SYT2_RAT
ID SYT2_RAT Reviewed; 422 AA.
AC P29101;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Synaptotagmin-2 {ECO:0000305};
DE AltName: Full=Synaptotagmin II {ECO:0000303|PubMed:1856191, ECO:0000312|RGD:3804};
DE Short=SytII {ECO:0000303|PubMed:1856191};
GN Name=Syt2 {ECO:0000312|RGD:3804};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=1856191; DOI=10.1016/s0021-9258(18)92733-x;
RA Geppert M., Archer B.T. III, Suedhof T.C.;
RT "Synaptotagmin II. A novel differentially distributed form of
RT synaptotagmin.";
RL J. Biol. Chem. 266:13548-13552(1991).
RN [2]
RP COFACTOR.
RX PubMed=11823420; DOI=10.1093/emboj/21.3.270;
RA Sugita S., Shin O.H., Han W., Lao Y., Suedhof T.C.;
RT "Synaptotagmins form a hierarchy of exocytotic Ca(2+) sensors with distinct
RT Ca(2+) affinities.";
RL EMBO J. 21:270-280(2002).
RN [3]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE G RECEPTOR (MICROBIAL INFECTION),
RP AND SUBUNIT (MICROBIAL INFECTION).
RX PubMed=15123599; DOI=10.1074/jbc.m403945200;
RA Rummel A., Karnath T., Henke T., Bigalke H., Binz T.;
RT "Synaptotagmins I and II act as nerve cell receptors for botulinum
RT neurotoxin G.";
RL J. Biol. Chem. 279:30865-30870(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125 AND THR-128, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5] {ECO:0007744|PDB:2NM1}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 44-60 IN COMPLEX WITH C.BOTULINUM
RP NEUROTOXIN TYPE B C-TERMINUS, FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE B
RP RECEPTOR (MICROBIAL INFECTION), SUBUNIT (MICROBIAL INFECTION), DOMAIN
RP (MICROBIAL INFECTION), AND MUTAGENESIS OF MET-46; PHE-47; LEU-50; PHE-54;
RP PHE-55; GLU-57 AND ASN-59.
RX PubMed=17167421; DOI=10.1038/nature05387;
RA Jin R., Rummel A., Binz T., Brunger A.T.;
RT "Botulinum neurotoxin B recognizes its protein receptor with high affinity
RT and specificity.";
RL Nature 444:1092-1095(2006).
CC -!- FUNCTION: Exhibits calcium-dependent phospholipid and inositol
CC polyphosphate binding properties. May have a regulatory role in the
CC membrane interactions during trafficking of synaptic vesicles at the
CC active zone of the synapse. Plays a role in dendrite formation by
CC melanocytes. {ECO:0000250|UniProtKB:P46097,
CC ECO:0000250|UniProtKB:Q8N9I0}.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type B (BoNT/B, botB); unlike the case with BoNT/B interaction is not
CC improved in the presence of gangliosides (PubMed:17167421). The toxin
CC binds to the vesicular domain of Syt2 (residues 1-61)
CC (PubMed:15123599). {ECO:0000269|PubMed:15123599}.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type G (BoNT/G, botG); unlike the case with BoNT/B interaction is not
CC improved in the presence of gangliosides (PubMed:15123599). The toxin
CC binds to the vesicular domain of Syt2 (residues 1-61)
CC (PubMed:15123599). {ECO:0000269|PubMed:15123599}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:11823420};
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 (By similarity). {ECO:0000250|UniProtKB:P46097,
CC ECO:0000250|UniProtKB:Q8N9I0, ECO:0000305}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC type G (BoNT/G, botG). {ECO:0000269|PubMed:15123599}.
CC -!- INTERACTION:
CC P29101; Q9JIH7: Wnk1; NbExp=9; IntAct=EBI-458017, EBI-457953;
CC P29101; A5JGM8: bont; Xeno; NbExp=2; IntAct=EBI-458017, EBI-16067725;
CC P29101; P10844: botB; Xeno; NbExp=6; IntAct=EBI-458017, EBI-7661991;
CC P29101; Q9H4A3: WNK1; Xeno; NbExp=2; IntAct=EBI-458017, EBI-457907;
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 -!- TISSUE SPECIFICITY: Predominantly expressed in brain regions such as
CC the spinal cord, brain stem and cerebellum (PubMed:1856191).
CC {ECO:0000269|PubMed:1856191}.
CC -!- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid
CC binding. {ECO:0000250|UniProtKB:P46097}.
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.
CC {ECO:0000250|UniProtKB:P46097}.
CC -!- DOMAIN: (Microbial infection) Binding to BoNT/B induces formation of an
CC alpha-helix in the membrane-proximal extracytoplasmic domain
CC (PubMed:17167421). {ECO:0000305|PubMed:17167421}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M64488; AAA63502.1; -; mRNA.
DR PIR; A39454; BMRT2Y.
DR RefSeq; NP_036797.1; NM_012665.1.
DR PDB; 2NM1; X-ray; 2.15 A; B=44-60.
DR PDB; 4ISR; X-ray; 2.59 A; D/E/F=40-60.
DR PDBsum; 2NM1; -.
DR PDBsum; 4ISR; -.
DR AlphaFoldDB; P29101; -.
DR SMR; P29101; -.
DR BioGRID; 246928; 4.
DR CORUM; P29101; -.
DR DIP; DIP-32642N; -.
DR IntAct; P29101; 8.
DR MINT; P29101; -.
DR STRING; 10116.ENSRNOP00000006637; -.
DR GlyGen; P29101; 1 site.
DR iPTMnet; P29101; -.
DR PhosphoSitePlus; P29101; -.
DR SwissPalm; P29101; -.
DR PaxDb; P29101; -.
DR PRIDE; P29101; -.
DR GeneID; 24805; -.
DR KEGG; rno:24805; -.
DR UCSC; RGD:3804; rat.
DR CTD; 127833; -.
DR RGD; 3804; Syt2.
DR eggNOG; KOG1028; Eukaryota.
DR InParanoid; P29101; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; P29101; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; P29101; -.
DR PRO; PR:P29101; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:RGD.
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; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:BHF-UCL.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IDA:BHF-UCL.
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; ISO:RGD.
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:RGD.
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:0016079; P:synaptic vesicle exocytosis; TAS:RGD.
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_0000183944"
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 16..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:0007744|PubMed:22673903"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 230
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46097"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 46
FT /note="M->A: Nearly wild-type binding of fragment 1-61 to
FT BoNT/B heavy chain."
FT /evidence="ECO:0000269|PubMed:17167421"
FT MUTAGEN 47
FT /note="F->A: No binding of fragment 1-61 to BoNT/B heavy
FT chain."
FT /evidence="ECO:0000269|PubMed:17167421"
FT MUTAGEN 50
FT /note="L->A: Decreased binding of fragment 1-61 to BoNT/B
FT heavy chain."
FT /evidence="ECO:0000269|PubMed:17167421"
FT MUTAGEN 54
FT /note="F->A: No binding of fragment 1-61 to BoNT/B heavy
FT chain."
FT /evidence="ECO:0000269|PubMed:17167421"
FT MUTAGEN 55
FT /note="F->A: No binding of fragment 1-61 to BoNT/B heavy
FT chain."
FT /evidence="ECO:0000269|PubMed:17167421"
FT MUTAGEN 57
FT /note="E->K: No binding of fragment 1-61 to BoNT/B heavy
FT chain."
FT /evidence="ECO:0000269|PubMed:17167421"
FT MUTAGEN 59
FT /note="N->H: Nearly wild-type binding of fragment 1-61 to
FT BoNT/B heavy chain."
FT /evidence="ECO:0000269|PubMed:17167421"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:2NM1"
SQ SEQUENCE 422 AA; 47210 MW; D852AF5387E0C7FD CRC64;
MRNIFKRNQE PIVAPATTTA TMPLAPAAPA DNSTESTGTG ESQEDMFAKL KDKFFNEINK
IPLPPWALIA MAVVAGLLLL TCCFCICKKC CCKKKKNKKE KGKGMKNAMN MKDMKGGQDD
DDAETGLTEG EGEGEEEKEP ENLGKLQFSL DYDFQANQLT VGVLQAAELP ALDMGGTSDP
YVKVFLLPDK KKKYETKVHR KTLNPAFNET FTFKVPYQEL GGKTLVMAIY DFDRFSKHDI
IGEVKVPMNT VDLGQPIEEW RDLQGGEKEE PEKLGDICTS LRYVPTAGKL TVCILEAKNL
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT VKKKTLNPYF NESFSFEIPF EQIQKVQVVV
TVLDYDKLGK NEAIGKIFVG SNATGTELRH WSDMLANPRR PIAQWHSLKP EEEVDALLGK
NK
