACTOR, AND MUTAGENESIS OF ASP-172 AND ASP-225.
RX PubMed=11395007; DOI=10.1016/s0896-6273(01)00290-2;
RA Sugita S., Han W., Butz S., Liu X., Fernandez-Chacon R., Lao Y.,
RA Sudhof T.C.;
RT "Synaptotagmin VII as a plasma membrane Ca(2+) sensor in exocytosis.";
RL Neuron 30:459-473(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10725327; DOI=10.1083/jcb.148.6.1141;
RA Martinez I., Chakrabarti S., Hellevik T., Morehead J., Fowler K.,
RA Andrews N.W.;
RT "Synaptotagmin VII regulates Ca(2+)-dependent exocytosis of lysosomes in
RT fibroblasts.";
RL J. Cell Biol. 148:1141-1149(2000).
RN [6]
RP FUNCTION.
RX PubMed=11511344; DOI=10.1016/s0092-8674(01)00421-4;
RA Reddy A., Caler E.V., Andrews N.W.;
RT "Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of
RT lysosomes.";
RL Cell 106:157-169(2001).
RN [7]
RP ALTERNATIVE SPLICING.
RX PubMed=12071850; DOI=10.1042/bj20011877;
RA Fukuda M., Ogata Y., Saegusa C., Kanno E., Mikoshiba K.;
RT "Alternative splicing isoforms of synaptotagmin VII in the mouse, rat and
RT human.";
RL Biochem. J. 365:173-180(2002).
RN [8]
RP COFACTOR, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=11823420; DOI=10.1093/emboj/21.3.270;
RA Sugita S., Shin O.H., Han W., Lao Y., Suedhof T.C.;
RT "Synaptotagmins form a hierarchy of exocytotic Ca(2+) sensors with distinct
RT Ca(2+) affinities.";
RL EMBO J. 21:270-280(2002).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15456748; DOI=10.1074/jbc.m409241200;
RA Fukuda M., Kanno E., Satoh M., Saegusa C., Yamamoto A.;
RT "Synaptotagmin VII is targeted to dense-core vesicles and regulates their
RT Ca2+ -dependent exocytosis in PC12 cells.";
RL J. Biol. Chem. 279:52677-52684(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17190793; DOI=10.1083/jcb.200607021;
RA Maximov A., Shin O.H., Liu X., Suedhof T.C.;
RT "Synaptotagmin-12, a synaptic vesicle phosphoprotein that modulates
RT spontaneous neurotransmitter release.";
RL J. Cell Biol. 176:113-124(2007).
RN [11]
RP FUNCTION.
RX PubMed=18508778; DOI=10.1074/jbc.m709628200;
RA Bhalla A., Chicka M.C., Chapman E.R.;
RT "Analysis of the synaptotagmin family during reconstituted membrane fusion.
RT Uncovering a class of inhibitory isoforms.";
RL J. Biol. Chem. 283:21799-21807(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; THR-58; SER-61; SER-119
RP AND SER-122, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of
CC secretory and synaptic vesicles through Ca(2+) and phospholipid binding
CC to the C2 domain (PubMed:11395007, PubMed:10725327, PubMed:11511344).
CC Ca(2+) induces binding of the C2-domains to phospholipid membranes and
CC to assembled SNARE-complexes; both actions contribute to triggering
CC exocytosis (PubMed:11395007). SYT7 binds Ca(2+) with high affinity and
CC slow kinetics compared to other synaptotagmins (By similarity).
CC Involved in Ca(2+)-triggered lysosomal exocytosis, a major component of
CC the plasma membrane repair (PubMed:10725327, PubMed:11511344). Ca(2+)-
CC regulated delivery of lysosomal membranes to the cell surface is also
CC involved in the phagocytic uptake of particles by macrophages. Ca(2+)-
CC triggered lysosomal exocytosis also plays a role in bone remodeling by
CC regulating secretory pathways in osteoclasts and osteoblasts. Involved
CC in cholesterol transport from lysosome to peroxisome by promoting
CC membrane contacts between lysosomes and peroxisomes: probably acts by
CC promoting vesicle fusion by binding phosphatidylinositol-4,5-
CC bisphosphate on peroxisomal membranes. Acts as a key mediator of
CC synaptic facilitation, a process also named short-term synaptic
CC potentiation: synaptic facilitation takes place at synapses with a low
CC initial release probability and is caused by influx of Ca(2+) into the
CC axon terminal after spike generation, increasing the release
CC probability of neurotransmitters. Probably mediates synaptic
CC facilitation by directly increasing the probability of release. May
CC also contribute to synaptic facilitation by regulating synaptic vesicle
CC replenishment, a process required to ensure that synaptic vesicles are
CC ready for the arrival of the next action potential: SYT7 is required
CC for synaptic vesicle replenishment by acting as a sensor for Ca(2+) and
CC by forming a complex with calmodulin. Also acts as a regulator of
CC Ca(2+)-dependent insulin and glucagon secretion in beta-cells. Triggers
CC exocytosis by promoting fusion pore opening and fusion pore expansion
CC in chromaffin cells (By similarity). Also regulates the secretion of
CC some non-synaptic secretory granules of specialized cells
CC (PubMed:15456748). {ECO:0000250|UniProtKB:Q9R0N7,
CC ECO:0000269|PubMed:10725327, ECO:0000269|PubMed:11395007,
CC ECO:0000269|PubMed:11511344, ECO:0000269|PubMed:15456748}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:11823420, ECO:0000305|PubMed:11395007};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBUNIT: Homodimer. Can also form heterodimers with SYT6, SYT9 and
CC SYT10. Interacts with calmodulin (CALM1, CALM2 or CALM3). Interacts
CC with CD63; required for localization to lysosomes. Interacts with APP
CC (By similarity). {ECO:0000250|UniProtKB:Q9R0N7}.
CC -!- INTERACTION:
CC Q62747; O35526: Stx1a; Xeno; NbExp=2; IntAct=EBI-16179541, EBI-400878;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11823420};
CC Single-pass membrane protein {ECO:0000255}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000269|PubMed:17190793}; Single-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:10725327}; Single-
CC pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein
CC {ECO:0000255}. Peroxisome membrane {ECO:0000250|UniProtKB:Q9R0N7};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle,
CC secretory vesicle membrane {ECO:0000269|PubMed:15456748}; Single-pass
CC membrane protein {ECO:0000255}. Note=Localization to lysosomes is
CC dependent on N-terminal palmitoylation and interaction with CD63.
CC {ECO:0000250|UniProtKB:Q9R0N7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=Synaptotagmin VIIs {ECO:0000303|PubMed:11395007};
CC IsoId=Q62747-1; Sequence=Displayed;
CC Name=2; Synonyms=Synaptotagmin VIIL {ECO:0000303|PubMed:11395007};
CC IsoId=Q62747-2; Sequence=VSP_058239;
CC Name=3; Synonyms=Synaptotagmin VIId {ECO:0000303|PubMed:11395007};
CC IsoId=Q62747-3; Sequence=VSP_058240;
CC Name=4; Synonyms=Synaptotagmin VIIe {ECO:0000303|PubMed:11395007};
CC IsoId=Q62747-4; Sequence=VSP_058241;
CC Name=5; Synonyms=Synaptotagmin VIIb {ECO:0000303|PubMed:11395007};
CC IsoId=Q62747-5; Sequence=VSP_058242;
CC Name=6; Synonyms=Synaptotagmin VIIc {ECO:0000303|PubMed:11395007};
CC IsoId=Q62747-6; Sequence=VSP_058243;
CC Name=7; Synonyms=Synaptotagmin VIIa {ECO:0000303|PubMed:11395007};
CC IsoId=Q62747-7; Sequence=VSP_058244;
CC Name=8; Synonyms=Synaptotagmin VIIT1 {ECO:0000303|PubMed:11395007},
CC Synaptotagmin VIIT2 {ECO:0000303|PubMed:11395007};
CC IsoId=Q62747-8; Sequence=VSP_058238, VSP_058245;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC {ECO:0000269|PubMed:17190793}.
CC -!- DOMAIN: The C2 domains bind Ca(2+) and membranes (PubMed:11823420).
CC Binding to membranes involves Ca(2+)-dependent phospholipid binding
CC (PubMed:11823420). Compared to other members of the family, the C2
CC domains of SYT7 dock and insert into cellular membranes in response to
CC intracellular Ca(2+) concentrations that are lower than those required
CC for other synaptotagmins. The two C2 domains bind independently to
CC planar membranes, without interdomain cooperativity. Moreover, SYT7 C2
CC domains insert more deeply into membranes compared to other
CC synaptotagmins (By similarity). {ECO:0000250|UniProtKB:O43581,
CC ECO:0000269|PubMed:11823420}.
CC -!- PTM: Palmitoylated at its vesicular N-terminus; palmitoylation is
CC required for localization to lysosome and phagocytosis in macrophages.
CC {ECO:0000250|UniProtKB:Q9R0N7}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC {ECO:0000269|PubMed:12071850}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; U20106; AAA87725.1; -; mRNA.
DR EMBL; AF336852; AAK01447.1; -; mRNA.
DR EMBL; AF336853; AAK01448.1; -; mRNA.
DR EMBL; AF336854; AAK01449.1; -; mRNA.
DR EMBL; AF336855; AAK01450.1; -; mRNA.
DR EMBL; AF336856; AAK01451.1; -; mRNA.
DR EMBL; AF336857; AAK01452.1; -; mRNA.
DR EMBL; AF336858; AAK01453.1; -; mRNA.
DR EMBL; AF336859; AAK01454.1; -; mRNA.
DR EMBL; AF336860; AAK01455.1; -; mRNA.
DR EMBL; AC095662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473953; EDM12801.1; -; Genomic_DNA.
DR EMBL; CH473953; EDM12802.1; -; Genomic_DNA.
DR EMBL; CH473953; EDM12803.1; -; Genomic_DNA.
DR EMBL; CH473953; EDM12804.1; -; Genomic_DNA.
DR EMBL; CH473953; EDM12805.1; -; Genomic_DNA.
DR EMBL; CH473953; EDM12806.1; -; Genomic_DNA.
DR EMBL; CH473953; EDM12807.1; -; Genomic_DNA.
DR PIR; S58400; S58400.
DR RefSeq; NP_067691.1; NM_021659.1. [Q62747-1]
DR RefSeq; XP_006231127.1; XM_006231065.3. [Q62747-2]
DR RefSeq; XP_006231129.1; XM_006231067.3. [Q62747-4]
DR RefSeq; XP_006231130.1; XM_006231068.3. [Q62747-3]
DR PDB; 6ANJ; X-ray; 1.70 A; A=134-262.
DR PDB; 6ANK; X-ray; 2.25 A; A/B=134-403.
DR PDBsum; 6ANJ; -.
DR PDBsum; 6ANK; -.
DR AlphaFoldDB; Q62747; -.
DR SMR; Q62747; -.
DR CORUM; Q62747; -.
DR DIP; DIP-61710N; -.
DR IntAct; Q62747; 2.
DR MINT; Q62747; -.
DR iPTMnet; Q62747; -.
DR PhosphoSitePlus; Q62747; -.
DR SwissPalm; Q62747; -.
DR PaxDb; Q62747; -.
DR PRIDE; Q62747; -.
DR ABCD; Q62747; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000007429; ENSRNOP00000007429; ENSRNOG00000026432. [Q62747-8]
DR Ensembl; ENSRNOT00000035576; ENSRNOP00000031890; ENSRNOG00000026432. [Q62747-4]
DR Ensembl; ENSRNOT00000036168; ENSRNOP00000031944; ENSRNOG00000026432. [Q62747-6]
DR Ensembl; ENSRNOT00000036232; ENSRNOP00000031195; ENSRNOG00000026432. [Q62747-2]
DR Ensembl; ENSRNOT00000036283; ENSRNOP00000031816; ENSRNOG00000026432. [Q62747-7]
DR Ensembl; ENSRNOT00000047964; ENSRNOP00000049360; ENSRNOG00000026432. [Q62747-5]
DR Ensembl; ENSRNOT00000048704; ENSRNOP00000040667; ENSRNOG00000026432. [Q62747-1]
DR GeneID; 59267; -.
DR KEGG; rno:59267; -.
DR UCSC; RGD:62013; rat.
DR CTD; 9066; -.
DR RGD; 62013; Syt7.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000157180; -.
DR HOGENOM; CLU_023008_11_3_1; -.
DR OMA; QNHEANS; -.
DR OrthoDB; 925064at2759; -.
DR TreeFam; TF315600; -.
DR PRO; PR:Q62747; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000026432; Expressed in frontal cortex and 17 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0031045; C:dense core granule; IDA:RGD.
DR GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; IMP:RGD.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0030276; F:clathrin binding; IDA:BHF-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; ISO:RGD.
DR GO; GO:0019905; F:syntaxin binding; IDA:BHF-UCL.
DR GO; GO:1990927; P:calcium ion regulated lysosome exocytosis; IDA:UniProtKB.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; ISS:UniProtKB.
DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; ISO:RGD.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0005513; P:detection of calcium ion; IC:RGD.
DR GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; IDA:UniProtKB.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IDA:RGD.
DR GO; GO:0046850; P:regulation of bone remodeling; ISS:UniProtKB.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IMP:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:RGD.
DR GO; GO:0070092; P:regulation of glucagon secretion; ISS:UniProtKB.
DR GO; GO:0050796; P:regulation of insulin secretion; IMP:RGD.
DR GO; GO:0050764; P:regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:1990926; P:short-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0036465; P:synaptic vesicle recycling; ISS:UniProtKB.
DR GO; GO:0090119; P:vesicle-mediated cholesterol transport; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd08386; C2A_Synaptotagmin-7; 1.
DR CDD; cd08405; C2B_Synaptotagmin-7; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037732; C2A_Synaptotagmin-7.
DR InterPro; IPR037741; C2B_Synaptotagmin-7.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR015427; Synaptotagmin7.
DR PANTHER; PTHR10024:SF358; PTHR10024:SF358; 2.
DR Pfam; PF00168; C2; 2.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calmodulin-binding;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Exocytosis;
KW Lipoprotein; Lysosome; Membrane; Metal-binding; Palmitate; Peroxisome;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..403
FT /note="Synaptotagmin-7"
FT /id="PRO_0000436055"
FT TOPO_DOM 1..16
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 135..255
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 266..399
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 75..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9R0N7"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 72..122
FT /note="KLPAGGKAVNTAPVPGQTPHDESDRRTEPRSSVSDLVNSLTSEMLMLSPGS
FT -> NDLDRDFWNNNESTVQQKWSSYPPKEFILNISPYAPYGDPRLSLNPLFLRR (in
FT isoform 8)"
FT /id="VSP_058238"
FT VAR_SEQ 72
FT /note="K -> NDLDRDFWNNNESTVQQKWSSYPPKEFILNISPYAPYGDPRLSLNGT
FT LLSGAKVATAAAGLAVEREGRLGEKPAPVPPPGEDALRSGGAAPSEPGSSGKAGRGRWR
FT MVQSHLAAGKLNLSNFEDSTLSTATTLESIPSSAGEPKCQRPRTLMRQQSLQQPLSQNQ
FT RGRQPSQPTTSQSLGQLQAHAASAPGSNPRAYGRGQARQGTSAGSKYRAAGGRSRSNPG
FT SWDHVVGQIRNRGLDMKSFLEGRMVVLSLVLGLSEQDDFANIPDLQNPGTQQNQNAQGD
FT KR (in isoform 2)"
FT /id="VSP_058239"
FT VAR_SEQ 72
FT /note="K -> NDLDRDFWNNNESTVQQKWSSYPPKEFILNISPYAPYGDPRLSLNFE
FT DSTLSTATTLESIPSSAGEPKCQRPRTLMRQQSLQQPLSQNQRGRQPSQPTTSQSLGQL
FT QAHAASAPGSNPRAYGRGQARQGTSAGSKYRAAGGRSRSNPGSWDHVVGQIRNRGLDMK
FT SFLEGRMVVLSLVLGLSEQDDFANIPDLQNPGTQQNQNAQGDKR (in isoform
FT 3)"
FT /id="VSP_058240"
FT VAR_SEQ 72
FT /note="K -> NGTLLSGAKVATAAAGLAVEREGRLGEKPAPVPPPGEDALRSGGAAP
FT SEPGSSGKAGRGRWRMVQSHLAAGKLNLSNFEDSTLSTATTLESIPSSAGEPKCQRPRT
FT LMRQQSLQQPLSQNQRGRQPSQPTTSQSLGQLQAHAASAPGSNPRAYGRGQARQGTSAG
FT SKYRAAGGRSRSNPGSWDHVVGQIRNRGLDMKSFLEGRMVVLSLVLGLSEQDDFANIPD
FT LQNPGTQQNQNAQGDKR (in isoform 4)"
FT /id="VSP_058241"
FT VAR_SEQ 72
FT /note="K -> NDLDRDFWNNNESTVQQKWSSYPPKEFILNISPYAPYGDPRLSLNGT
FT LLSGAKVATAAAGLAVEREGRLGEKPAPVPPPGEDALRSGGAAPSEPGSSGKAGRGRWR
FT MVQSHLAAGKLNLSK (in isoform 5)"
FT /id="VSP_058242"
FT VAR_SEQ 72
FT /note="K -> NFEDSTLSTATTLESIPSSAGEPKCQRPRTLMRQQSLQQPLSQNQRG
FT RQPSQPTTSQSLGQLQAHAASAPGSNPRAYGRGQARQGTSAGSKYRAAGGRSRSNPGSW
FT DHVVGQIRNRGLDMKSFLEGRMVVLSLVLGLSEQDDFANIPDLQNPGTQQNQNAQGDKR
FT (in isoform 6)"
FT /id="VSP_058243"
FT VAR_SEQ 72
FT /note="K -> NGTLLSGAKVATAAAGLAVEREGRLGEKPAPVPPPGEDALRSGGAAP
FT SEPGSSGKAGRGRWRMVQSHLAAGKLNLSKEGRMVVLSLVLGLSEQDDFANIPDLQNPG
FT TQQNQNAQGDKR (in isoform 7)"
FT /id="VSP_058244"
FT VAR_SEQ 123..403
FT /note="Missing (in isoform 8)"
FT /id="VSP_058245"
FT MUTAGEN 172
FT /note="D->N: Loss of Ca(2+)-binding in the first C2 domain;
FT when associated with N-225."
FT /evidence="ECO:0000269|PubMed:11395007"
FT MUTAGEN 225
FT /note="D->N: Loss of Ca(2+)-binding in the first C2 domain;
FT when associated with N-172."
FT /evidence="ECO:0000269|PubMed:11395007"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:6ANJ"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:6ANJ"
FT STRAND 151..161
FT /evidence="ECO:0007829|PDB:6ANJ"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:6ANJ"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:6ANK"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:6ANJ"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:6ANJ"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:6ANJ"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6ANJ"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:6ANJ"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:6ANJ"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:6ANJ"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:6ANK"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:6ANK"
FT STRAND 282..292
FT /evidence="ECO:0007829|PDB:6ANK"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:6ANK"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:6ANK"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:6ANK"
FT STRAND 332..340
FT /evidence="ECO:0007829|PDB:6ANK"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6ANK"
FT STRAND 349..357
FT /evidence="ECO:0007829|PDB:6ANK"
FT STRAND 365..376
FT /evidence="ECO:0007829|PDB:6ANK"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:6ANK"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:6ANK"
SQ SEQUENCE 403 AA; 45482 MW; 3153FD7FC1DEEEFB CRC64;
MYRDPEAASP GAPTRDVLLV SAIITVSLSV TIVLCGLCHW CQRKLGKRYK NSLETVGTPD
SGRGRGEKKA IKLPAGGKAV NTAPVPGQTP HDESDRRTEP RSSVSDLVNS LTSEMLMLSP
GSEEDEAHEG CSRENLGRIQ FSVGYNFQES TLTVKVMKAQ ELPAKDFSGT SDPFVKIYLL
PDKKHKLETK VKRKNLNPHW NETFLFEGFP YEKVVQRILY LQVLDYDRFS RNDPIGEVSI
PLNKVDLTQM QTFWKDLKPC SDGSGSRGEL LLSLCYNPSA NSIIVNIIKA RNLKAMDIGG
TSDPYVKVWL MYKDKRVEKK KTVTKKRNLN PIFNESFAFD IPTEKLRETT IIITVMDKDK
LSRNDVIGKI YLSWKSGPGE VKHWKDMIAR PRQPVAQWHQ LKA
