SYT1_MOUSE
ID SYT1_MOUSE Reviewed; 421 AA.
AC P46096;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Synaptotagmin-1;
DE AltName: Full=Synaptotagmin I;
DE Short=SytI;
DE AltName: Full=p65;
GN Name=Syt1;
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].
RX PubMed=7961887; DOI=10.1016/s0021-9258(19)62031-4;
RA Fukuda M., Aruga J., Niinobe M., Aimoto S., Mikoshiba K.;
RT "Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of
RT IP4BP/synaptotagmin II.";
RL J. Biol. Chem. 269:29206-29211(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 TISSUE=Eye;
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 PROTEIN SEQUENCE OF 183-189; 201-233; 245-260; 273-281; 289-297; 302-313;
RP 333-366 AND 376-388, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF ARG-233 AND LYS-236.
RX PubMed=11242035; DOI=10.1038/35065004;
RA Fernandez-Chacon R., Koenigstorfer A., Gerber S.H., Garcia J., Matos M.F.,
RA Stevens C.F., Brose N., Rizo J., Rosenmund C., Suedhof T.C.;
RT "Synaptotagmin I functions as a calcium regulator of release probability.";
RL Nature 410:41-49(2001).
RN [6]
RP INTERACTION WITH SV2B; SYNTAXIN-1 AND SNAP25.
RX PubMed=15466855; DOI=10.1074/jbc.m407502200;
RA Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.;
RT "SV2B regulates synaptotagmin 1 by direct interaction.";
RL J. Biol. Chem. 279:52124-52131(2004).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Liver;
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 [10]
RP FUNCTION.
RX PubMed=21496647; DOI=10.1016/j.cell.2011.03.034;
RA Cao P., Maximov A., Suedhof T.C.;
RT "Activity-dependent IGF-1 exocytosis is controlled by the Ca(2+)-sensor
RT synaptotagmin-10.";
RL Cell 145:300-311(2011).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=23345244; DOI=10.1523/jneurosci.4087-12.2013;
RA Cao P., Yang X., Suedhof T.C.;
RT "Complexin activates exocytosis of distinct secretory vesicles controlled
RT by different synaptotagmins.";
RL J. Neurosci. 33:1714-1727(2013).
RN [12]
RP INTERACTION WITH PRRT2.
RX PubMed=27052163; DOI=10.1016/j.celrep.2016.03.005;
RA Valente P., Castroflorio E., Rossi P., Fadda M., Sterlini B.,
RA Cervigni R.I., Prestigio C., Giovedi S., Onofri F., Mura E.,
RA Guarnieri F.C., Marte A., Orlando M., Zara F., Fassio A., Valtorta F.,
RA Baldelli P., Corradi A., Benfenati F.;
RT "PRRT2 Is a Key Component of the Ca(2+)-Dependent Neurotransmitter Release
RT Machinery.";
RL Cell Rep. 15:117-131(2016).
CC -!- FUNCTION: Calcium sensor that participates in triggering
CC neurotransmitter release at the synapse (PubMed:11242035). May have a
CC regulatory role in the membrane interactions during trafficking of
CC synaptic vesicles at the active zone of the synapse (PubMed:7961887).
CC It binds acidic phospholipids with a specificity that requires the
CC presence of both an acidic head group and a diacyl backbone. A Ca(2+)-
CC dependent interaction between synaptotagmin and putative receptors for
CC activated protein kinase C has also been reported. It can bind to at
CC least three additional proteins in a Ca(2+)-independent manner; these
CC are neurexins, syntaxin and AP2. Plays a role in dendrite formation by
CC melanocytes (By similarity). {ECO:0000250|UniProtKB:P21579,
CC ECO:0000269|PubMed:11242035, ECO:0000269|PubMed:7961887}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:11242035};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domains. {ECO:0000250|UniProtKB:P21707};
CC -!- SUBUNIT: Homotetramer (Probable). Interacts with SCAMP5 (By
CC similarity). Interacts with STON2 (By similarity). Forms a complex with
CC SV2B, syntaxin 1 and SNAP25 (PubMed:15466855). Interacts with SV2A,
CC SV2B and SV2C (By similarity). Interacts with RIMS1 (By similarity).
CC Interacts with PRRT2 (PubMed:27052163). Interacts with DNAJC5 in a
CC phosphorylation-dependent manner (By similarity). Interacts (via N-
CC terminus) with RAB3A (By similarity). Interacts with SYT12 (By
CC similarity). Interacts with calmodulin (By similarity).
CC {ECO:0000250|UniProtKB:P21579, ECO:0000250|UniProtKB:P21707,
CC ECO:0000250|UniProtKB:P48018, ECO:0000269|PubMed:15466855,
CC ECO:0000269|PubMed:27052163, ECO:0000305}.
CC -!- INTERACTION:
CC P46096; P49769: Psen1; NbExp=6; IntAct=EBI-445340, EBI-990067;
CC P46096; Q8TAC9: SCAMP5; Xeno; NbExp=2; IntAct=EBI-445340, EBI-2695784;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000269|PubMed:23345244}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, chromaffin
CC granule membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane
CC protein {ECO:0000250|UniProtKB:P21707}. Cytoplasm
CC {ECO:0000250|UniProtKB:P21707}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain and adrenal medulla (at
CC protein level). {ECO:0000269|PubMed:17190793}.
CC -!- DEVELOPMENTAL STAGE: Detected in the brain at 18 days post coitum (dpc)
CC (at protein level). Expression increases after birth, with expression
CC increasing till adulthood. {ECO:0000269|PubMed:17190793}.
CC -!- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid
CC binding. {ECO:0000250|UniProtKB:P21707}.
CC -!- DOMAIN: The second C2 domain mediates interaction with SV2A and
CC probably with STN2. {ECO:0000250|UniProtKB:P21707}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P21707}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; D37792; BAA07040.1; -; mRNA.
DR EMBL; AK078790; BAC37395.1; -; mRNA.
DR EMBL; BC042519; AAH42519.1; -; mRNA.
DR CCDS; CCDS24163.1; -.
DR RefSeq; NP_001239270.1; NM_001252341.1.
DR RefSeq; NP_001239271.1; NM_001252342.1.
DR RefSeq; NP_033332.1; NM_009306.3.
DR RefSeq; XP_006513509.1; XM_006513446.1.
DR RefSeq; XP_006513510.1; XM_006513447.1.
DR RefSeq; XP_006513511.1; XM_006513448.1.
DR RefSeq; XP_017169355.1; XM_017313866.1.
DR PDB; 5T0R; X-ray; 1.95 A; A=140-265.
DR PDB; 5T0S; X-ray; 1.42 A; A=271-421.
DR PDB; 5VFE; X-ray; 1.38 A; A/B=140-265.
DR PDB; 5VFF; X-ray; 1.41 A; A=271-421.
DR PDB; 5VFG; X-ray; 1.82 A; A=271-421.
DR PDBsum; 5T0R; -.
DR PDBsum; 5T0S; -.
DR PDBsum; 5VFE; -.
DR PDBsum; 5VFF; -.
DR PDBsum; 5VFG; -.
DR AlphaFoldDB; P46096; -.
DR SMR; P46096; -.
DR BioGRID; 203611; 22.
DR DIP; DIP-31322N; -.
DR IntAct; P46096; 20.
DR MINT; P46096; -.
DR STRING; 10090.ENSMUSP00000100912; -.
DR TCDB; 9.A.48.1.1; the unconventional protein secretion (ups) system.
DR GlyConnect; 2750; 6 N-Linked glycans (1 site).
DR GlyGen; P46096; 1 site, 6 N-linked glycans (1 site).
DR iPTMnet; P46096; -.
DR PhosphoSitePlus; P46096; -.
DR SwissPalm; P46096; -.
DR MaxQB; P46096; -.
DR PaxDb; P46096; -.
DR PRIDE; P46096; -.
DR ProteomicsDB; 253445; -.
DR Antibodypedia; 1609; 850 antibodies from 44 providers.
DR DNASU; 20979; -.
DR Ensembl; ENSMUST00000064054; ENSMUSP00000063293; ENSMUSG00000035864.
DR Ensembl; ENSMUST00000105276; ENSMUSP00000100912; ENSMUSG00000035864.
DR GeneID; 20979; -.
DR KEGG; mmu:20979; -.
DR UCSC; uc007gzg.2; mouse.
DR CTD; 6857; -.
DR MGI; MGI:99667; Syt1.
DR VEuPathDB; HostDB:ENSMUSG00000035864; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000155394; -.
DR HOGENOM; CLU_023008_0_1_1; -.
DR InParanoid; P46096; -.
DR OMA; TELRHWM; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; P46096; -.
DR TreeFam; TF315600; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
DR BioGRID-ORCS; 20979; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Syt1; mouse.
DR PRO; PR:P46096; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P46096; protein.
DR Bgee; ENSMUSG00000035864; Expressed in medial dorsal nucleus of thalamus and 195 other tissues.
DR ExpressionAtlas; P46096; baseline and differential.
DR Genevisible; P46096; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031045; C:dense core granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR GO; GO:0044306; C:neuron projection terminus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0061891; F:calcium ion sensor activity; IDA:MGI.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:HGNC-UCL.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030348; F:syntaxin-3 binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IMP:MGI.
DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IDA:SynGO.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005513; P:detection of calcium ion; ISO:MGI.
DR GO; GO:0098746; P:fast, calcium ion-dependent exocytosis of neurotransmitter; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007269; P:neurotransmitter secretion; IDA:MGI.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISO:MGI.
DR GO; GO:1903235; P:positive regulation of calcium ion-dependent exocytosis of neurotransmitter; IMP:UniProtKB.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; ISO:MGI.
DR GO; GO:0051291; P:protein heterooligomerization; ISO:MGI.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IMP:CACAO.
DR GO; GO:0014059; P:regulation of dopamine secretion; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903305; P:regulation of regulated secretory pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:ParkinsonsUK-UCL.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IMP:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI.
DR GO; GO:0071911; P:synchronous neurotransmitter secretion; IMP:MGI.
DR GO; GO:0048278; P:vesicle docking; ISO:MGI.
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; IPR015428; Synaptotagmin1.
DR PANTHER; PTHR10024:SF239; PTHR10024:SF239; 1.
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; Calcium; Cytoplasm; Cytoplasmic vesicle; Differentiation;
KW Direct protein sequencing; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Repeat;
KW Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..421
FT /note="Synaptotagmin-1"
FT /id="PRO_0000183938"
FT TOPO_DOM 1..57
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 141..260
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 272..405
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 112..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..381
FT /note="Phospholipid binding"
FT /evidence="ECO:0000305"
FT BINDING 171
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 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
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:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21579"
FT MOD_RES 229
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 74
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 75
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 77
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 79
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 82
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT MUTAGEN 233
FT /note="R->Q: Reduces affinity for calcium and results in
FT decreased calcium-dependent neurotransmitter release."
FT /evidence="ECO:0000269|PubMed:11242035"
FT MUTAGEN 236
FT /note="K->Q: No effect on calcium-dependent
FT neurotransmitter release."
FT /evidence="ECO:0000269|PubMed:11242035"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:5VFE"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:5VFE"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:5VFE"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:5VFE"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:5VFE"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:5VFE"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:5VFE"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:5VFE"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:5VFE"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5VFE"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:5VFE"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:5VFE"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:5VFE"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:5VFF"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:5VFF"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:5VFF"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:5VFF"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:5VFF"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:5VFF"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:5VFF"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:5VFF"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5VFF"
FT STRAND 371..379
FT /evidence="ECO:0007829|PDB:5VFF"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:5VFF"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:5VFF"
FT HELIX 410..417
FT /evidence="ECO:0007829|PDB:5VFF"
SQ SEQUENCE 421 AA; 47418 MW; 7FDEFF37170BD169 CRC64;
MVSASRPEAL AAPVTTVATL VPHNATEPAS PGEGKEDAFS KLKQKFMNEL HKIPLPPWAL
IAIAIVAVLL VVTCCFCVCK KCLFKKKNKK KGKEKGGKNA INMKDVKDLG KTMKDQALKD
DDAETGLTDG EEKEEPKEEE KLGKLQYSLD YDFQNNQLLV GIIQAAELPA LDMGGTSDPY
VKVFLLPDKK KKFETKVHRK TLNPVFNEQF TFKVPYSELG GKTLVMAVYD FDRFSKHDII
GEFKVPMNTV DFGHVTEEWR DLQSAEKEEQ EKLGDICFSL RYVPTAGKLT VVILEAKNLK
KMDVGGLSDP YVKIHLMQNG KRLKKKKTTI KKNTLNPYYN ESFSFEVPFE QIQKVQVVVT
VLDYDKIGKN DAIGKVFVGY NSTGAELRHW SDMLANPRRP IAQWHTLQVE EEVDAMLAVK
K
