SYT2_CAEEL
ID SYT2_CAEEL Reviewed; 369 AA.
AC K8FE10;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Synaptotagmin 2 {ECO:0000312|WormBase:F42G9.7};
GN Name=snt-2 {ECO:0000312|WormBase:F42G9.7};
GN ORFNames=F42G9.7 {ECO:0000312|WormBase:F42G9.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-247 AND ASP-253.
RX PubMed=23583549; DOI=10.1016/j.cub.2013.03.049;
RA Wang H., Girskis K., Janssen T., Chan J.P., Dasgupta K., Knowles J.A.,
RA Schoofs L., Sieburth D.;
RT "Neuropeptide secreted from a pacemaker activates neurons to control a
RT rhythmic behavior.";
RL Curr. Biol. 23:746-754(2013).
CC -!- FUNCTION: Ca(2+) sensor involved in Ca(2+)-dependent secretion of the
CC nlp-40 neuropeptide from intestinal cells. Involved in the defecation
CC motor program, which is a coordinated series of three muscle
CC contractions that occurs every 45 seconds.
CC {ECO:0000269|PubMed:23583549}.
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 C2 domain. {ECO:0000250|UniProtKB:Q9R0N7,
CC ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:23583549}. Note=Co-localizes with nlp-40 in
CC cytoplasmic vesicles. {ECO:0000269|PubMed:23583549}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the intestine and in several
CC neurons in the head and tail. {ECO:0000269|PubMed:23583549}.
CC -!- DISRUPTION PHENOTYPE: Defecation abnormalities.
CC {ECO:0000269|PubMed:23583549}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; BX284603; CCO25912.1; -; Genomic_DNA.
DR RefSeq; NP_497261.2; NM_064860.4.
DR AlphaFoldDB; K8FE10; -.
DR SMR; K8FE10; -.
DR IntAct; K8FE10; 1.
DR STRING; 6239.F42G9.7; -.
DR EPD; K8FE10; -.
DR PaxDb; K8FE10; -.
DR EnsemblMetazoa; F42G9.7.1; F42G9.7.1; WBGene00004922.
DR GeneID; 185680; -.
DR KEGG; cel:CELE_F42G9.7; -.
DR CTD; 185680; -.
DR WormBase; F42G9.7; CE37915; WBGene00004922; snt-2.
DR eggNOG; KOG1028; Eukaryota.
DR HOGENOM; CLU_023008_11_0_1; -.
DR InParanoid; K8FE10; -.
DR OMA; HWHTLQP; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; K8FE10; -.
DR Reactome; R-CEL-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-CEL-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-CEL-888590; GABA synthesis, release, reuptake and degradation.
DR PRO; PR:K8FE10; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004922; Expressed in adult organism and 4 other tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0031045; C:dense core granule; IDA:WormBase.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
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:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
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: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 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 Calcium; Cytoplasmic vesicle; Exocytosis; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..369
FT /note="Synaptotagmin 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438195"
FT DOMAIN 83..204
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 216..354
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 120
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="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 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 307
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 309
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="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MUTAGEN 247
FT /note="D->N: Defecation defect; when associated with N-
FT 253."
FT /evidence="ECO:0000269|PubMed:23583549"
FT MUTAGEN 253
FT /note="D->N: Defecation defect; when associated with N-
FT 247."
FT /evidence="ECO:0000269|PubMed:23583549"
SQ SEQUENCE 369 AA; 42411 MW; F4E45EC64CB86821 CRC64;
MWATGAIVCS PVFRILSTCC PIRRGVPTSN GYHPRPKHVD IGNGAVPILS SKPITVQPTN
SDYYEPVNNG TLPLSSSGAL IKQYGNIHFR VEYDFEQSKL SVTIVSASDL PAMDRNGMSD
PYVKVYVLPE RKQKFETRII RNTLNPTYNE TFQFSIPFNE LHSKTLMLVV YDYDRLSKDD
KMGQLSVPLE SIDFGITTDI ERPLQKPEKD DEKECRLGDI CFSTRYRPAT GTVTLTIMEA
RNLKKMDVGG SSDPYVKIYL HHGRKLLSKK KTSRKYKTLN PYYNESFQFK IEPHMIEKVH
LIVSVWDYDK MSKNDFIGEV TLGSKHLNLP QITHACSEQW AEMMTSRRPV VQWHTLQERM
EKEKKKDDD
