SYT1_CAEEL
ID SYT1_CAEEL Reviewed; 441 AA.
AC P34693;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Synaptotagmin-1;
DE AltName: Full=Synaptotagmin I;
GN Name=snt-1; ORFNames=F31E8.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=8391930; DOI=10.1016/0092-8674(93)90357-v;
RA Nonet M.L., Grundahl K., Meyer B.J., Rand J.B.;
RT "Synaptic function is impaired but not eliminated in C. elegans mutants
RT lacking synaptotagmin.";
RL Cell 73:1291-1305(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22157748; DOI=10.1038/emboj.2011.447;
RA Troulinaki K., Tavernarakis N.;
RT "Endocytosis and intracellular trafficking contribute to necrotic
RT neurodegeneration in C. elegans.";
RL EMBO J. 31:654-666(2012).
CC -!- FUNCTION: May have a regulatory role in the membrane interactions
CC during trafficking of synaptic vesicles at the active zone of the
CC synapse. It binds acidic phospholipids with a specificity that requires
CC the presence of both an acidic head group and a diacyl backbone (By
CC similarity). Involved in necrotic cell death (PubMed:22157748).
CC {ECO:0000250|UniProtKB:P21579, ECO:0000269|PubMed:22157748}.
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane; Single-pass membrane protein. Synapse. Note=And
CC vesicle-like structures.
CC -!- TISSUE SPECIFICITY: Localized to regions known to be rich in synapses
CC and appears to be associated with synaptic vesicles. Also found in some
CC non-neuronal secretory structures.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit severe behavioral abnormalities
CC that are characteristic of deficiencies in synaptic function, including
CC severe locomotion, feeding, and defecation defects (PubMed:8391930).
CC Increased survival in response to hypoxia induced by sodium azide
CC (PubMed:22157748). Reduces the formation of neuron cell corpses in a
CC hyperactive mec-4 or deg-3 mutant background (PubMed:22157748).
CC {ECO:0000269|PubMed:22157748, ECO:0000269|PubMed:8391930}.
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; L15302; AAA28145.1; -; mRNA.
DR EMBL; FO080321; CCD62852.1; -; Genomic_DNA.
DR PIR; A40707; A40707.
DR RefSeq; NP_001022129.1; NM_001026958.3.
DR AlphaFoldDB; P34693; -.
DR SMR; P34693; -.
DR BioGRID; 39458; 3.
DR STRING; 6239.F31E8.2b; -.
DR TCDB; 1.F.1.1.3; the synaptosomal vesicle fusion pore (svf-pore) family.
DR EPD; P34693; -.
DR PaxDb; P34693; -.
DR PeptideAtlas; P34693; -.
DR PRIDE; P34693; -.
DR EnsemblMetazoa; F31E8.2a.1; F31E8.2a.1; WBGene00004921.
DR GeneID; 174120; -.
DR UCSC; F31E8.2a; c. elegans.
DR CTD; 174120; -.
DR WormBase; F31E8.2a; CE02711; WBGene00004921; snt-1.
DR eggNOG; KOG1028; Eukaryota.
DR HOGENOM; CLU_023008_0_1_1; -.
DR InParanoid; P34693; -.
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:P34693; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004921; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; P34693; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0031045; C:dense core granule; IBA:GO_Central.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0008021; C:synaptic vesicle; IDA:WormBase.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:WormBase.
DR GO; GO:0061891; F:calcium ion sensor activity; IMP:WormBase.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:WormBase.
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:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
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:0046928; P:regulation of neurotransmitter secretion; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:WormBase.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; TAS:WormBase.
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 2: Evidence at transcript level;
KW Calcium; Cytoplasmic vesicle; Membrane; Metal-binding; Necrosis;
KW Reference proteome; Repeat; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..441
FT /note="Synaptotagmin-1"
FT /id="PRO_0000183988"
FT TOPO_DOM 1..69
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 159..278
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 292..425
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 441 AA; 49904 MW; F8D174337EB472DB CRC64;
MVKLDFSSQD EENDEDLTKE FVRDEAPMEE TTSEAVKQIA TTTKETLKDV VVNKVIDVKD
VVKEKVMQQT GMPEWAFVFL GFVFILLVLA CAFCLIRKLF GKKRHGEKNK KGGLKGFFGK
GQDVVDGKNI QGMAQDLEEL GDAMEQNEKE QAEEKEEVKL GRIQYKLDYD FQQGQLTVTV
IQAEDLPGMD MSGTSDPYVK LYLLPEKKKK VETKVHRKTL NPVFNETFIF KVAFNEITAK
TLVFAIYDFD RFSKHDQIGQ VLIPLGKIDL GAVIEEWKDI APPPDDKEAE KSLGDICFSL
RYVPTAGKLT VVILEAKNLK KMDVGGLSDP YVKIVLMQGG KRLKKKKTSI KKCTLNPYYN
ESFSFEVPFE QIQKVSLMIT VMDYDKLGSN DAIGRCLLGC NGTGAELRHW MDMLASPRRP
IAQWHTLGPV EEEGDKKDDK K
