SYT2_MOUSE
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 03-AUG-2022, entry version 177.
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;
CC Evidence={ECO:0000255|PROSITE-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). Interacts with SCAMP5 (By
CC similarity). Interacts with STON2 (By similarity). Interacts with PRRT2
CC (PubMed:27052163). {ECO:0000250|UniProtKB:Q8N9I0,
CC ECO:0000269|PubMed:27052163, 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; Single-pass membrane protein. Cytoplasmic vesicle,
CC secretory vesicle, chromaffin granule membrane; Single-pass membrane
CC protein. Cytoplasm.
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 -!- 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; 24.
DR DIP; DIP-32645N; -.
DR IntAct; P46097; 10.
DR MINT; P46097; -.
DR STRING; 10090.ENSMUSP00000112438; -.
DR GlyGen; P46097; 1 site.
DR iPTMnet; P46097; -.
DR PhosphoSitePlus; P46097; -.
DR SwissPalm; P46097; -.
DR MaxQB; P46097; -.
DR PaxDb; P46097; -.
DR PeptideAtlas; P46097; -.
DR PRIDE; P46097; -.
DR ProteomicsDB; 254797; -.
DR DNASU; 20980; -.
DR GeneID; 20980; -.
DR KEGG; mmu:20980; -.
DR UCSC; uc007csj.1; mouse.
DR CTD; 127833; -.
DR MGI; MGI:99666; Syt2.
DR eggNOG; KOG1028; Eukaryota.
DR InParanoid; P46097; -.
DR OrthoDB; 925064at2759; -.
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 74 CRISPR screens.
DR EvolutionaryTrace; P46097; -.
DR PRO; PR:P46097; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P46097; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
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; IBA:GO_Central.
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:0000149; F:SNARE binding; IBA:GO_Central.
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: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; 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 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:SF223; PTHR10024:SF223; 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 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 230
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
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, wild-
FT 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
