SYT11_MOUSE
ID SYT11_MOUSE Reviewed; 430 AA.
AC Q9R0N3; Q7TQG8;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Synaptotagmin-11 {ECO:0000305};
DE AltName: Full=Synaptotagmin XI {ECO:0000303|PubMed:23303671};
DE Short=SytXI;
GN Name=Syt11 {ECO:0000312|MGI:MGI:1859547};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Cerebellum;
RX PubMed=10531343; DOI=10.1074/jbc.274.44.31421;
RA Fukuda M., Kanno E., Mikoshiba K.;
RT "Conserved N-terminal cysteine motif is essential for homo- and heterodimer
RT formation of synaptotagmins III, V, VI, and X.";
RL J. Biol. Chem. 274:31421-31427(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23303671; DOI=10.4049/jimmunol.1202500;
RA Arango Duque G., Fukuda M., Descoteaux A.;
RT "Synaptotagmin XI regulates phagocytosis and cytokine secretion in
RT macrophages.";
RL J. Immunol. 190:1737-1745(2013).
RN [6]
RP INTERACTION WITH AGO2 AND SND1.
RX PubMed=24882364; DOI=10.1016/j.febslet.2014.05.031;
RA Milochau A., Lagree V., Benassy M.N., Chaignepain S., Papin J.,
RA Garcia-Arcos I., Lajoix A., Monterrat C., Coudert L., Schmitter J.M.,
RA Ochoa B., Lang J.;
RT "Synaptotagmin 11 interacts with components of the RNA-induced silencing
RT complex RISC in clonal pancreatic beta-cells.";
RL FEBS Lett. 588:2217-2222(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26450452; DOI=10.1038/cdd.2015.124;
RA Sreetama S.C., Takano T., Nedergaard M., Simon S.M., Jaiswal J.K.;
RT "Injured astrocytes are repaired by Synaptotagmin XI-regulated lysosome
RT exocytosis.";
RL Cell Death Differ. 23:596-607(2016).
RN [8]
RP FUNCTION.
RX PubMed=27278822; DOI=10.1038/ncomms11803;
RA Bento C.F., Ashkenazi A., Jimenez-Sanchez M., Rubinsztein D.C.;
RT "The Parkinson's disease-associated genes ATP13A2 and SYT11 regulate
RT autophagy via a common pathway.";
RL Nat. Commun. 7:11803-11803(2016).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28686317; DOI=10.1002/glia.23186;
RA Du C., Wang Y., Zhang F., Yan S., Guan Y., Gong X., Zhang T., Cui X.,
RA Wang X., Zhang C.X.;
RT "Synaptotagmin-11 inhibits cytokine secretion and phagocytosis in
RT microglia.";
RL Glia 65:1656-1667(2017).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29311685; DOI=10.1038/s41467-017-02593-y;
RA Wang C., Kang X., Zhou L., Chai Z., Wu Q., Huang R., Xu H., Hu M., Sun X.,
RA Sun S., Li J., Jiao R., Zuo P., Zheng L., Yue Z., Zhou Z.;
RT "Synaptotagmin-11 is a critical mediator of parkin-linked neurotoxicity and
RT Parkinson's disease-like pathology.";
RL Nat. Commun. 9:81-81(2018).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INTERACTION WITH KIF1A.
RX PubMed=30808661; DOI=10.1101/gad.320077.118;
RA Shimojo M., Madara J., Pankow S., Liu X., Yates J. III, Suedhof T.C.,
RA Maximov A.;
RT "Synaptotagmin-11 mediates a vesicle trafficking pathway that is essential
RT for development and synaptic plasticity.";
RL Genes Dev. 33:365-376(2019).
CC -!- FUNCTION: Synaptotagmin family member involved in vesicular and
CC membrane trafficking which does not bind Ca(2+) (Probable). Inhibits
CC clathrin-mediated and bulk endocytosis, functions to ensure precision
CC in vesicle retrieval (PubMed:29311685). Plays an important role in
CC dopamine transmission by regulating endocytosis and the vesicle-
CC recycling process (PubMed:29311685). Essential component of a neuronal
CC vesicular trafficking pathway that differs from the synaptic vesicle
CC trafficking pathway but is crucial for development and synaptic
CC plasticity (PubMed:30808661). In macrophages and microglia, inhibits
CC the conventional cytokine secretion, of at least IL6 and TNF, and
CC phagocytosis (PubMed:28686317, PubMed:23303671). In astrocytes,
CC regulates lysosome exocytosis, mechanism required for the repair of
CC injured astrocyte cell membrane (PubMed:26450452). Required for the
CC ATP13A2-mediated regulation of the autophagy-lysosome pathway
CC (PubMed:27278822). {ECO:0000269|PubMed:23303671,
CC ECO:0000269|PubMed:26450452, ECO:0000269|PubMed:27278822,
CC ECO:0000269|PubMed:28686317, ECO:0000269|PubMed:29311685,
CC ECO:0000269|PubMed:30808661, ECO:0000305}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Homodimer. Can also form heterodimers. Interacts with PRKN (By
CC similarity). Interacts (via C2 2 domain) with AGO2 and SND1; the
CC interaction with SND1 is direct (PubMed:24882364). Interacts with
CC KIF1A; the interaction increases in presence of calcium
CC (PubMed:30808661). {ECO:0000250|UniProtKB:Q9BT88,
CC ECO:0000269|PubMed:24882364, ECO:0000269|PubMed:30808661}.
CC -!- INTERACTION:
CC Q9R0N3; Q9JI51: Vti1a; Xeno; NbExp=2; IntAct=EBI-647443, EBI-7573650;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:30808661}; Single-pass membrane protein
CC {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:30808661}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:28686317};
CC Single-pass membrane protein {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000269|PubMed:23303671, ECO:0000269|PubMed:28686317}; Single-pass
CC membrane protein {ECO:0000305}. Lysosome membrane
CC {ECO:0000269|PubMed:23303671, ECO:0000269|PubMed:26450452,
CC ECO:0000269|PubMed:28686317}; Single-pass membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:23303671, ECO:0000269|PubMed:28686317}. Cell
CC projection, axon {ECO:0000269|PubMed:30808661}. Cell projection,
CC dendrite {ECO:0000269|PubMed:30808661}. Postsynaptic density
CC {ECO:0000269|PubMed:30808661}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:O08835}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O08835}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000250|UniProtKB:O08835}; Single-pass membrane
CC protein {ECO:0000250|UniProtKB:O08835}. Perikaryon
CC {ECO:0000250|UniProtKB:O08835}. Note=Localized in vesicles that travels
CC in axonal and dendritic shafts in both anterograde and retrograde
CC directions (PubMed:30808661). In macrophages and microglia, recruited
CC in phagosomes at early stages of phagocytosis (PubMed:28686317,
CC PubMed:23303671). {ECO:0000269|PubMed:23303671,
CC ECO:0000269|PubMed:28686317, ECO:0000269|PubMed:30808661}.
CC -!- TISSUE SPECIFICITY: Expressed in cerebellun, cerebellar cortex,
CC hippocampus, olfactory bulb and spinal cord (at protein level)
CC (PubMed:30808661). Expressed by neurons, astrocytes and microglia (at
CC protein level) (PubMed:28686317, PubMed:26450452). Expressed in
CC macrophages (at protein level) (PubMed:23303671).
CC {ECO:0000269|PubMed:23303671, ECO:0000269|PubMed:26450452,
CC ECO:0000269|PubMed:28686317, ECO:0000269|PubMed:30808661}.
CC -!- DEVELOPMENTAL STAGE: Abundant across the brain, expression increases
CC progressively over the first 2 weeks after birth.
CC {ECO:0000269|PubMed:30808661}.
CC -!- DOMAIN: The second C2 domain/C2B is required for the inhibitory role in
CC both clathrin-mediated and bulk endocytosis. The transmembrane domain
CC and the first C2 domain/C2A are critical for the inhibitory role in
CC clathrin-mediated endocytosis or bulk endocytosis, respectively.
CC {ECO:0000250|UniProtKB:O08835}.
CC -!- DOMAIN: Unlike in other synaptotagmin family members, the first C2
CC domain/C2A does not bind Ca(2+) neither mediates Ca(2+)-dependent
CC phospholipid binding. An aspartate-to-serine substitution in this
CC domain inactivates Ca(2+)/phospho-lipid binding.
CC {ECO:0000250|UniProtKB:O08835}.
CC -!- PTM: Ubiquitinated, at least by PRKN, and targeted to the proteasome
CC complex for degradation. Ubiquitination is inhibited by ATP13A2.
CC {ECO:0000250|UniProtKB:Q9BT88}.
CC -!- DISRUPTION PHENOTYPE: Knockout is lethal (PubMed:30808661). Conditional
CC knockout mice for dopaminergic neurons show increased dopamine release,
CC accelerated vesicle pools replenishment and enlarged releasable vesicle
CC pools in the striatum (PubMed:29311685). Forebrain-specific conditional
CC knockouts are viable, fertile and have normal life span. They show
CC impaired learning an memory (PubMed:30808661).
CC {ECO:0000269|PubMed:29311685, ECO:0000269|PubMed:30808661}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AB026808; BAA85780.1; -; mRNA.
DR EMBL; AK144169; BAE25745.1; -; mRNA.
DR EMBL; BC054526; AAH54526.1; -; mRNA.
DR CCDS; CCDS38484.1; -.
DR RefSeq; NP_061274.2; NM_018804.3.
DR RefSeq; XP_006501411.1; XM_006501348.1.
DR AlphaFoldDB; Q9R0N3; -.
DR SMR; Q9R0N3; -.
DR BioGRID; 230854; 4.
DR IntAct; Q9R0N3; 23.
DR MINT; Q9R0N3; -.
DR STRING; 10090.ENSMUSP00000103129; -.
DR iPTMnet; Q9R0N3; -.
DR PhosphoSitePlus; Q9R0N3; -.
DR SwissPalm; Q9R0N3; -.
DR MaxQB; Q9R0N3; -.
DR PaxDb; Q9R0N3; -.
DR PRIDE; Q9R0N3; -.
DR ProteomicsDB; 263193; -.
DR Antibodypedia; 34201; 213 antibodies from 29 providers.
DR DNASU; 229521; -.
DR Ensembl; ENSMUST00000090945; ENSMUSP00000088464; ENSMUSG00000068923.
DR Ensembl; ENSMUST00000107505; ENSMUSP00000103129; ENSMUSG00000068923.
DR GeneID; 229521; -.
DR KEGG; mmu:229521; -.
DR UCSC; uc008pwk.1; mouse.
DR CTD; 23208; -.
DR MGI; MGI:1859547; Syt11.
DR VEuPathDB; HostDB:ENSMUSG00000068923; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000159088; -.
DR InParanoid; Q9R0N3; -.
DR OMA; LQVINHD; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q9R0N3; -.
DR TreeFam; TF315600; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 229521; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Syt11; mouse.
DR PRO; PR:Q9R0N3; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9R0N3; protein.
DR Bgee; ENSMUSG00000068923; Expressed in motor neuron and 249 other tissues.
DR ExpressionAtlas; Q9R0N3; baseline and differential.
DR Genevisible; Q9R0N3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0032009; C:early phagosome; IDA:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0060077; C:inhibitory synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:1990927; P:calcium ion regulated lysosome exocytosis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0051650; P:establishment of vesicle localization; IMP:UniProtKB.
DR GO; GO:0007612; P:learning; IMP:UniProtKB.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:1905469; P:negative regulation of clathrin-coated pit assembly; ISO:MGI.
DR GO; GO:1900186; P:negative regulation of clathrin-dependent endocytosis; ISO:MGI.
DR GO; GO:0001818; P:negative regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; IDA:UniProtKB.
DR GO; GO:0045806; P:negative regulation of endocytosis; IDA:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:1905154; P:negative regulation of membrane invagination; ISO:MGI.
DR GO; GO:1903979; P:negative regulation of microglial cell activation; IDA:UniProtKB.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IDA:UniProtKB.
DR GO; GO:1900243; P:negative regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; IMP:ParkinsonsUK-UCL.
DR GO; GO:1905171; P:positive regulation of protein localization to phagocytic vesicle; IMP:ParkinsonsUK-UCL.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IMP:ParkinsonsUK-UCL.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:1905162; P:regulation of phagosome maturation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0009611; P:response to wounding; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR028699; SYT11.
DR PANTHER; PTHR10024:SF115; PTHR10024:SF115; 1.
DR Pfam; PF00168; C2; 2.
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 Calcium; Cell projection; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW Lysosome; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..430
FT /note="Synaptotagmin-11"
FT /id="PRO_0000183970"
FT TOPO_DOM 1..15
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 156..278
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 290..425
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 79..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 145
FT /note="A -> P (in Ref. 1; BAA85780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 48333 MW; 4E989259BE4FB423 CRC64;
MAEITNIRPS FDVSPVAAGL IGASVLVVCV SVTVFVWTCC HQQAEKKHKT PPYKFIHMLK
GISIYPETLS NKKKIIKVRR DKDGPRRESG RGNLLINAES GLLSHDKDPR GPSPASCMDQ
LPIKRDYGEE LRSPMTSLTP GESKATSPSS PEEDVMLGSL TFSVDYNFPK KALVVTIQEA
HGLPVMDDQT QGSDPYIKMT ILPDKRHRVK TRVLRKTLDP VFDETFTFYG IPYSQLQDLV
LHFLVLSFDR FSRDDVIGEV MVPLAGVDPS TGKVQLTRDI IKRNIQKCIS RGELQVSLSY
QPVAQRMTVV VLKARHLPKM DITGLSGNPY VKVNVYYGRK RIAKKKTHVK KCTLNPVFNE
SFIYDIPTDL LPDISIEFLV IDFDRTTKNE VVGRLILGAH SVTTSGAEHW REVCESPRKP
IAKWHSLSEY
