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Synaptotagmin-1 (Synaptotagmin I)

 SYT1_CAEEL              Reviewed;         441 AA.
P34693;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
23-MAY-2018, entry version 144.
RecName: Full=Synaptotagmin-1;
AltName: Full=Synaptotagmin I;
Name=snt-1; ORFNames=F31E8.2;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
STRAIN=Bristol N2;
PubMed=8391930; DOI=10.1016/0092-8674(93)90357-V;
Nonet M.L., Grundahl K., Meyer B.J., Rand J.B.;
"Synaptic function is impaired but not eliminated in C. elegans
mutants lacking synaptotagmin.";
Cell 73:1291-1305(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22157748; DOI=10.1038/emboj.2011.447;
Troulinaki K., Tavernarakis N.;
"Endocytosis and intracellular trafficking contribute to necrotic
neurodegeneration in C. elegans.";
EMBO J. 31:654-666(2012).
-!- FUNCTION: May have a regulatory role in the membrane interactions
during trafficking of synaptic vesicles at the active zone of the
synapse. It binds acidic phospholipids with a specificity that
requires the presence of both an acidic head group and a diacyl
backbone (By similarity). Involved in necrotic cell death
(PubMed:22157748). {ECO:0000250|UniProtKB:P21579,
ECO:0000269|PubMed:22157748}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
domains. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
synaptic vesicle membrane; Single-pass membrane protein. Cell
junction, synapse. Note=And vesicle-like structures.
-!- TISSUE SPECIFICITY: Localized to regions known to be rich in
synapses and appears to be associated with synaptic vesicles. Also
found in some non-neuronal secretory structures.
-!- DISRUPTION PHENOTYPE: Worms exhibit severe behavioral
abnormalities that are characteristic of deficiencies in synaptic
function, including severe locomotion, feeding, and defecation
defects (PubMed:8391930). Increased survival in response to
hypoxia induced by sodium azide (PubMed:22157748). Reduces the
formation of neuron cell corpses in a hyperactive mec-4 or deg-3
mutant background (PubMed:22157748). {ECO:0000269|PubMed:22157748,
ECO:0000269|PubMed:8391930}.
-!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L15302; AAA28145.1; -; mRNA.
EMBL; FO080321; CCD62852.1; -; Genomic_DNA.
PIR; A40707; A40707.
RefSeq; NP_001022129.1; NM_001026958.3.
UniGene; Cel.18270; -.
ProteinModelPortal; P34693; -.
SMR; P34693; -.
STRING; 6239.F31E8.2b; -.
TCDB; 1.F.1.1.3; the synaptosomal vesicle fusion pore (svf-pore) family.
EPD; P34693; -.
PaxDb; P34693; -.
PeptideAtlas; P34693; -.
PRIDE; P34693; -.
EnsemblMetazoa; F31E8.2a; F31E8.2a; WBGene00004921.
GeneID; 174120; -.
UCSC; F31E8.2a; c. elegans.
CTD; 174120; -.
WormBase; F31E8.2a; CE02711; WBGene00004921; snt-1.
eggNOG; ENOG410IT3Q; Eukaryota.
eggNOG; ENOG410Z15P; LUCA.
GeneTree; ENSGT00760000118973; -.
HOGENOM; HOG000232127; -.
InParanoid; P34693; -.
Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
PRO; PR:P34693; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00004921; -.
ExpressionAtlas; P34693; baseline and differential.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0045202; C:synapse; IDA:WormBase.
GO; GO:0008021; C:synaptic vesicle; IDA:WormBase.
GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
GO; GO:0030421; P:defecation; IMP:WormBase.
GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:WormBase.
GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:WormBase.
GO; GO:0016079; P:synaptic vesicle exocytosis; TAS:WormBase.
GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
Gene3D; 2.60.40.150; -; 2.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR001565; Synaptotagmin.
InterPro; IPR015428; Synaptotagmin1/2.
PANTHER; PTHR10024:SF239; PTHR10024:SF239; 1.
Pfam; PF00168; C2; 2.
PRINTS; PR00360; C2DOMAIN.
PRINTS; PR00399; SYNAPTOTAGMN.
SMART; SM00239; C2; 2.
PROSITE; PS50004; C2; 2.
2: Evidence at transcript level;
Calcium; Cell junction; Complete proteome; Cytoplasmic vesicle;
Membrane; Metal-binding; Necrosis; Reference proteome; Repeat;
Synapse; Transmembrane; Transmembrane helix.
CHAIN 1 441 Synaptotagmin-1.
/FTId=PRO_0000183988.
TOPO_DOM 1 69 Vesicular. {ECO:0000255}.
TRANSMEM 70 96 Helical. {ECO:0000255}.
TOPO_DOM 97 441 Cytoplasmic. {ECO:0000255}.
DOMAIN 175 262 C2 1. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 306 397 C2 2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
METAL 190 190 Calcium 1. {ECO:0000250}.
METAL 190 190 Calcium 2. {ECO:0000250}.
METAL 196 196 Calcium 1. {ECO:0000250}.
METAL 248 248 Calcium 1. {ECO:0000250}.
METAL 248 248 Calcium 2. {ECO:0000250}.
METAL 249 249 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 250 250 Calcium 1. {ECO:0000250}.
METAL 250 250 Calcium 2. {ECO:0000250}.
METAL 250 250 Calcium 3. {ECO:0000250}.
METAL 253 253 Calcium 3. {ECO:0000250}.
METAL 254 254 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 256 256 Calcium 2. {ECO:0000250}.
METAL 256 256 Calcium 3. {ECO:0000250}.
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


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