ID   SYT2_MOUSE              Reviewed;         422 AA.
AC   P46097; Q8R0E1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-NOV-2023, entry version 182.
DE   RecName: Full=Synaptotagmin-2 {ECO:0000305};
DE   AltName: Full=Inositol polyphosphate-binding protein {ECO:0000303|PubMed:7961887};
DE            Short=IP4-binding protein {ECO:0000303|PubMed:7961887};
DE            Short=IP4BP {ECO:0000303|PubMed:7961887};
DE   AltName: Full=Synaptotagmin II {ECO:0000312|MGI:MGI:99666};
DE            Short=SytII {ECO:0000250|UniProtKB:P29101};
GN   Name=Syt2 {ECO:0000312|MGI:MGI:99666};
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], FUNCTION, AND DOMAIN.
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 [GENOMIC DNA].
RA   Adachi R., Teich A.H., Nigam R.;
RT   "Genomic structure of the murine Syt2 gene.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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   [4]
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   [5]
RP   FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE B RECEPTOR (MICROBIAL INFECTION),
RP   AND SUBUNIT (MICROBIAL INFECTION).
RX   PubMed=14504267; DOI=10.1083/jcb.200305098;
RA   Dong M., Richards D.A., Goodnough M.C., Tepp W.H., Johnson E.A.,
RA   Chapman E.R.;
RT   "Synaptotagmins I and II mediate entry of botulinum neurotoxin B into
RT   cells.";
RL   J. Cell Biol. 162:1293-1303(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-230, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Brown adipose tissue;
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   [8]
RP   FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE G RECEPTOR (MICROBIAL INFECTION),
RP   SUBUNIT (MICROBIAL INFECTION), AND MUTAGENESIS OF PHE-47; LEU-50; GLU-52;
RP   PHE-54 AND PHE-55.
RX   PubMed=20219474; DOI=10.1016/j.jmb.2010.02.041;
RA   Stenmark P., Dong M., Dupuy J., Chapman E.R., Stevens R.C.;
RT   "Crystal structure of the botulinum neurotoxin type G binding domain:
RT   insight into cell surface binding.";
RL   J. Mol. Biol. 397:1287-1297(2010).
RN   [9]
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).
RN   [10] {ECO:0007744|PDB:2NP0}
RP   X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 40-60 IN COMPLEX WITH C.BOTULINUM
RP   NEUROTOXIN TYPE B, FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE B RECEPTOR
RP   (MICROBIAL INFECTION), SUBUNIT (MICROBIAL INFECTION), DOMAIN (MICROBIAL
RP   INFECTION), AND MUTAGENESIS OF PHE-47; 48-ALA--GLU-52; 52-GLU--PHE-55;
RP   GLU-52; PHE-54; PHE-55 AND 58-ILE-ASN-59.
RX   PubMed=17167418; DOI=10.1038/nature05411;
RA   Chai Q., Arndt J.W., Dong M., Tepp W.H., Johnson E.A., Chapman E.R.,
RA   Stevens R.C.;
RT   "Structural basis of cell surface receptor recognition by botulinum
RT   neurotoxin B.";
RL   Nature 444:1096-1100(2006).
RN   [11] {ECO:0007744|PDB:4KBB}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 8-61 IN COMPLEX WITH C.BOTULINUM
RP   NEUROTOXIN TYPE B AND GANGLIOSIDE GD1A, SUBUNIT (MICROBIAL INFECTION), AND
RP   DOMAIN (MICROBIAL INFECTION).
RX   PubMed=23807078; DOI=10.1038/ncomms3058;
RA   Berntsson R.P., Peng L., Dong M., Stenmark P.;
RT   "Structure of dual receptor binding to botulinum neurotoxin B.";
RL   Nat. Commun. 4:2058-2058(2013).
CC   -!- FUNCTION: Exhibits calcium-dependent phospholipid and inositol
CC       polyphosphate binding properties (PubMed:7961887). 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       Plays a role in dendrite formation by melanocytes (By similarity).
CC       {ECO:0000250|UniProtKB:Q8N9I0, ECO:0000269|PubMed:7961887}.
CC   -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC       type B (BoNT/B, botB); interaction is improved in the presence of
CC       gangliosides (PubMed:14504267). The toxin binds via the vesicular
CC       domain (residues 47-60) (PubMed:14504267, PubMed:17167418,
CC       PubMed:23807078). {ECO:0000269|PubMed:14504267,
CC       ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:23807078}.
CC   -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC       type G (BoNT/G, botG); gangliosides are not required for (or only very
CC       slightly improve) binding to a membrane-anchored receptor fragment
CC       (PubMed:20219474). The toxin binds via the vesicular domain (residues
CC       47-55) (PubMed:20219474). {ECO:0000269|PubMed:20219474}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00041};
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). Heterodimer; heterodimerizes with
CC       SYT1 in presence of calcium (By similarity). Interacts with SCAMP5 (By
CC       similarity). Interacts with STON2 (By similarity). Interacts with PRRT2
CC       (PubMed:27052163). {ECO:0000250|UniProtKB:P29101,
CC       ECO:0000250|UniProtKB:Q8N9I0, ECO:0000269|PubMed:27052163,
CC       ECO:0000305}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC       type B (BoNT/B, botB). {ECO:0000269|PubMed:14504267,
CC       ECO:0000269|PubMed:17167418, ECO:0000269|PubMed:23807078}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC       type G (BoNT/G, botG). {ECO:0000269|PubMed:20219474}.
CC   -!- INTERACTION:
CC       P46097; O35526: Stx1a; NbExp=2; IntAct=EBI-457969, EBI-400878;
CC       P46097; P10844: botB; Xeno; NbExp=3; IntAct=EBI-457969, EBI-7661991;
CC       P46097; Q8TAC9: SCAMP5; Xeno; NbExp=2; IntAct=EBI-457969, EBI-2695784;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250|UniProtKB:P29101}; Single-pass membrane
CC       protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle,
CC       chromaffin granule membrane {ECO:0000250|UniProtKB:P21707}; Single-pass
CC       membrane protein {ECO:0000250|UniProtKB:P29101}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P29101}.
CC   -!- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid
CC       binding (PubMed:7961887).
CC   -!- DOMAIN: The second C2 domain mediates interaction with Stonin 2. The
CC       second C2 domain mediates phospholipid and inositol polyphosphate
CC       binding in a calcium-independent manner (PubMed:7961887).
CC       {ECO:0000269|PubMed:7961887}.
CC   -!- DOMAIN: (Microbial infection) Binding to BoNT/B induces formation of an
CC       alpha-helix in the membrane-proximal extracytoplasmic domain
CC       (PubMed:17167418, PubMed:23807078). {ECO:0000305|PubMed:17167418,
CC       ECO:0000305|PubMed:23807078}.
CC   -!- PTM: Phosphorylation at Thr-202 by WNK1, changes the calcium
CC       requirement for SYT2-binding to phospholipid membranes.
CC       {ECO:0000250|UniProtKB:P29101}.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR   EMBL; D37793; BAA07041.1; -; mRNA.
DR   EMBL; AF257303; AAF68987.1; -; Genomic_DNA.
DR   EMBL; AF257304; AAF68988.1; -; mRNA.
DR   EMBL; AK036357; BAC29397.1; -; mRNA.
DR   EMBL; BC027019; AAH27019.1; -; mRNA.
DR   CCDS; CCDS15312.1; -.
DR   PIR; A55417; A55417.
DR   RefSeq; NP_033333.2; NM_009307.3.
DR   RefSeq; XP_006529385.1; XM_006529322.1.
DR   RefSeq; XP_006529386.1; XM_006529323.3.
DR   PDB; 2NP0; X-ray; 2.62 A; B=40-60.
DR   PDB; 4KBB; X-ray; 2.30 A; C/D=8-61.
DR   PDBsum; 2NP0; -.
DR   PDBsum; 4KBB; -.
DR   AlphaFoldDB; P46097; -.
DR   SMR; P46097; -.
DR   BioGRID; 203612; 25.
DR   DIP; DIP-32645N; -.
DR   IntAct; P46097; 10.
DR   MINT; P46097; -.
DR   STRING; 10090.ENSMUSP00000112438; -.
DR   GlyCosmos; P46097; 1 site, No reported glycans.
DR   GlyGen; P46097; 1 site.
DR   iPTMnet; P46097; -.
DR   PhosphoSitePlus; P46097; -.
DR   SwissPalm; P46097; -.
DR   MaxQB; P46097; -.
DR   PaxDb; 10090-ENSMUSP00000112438; -.
DR   PeptideAtlas; P46097; -.
DR   ProteomicsDB; 254797; -.
DR   DNASU; 20980; -.
DR   GeneID; 20980; -.
DR   KEGG; mmu:20980; -.
DR   UCSC; uc007csj.1; mouse.
DR   AGR; MGI:99666; -.
DR   CTD; 127833; -.
DR   MGI; MGI:99666; Syt2.
DR   eggNOG; KOG1028; Eukaryota.
DR   InParanoid; P46097; -.
DR   OrthoDB; 590187at2759; -.
DR   PhylomeDB; P46097; -.
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; 20980; 3 hits in 79 CRISPR screens.
DR   EvolutionaryTrace; P46097; -.
DR   PRO; PR:P46097; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P46097; Protein.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031045; C:dense core granule; IBA:GO_Central.
DR   GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR   GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR   GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0001786; F:phosphatidylserine binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR   GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
DR   GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IDA:SynGO.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR   GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR   GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR   GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR   CDD; cd08385; C2A_Synaptotagmin-1-5-6-9-10; 1.
DR   CDD; cd08402; C2B_Synaptotagmin-1; 1.
DR   CDD; cd21964; Syt2_N; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001565; Synaptotagmin.
DR   PANTHER; PTHR10024; SYNAPTOTAGMIN; 1.
DR   PANTHER; PTHR10024:SF223; SYNAPTOTAGMIN-2; 1.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   PROSITE; PS50004; C2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cytoplasm; Cytoplasmic vesicle; Differentiation;
KW   Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW   Repeat; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN           1..422
FT                   /note="Synaptotagmin-2"
FT                   /id="PRO_0000183943"
FT   TOPO_DOM        1..60
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          142..261
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          273..406
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..382
FT                   /note="Phospholipid binding"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        103..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..137
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         173
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         173
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         179
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
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         231
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="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         233
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
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         236
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         237
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         239
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         239
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         310
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         364
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   BINDING         366
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   MOD_RES         125
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P29101"
FT   MOD_RES         128
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         202
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P29101"
FT   MOD_RES         230
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   MOD_RES         386
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P29101"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         47
FT                   /note="F->A: No binding to C.botulinum neurotoxin type B
FT                   (BoNT/B, botB). Requires gangliosides to bind BoNT/B,
FT                   wild-type binding to BoNT/G."
FT                   /evidence="ECO:0000269|PubMed:17167418,
FT                   ECO:0000269|PubMed:20219474"
FT   MUTAGEN         48..52
FT                   /note="AKLKE->SKLKQ: Wild-type binding to BoNT/B."
FT                   /evidence="ECO:0000269|PubMed:17167418"
FT   MUTAGEN         50
FT                   /note="L->A: Wild-type in binding to C.botulinum neurotoxin
FT                   type G (BoNT/G, botG)."
FT                   /evidence="ECO:0000269|PubMed:20219474"
FT   MUTAGEN         52..55
FT                   /note="EKFF->QKFM: Wild-type binding to BoNT/B. Wild-type
FT                   in binding to BoNT/G."
FT                   /evidence="ECO:0000269|PubMed:17167418,
FT                   ECO:0000269|PubMed:20219474"
FT   MUTAGEN         52
FT                   /note="E->A: Wild-type binding to BoNT/B."
FT                   /evidence="ECO:0000269|PubMed:17167418"
FT   MUTAGEN         54
FT                   /note="F->A: No binding to BoNT/B. No binding to BoNT/G."
FT                   /evidence="ECO:0000269|PubMed:17167418,
FT                   ECO:0000269|PubMed:20219474"
FT   MUTAGEN         54
FT                   /note="F->M: Requires gangliosides to bind BoNT/B, no
FT                   binding to BoNT/G with or without gangliosides."
FT                   /evidence="ECO:0000269|PubMed:20219474"
FT   MUTAGEN         55
FT                   /note="F->A: No binding to BoNT/B. Wild-type binding to
FT                   BoNT/G."
FT                   /evidence="ECO:0000269|PubMed:17167418,
FT                   ECO:0000269|PubMed:20219474"
FT   MUTAGEN         58..59
FT                   /note="IN->LH: Only binds to BoNT/B in presence of
FT                   gangliosides."
FT                   /evidence="ECO:0000269|PubMed:17167418"
FT   CONFLICT        221
FT                   /note="A -> G (in Ref. 3; BAC29397 and 4; AAH27019)"
FT                   /evidence="ECO:0000305"
FT   HELIX           46..57
FT                   /evidence="ECO:0007829|PDB:4KBB"
SQ   SEQUENCE   422 AA;  47263 MW;  B4BD13FF70E0481B CRC64;
     MRNIFKRNQE PNVAPATTTA TMPLAPVAPA DNSTESTGPG ESQEDMFAKL KEKFFNEINK
     IPLPPWALIA MAVVAGLLLL TCCFCICKKC CCKKKKNKKE KGKGMKNAMN MKDMKGGQDD
     DDAETGLTEG EGEGEEEKEP ENLGKLQFSL DYDFQANQLT VGVLQAAELP ALDMGGTSDP
     YVKVFLLPDK KKKYETKVHR KTLNPAFNET FTFKVPYQEL AGKTLVMAIY DFDRFSKHDI
     IGEVKVPMNT VDLGQPIEEW RDLQGGEKEE PEKLGDICTS LRYVPTAGKL TVCILEAKNL
     KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT VKKKTLNPYF NESFSFEIPF EQIQKVQVVV
     TVLDYDKLGK NEAIGKIFVG SNATGTELRH WSDMLANPRR PIAQWHSLKP EEEVDALLGK
     NK
//