SYT11_HUMAN
ID SYT11_HUMAN Reviewed; 431 AA.
AC Q9BT88; Q14998; Q5W0D4; Q68CT5; Q8IXU3; Q96SU2;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Synaptotagmin-11 {ECO:0000305};
DE AltName: Full=Synaptotagmin XI;
DE Short=SytXI;
GN Name=SYT11 {ECO:0000312|HGNC:HGNC:19239}; Synonyms=KIAA0080;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-48.
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-48.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-48.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-48 AND VAL-231.
RC TISSUE=Brain, and Lymph;
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 [7]
RP INTERACTION WITH PRKN, UBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=12925569; DOI=10.1093/hmg/ddg269;
RA Huynh D.P., Scoles D.R., Nguyen D., Pulst S.M.;
RT "The autosomal recessive juvenile Parkinson disease gene product, parkin,
RT interacts with and ubiquitinates synaptotagmin XI.";
RL Hum. Mol. Genet. 12:2587-2597(2003).
RN [8]
RP FUNCTION, AND UBIQUITINATION.
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).
CC -!- FUNCTION: Synaptotagmin family member involved in vesicular and
CC membrane trafficking which does not bind Ca(2+). Inhibits clathrin-
CC mediated and bulk endocytosis, functions to ensure precision in vesicle
CC retrieval. Plays an important role in dopamine transmission by
CC regulating endocytosis and the vesicle-recycling process. Essential
CC component of a neuronal vesicular trafficking pathway that differs from
CC the synaptic vesicle trafficking pathway but is crucial for development
CC and synaptic plasticity. In macrophages and microglia, inhibits the
CC conventional cytokine secretion, of at least IL6 and TNF, and
CC phagocytosis. In astrocytes, regulates lysosome exocytosis, mechanism
CC required for the repair of injured astrocyte cell membrane (By
CC similarity). Required for the ATP13A2-mediated regulation of the
CC autophagy-lysosome pathway (PubMed:27278822).
CC {ECO:0000250|UniProtKB:Q9R0N3, ECO:0000269|PubMed:27278822}.
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
CC (PubMed:12925569). Interacts (via C2 2 domain) with AGO2 and SND1; the
CC interaction with SND1 is direct. Interacts with KIF1A; the interaction
CC increases in presence of calcium (By similarity).
CC {ECO:0000250|UniProtKB:O08835, ECO:0000250|UniProtKB:Q9R0N3,
CC ECO:0000269|PubMed:12925569}.
CC -!- INTERACTION:
CC Q9BT88; Q92624: APPBP2; NbExp=3; IntAct=EBI-751770, EBI-743771;
CC Q9BT88; Q9NQ11: ATP13A2; NbExp=2; IntAct=EBI-751770, EBI-6308763;
CC Q9BT88; O60260-5: PRKN; NbExp=6; IntAct=EBI-751770, EBI-21251460;
CC Q9BT88; O43765: SGTA; NbExp=7; IntAct=EBI-751770, EBI-347996;
CC Q9BT88; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-751770, EBI-744081;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000305|PubMed:12925569}; Single-pass membrane protein
CC {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q9R0N3}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9R0N3};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R0N3}. Recycling
CC endosome membrane {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane
CC protein {ECO:0000250|UniProtKB:Q9R0N3}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9R0N3}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:Q9R0N3}. Cell projection, axon
CC {ECO:0000269|PubMed:12925569}. Cell projection, dendrite
CC {ECO:0000269|PubMed:12925569}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9R0N3}. 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:0000269|PubMed:12925569}. Note=Localized in vesicles that travels
CC in axonal and dendritic shafts in both anterograde and retrograde
CC directions. In macrophages and microglia, recruited in phagosomes at
CC early stages of phagocytosis (By similarity). Found in the core of the
CC Lewy bodies in the brain of sporadic Parkinson disease patients
CC (PubMed:12925569). {ECO:0000250|UniProtKB:Q9R0N3,
CC ECO:0000269|PubMed:12925569}.
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 (PubMed:12925569, PubMed:27278822).
CC Ubiquitination is inhibited by ATP13A2 (PubMed:27278822).
CC {ECO:0000269|PubMed:12925569, ECO:0000269|PubMed:27278822}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07527.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D38522; BAA07527.2; ALT_INIT; mRNA.
DR EMBL; AK027540; BAB55186.1; -; mRNA.
DR EMBL; AK074931; BAC11300.1; -; mRNA.
DR EMBL; CR749792; CAH18653.1; -; mRNA.
DR EMBL; AL139128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004291; AAH04291.1; -; mRNA.
DR EMBL; BC013690; AAH13690.1; -; mRNA.
DR EMBL; BC039205; AAH39205.1; -; mRNA.
DR CCDS; CCDS1122.1; -.
DR RefSeq; NP_689493.3; NM_152280.4.
DR AlphaFoldDB; Q9BT88; -.
DR SMR; Q9BT88; -.
DR BioGRID; 116815; 27.
DR ELM; Q9BT88; -.
DR IntAct; Q9BT88; 10.
DR MINT; Q9BT88; -.
DR STRING; 9606.ENSP00000357307; -.
DR iPTMnet; Q9BT88; -.
DR PhosphoSitePlus; Q9BT88; -.
DR BioMuta; SYT11; -.
DR DMDM; 215273917; -.
DR jPOST; Q9BT88; -.
DR MassIVE; Q9BT88; -.
DR MaxQB; Q9BT88; -.
DR PaxDb; Q9BT88; -.
DR PeptideAtlas; Q9BT88; -.
DR PRIDE; Q9BT88; -.
DR ProteomicsDB; 78960; -.
DR Antibodypedia; 34201; 213 antibodies from 29 providers.
DR DNASU; 23208; -.
DR Ensembl; ENST00000368324.5; ENSP00000357307.4; ENSG00000132718.9.
DR GeneID; 23208; -.
DR KEGG; hsa:23208; -.
DR MANE-Select; ENST00000368324.5; ENSP00000357307.4; NM_152280.5; NP_689493.3.
DR UCSC; uc001fmg.4; human.
DR CTD; 23208; -.
DR DisGeNET; 23208; -.
DR GeneCards; SYT11; -.
DR HGNC; HGNC:19239; SYT11.
DR HPA; ENSG00000132718; Tissue enhanced (brain, retina).
DR MIM; 608741; gene.
DR neXtProt; NX_Q9BT88; -.
DR OpenTargets; ENSG00000132718; -.
DR PharmGKB; PA134898675; -.
DR VEuPathDB; HostDB:ENSG00000132718; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000159088; -.
DR HOGENOM; CLU_023008_7_3_1; -.
DR InParanoid; Q9BT88; -.
DR OMA; LQVINHD; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q9BT88; -.
DR TreeFam; TF315600; -.
DR PathwayCommons; Q9BT88; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q9BT88; -.
DR BioGRID-ORCS; 23208; 12 hits in 1063 CRISPR screens.
DR ChiTaRS; SYT11; human.
DR GeneWiki; SYT11; -.
DR GenomeRNAi; 23208; -.
DR Pharos; Q9BT88; Tbio.
DR PRO; PR:Q9BT88; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BT88; protein.
DR Bgee; ENSG00000132718; Expressed in ventricular zone and 163 other tissues.
DR Genevisible; Q9BT88; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:ParkinsonsUK-UCL.
DR GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0060077; C:inhibitory synapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0001891; C:phagocytic cup; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
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; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:1990927; P:calcium ion regulated lysosome exocytosis; ISS: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; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; ISS:UniProtKB.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISS:UniProtKB.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:1903979; P:negative regulation of microglial cell activation; ISS:UniProtKB.
DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; TAS:ParkinsonsUK-UCL.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; ISS:ParkinsonsUK-UCL.
DR GO; GO:1905171; P:positive regulation of protein localization to phagocytic vesicle; ISS: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; IEA:Ensembl.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:1905162; P:regulation of phagosome maturation; IC: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..431
FT /note="Synaptotagmin-11"
FT /id="PRO_0000183969"
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..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 157..279
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 291..426
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 134..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0N3"
FT VARIANT 48
FT /note="Q -> H (in dbSNP:rs822522)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:7584044"
FT /id="VAR_047656"
FT VARIANT 231
FT /note="G -> V (in dbSNP:rs17853892)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047657"
FT CONFLICT 50
FT /note="N -> S (in Ref. 3; BAB55186)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="V -> A (in Ref. 3; BAB55186)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="F -> L (in Ref. 4; CAH18653)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="D -> G (in Ref. 4; CAH18653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 48297 MW; 5C8667D2C23D758E CRC64;
MAEITNIRPS FDVSPVVAGL IGASVLVVCV SVTVFVWSCC HQQAEKKQKN PPYKFIHMLK
GISIYPETLS NKKKIIKVRR DKDGPGREGG RRNLLVDAAE AGLLSRDKDP RGPSSGSCID
QLPIKMDYGE ELRSPITSLT PGESKTTSPS SPEEDVMLGS LTFSVDYNFP KKALVVTIQE
AHGLPVMDDQ TQGSDPYIKM TILPDKRHRV KTRVLRKTLD PVFDETFTFY GIPYSQLQDL
VLHFLVLSFD RFSRDDVIGE VMVPLAGVDP STGKVQLTRD IIKRNIQKCI SRGELQVSLS
YQPVAQRMTV VVLKARHLPK MDITGLSGNP YVKVNVYYGR KRIAKKKTHV KKCTLNPIFN
ESFIYDIPTD LLPDISIEFL VIDFDRTTKN EVVGRLILGA HSVTASGAEH WREVCESPRK
PVAKWHSLSE Y
