ID SYT1_CHICK Reviewed; 424 AA. AC P47191; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 176. DE RecName: Full=Synaptotagmin-1; DE AltName: Full=Synaptotagmin I; DE Short=SytI; DE AltName: Full=p65; GN Name=SYT1; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8365570; DOI=10.1006/dbio.1993.1244; RA Lou X., Bixby J.L.; RT "Coordinate and noncoordinate regulation of synaptic vesicle protein genes RT during embryonic development."; RL Dev. Biol. 159:327-337(1993). CC -!- FUNCTION: Calcium sensor that participates in triggering CC neurotransmitter release at the synapse (By similarity). May have a CC regulatory role in the membrane interactions during trafficking of CC synaptic vesicles at the active zone of the synapse. It binds acidic CC phospholipids with a specificity that requires the presence of both an CC acidic head group and a diacyl backbone. May play a role in dendrite CC formation by melanocytes. {ECO:0000250|UniProtKB:P21579, CC ECO:0000250|UniProtKB:P46096}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC 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. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane CC {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle CC membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein CC {ECO:0000250|UniProtKB:P21707}. Cytoplasmic vesicle, secretory vesicle, CC chromaffin granule membrane {ECO:0000250|UniProtKB:P21707}; Single-pass CC membrane protein {ECO:0000250|UniProtKB:P21707}. Cytoplasm CC {ECO:0000250|UniProtKB:P21707}. CC -!- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid CC binding. {ECO:0000250|UniProtKB:P21707}. CC -!- DOMAIN: The second C2 domain mediates interaction with SV2A and CC probably with STN2. {ECO:0000250|UniProtKB:P21707}. 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; S64957; AAB28081.1; -; mRNA. DR PIR; I51210; I51210. DR RefSeq; NP_001383882.1; NM_001396953.1. DR RefSeq; NP_001383883.1; NM_001396954.1. DR RefSeq; NP_990502.1; NM_205171.2. DR RefSeq; XP_046762739.1; XM_046906783.1. DR RefSeq; XP_046762740.1; XM_046906784.1. DR RefSeq; XP_046770407.1; XM_046914451.1. DR RefSeq; XP_046770429.1; XM_046914473.1. DR AlphaFoldDB; P47191; -. DR SMR; P47191; -. DR FunCoup; P47191; 377. DR STRING; 9031.ENSGALP00000042075; -. DR GlyCosmos; P47191; 1 site, No reported glycans. DR GlyGen; P47191; 1 site. DR PaxDb; 9031-ENSGALP00000042075; -. DR Ensembl; ENSGALT00010028805.1; ENSGALP00010016573.1; ENSGALG00010012026.1. DR GeneID; 396083; -. DR KEGG; gga:396083; -. DR CTD; 6857; -. DR VEuPathDB; HostDB:geneid_396083; -. DR eggNOG; KOG1028; Eukaryota. DR GeneTree; ENSGT00940000155394; -. DR HOGENOM; CLU_023008_0_1_1; -. DR InParanoid; P47191; -. DR OMA; AXKEEEL; -. DR OrthoDB; 67700at2759; -. DR PhylomeDB; P47191; -. DR Reactome; R-GGA-181429; Serotonin Neurotransmitter Release Cycle. DR Reactome; R-GGA-181430; Norepinephrine Neurotransmitter Release Cycle. DR Reactome; R-GGA-212676; Dopamine Neurotransmitter Release Cycle. DR Reactome; R-GGA-264642; Acetylcholine Neurotransmitter Release Cycle. DR Reactome; R-GGA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-GGA-8856828; Clathrin-mediated endocytosis. DR Reactome; R-GGA-888590; GABA synthesis, release, reuptake and degradation. DR PRO; PR:P47191; -. DR Proteomes; UP000000539; Chromosome 1. DR Bgee; ENSGALG00000041094; Expressed in brain and 8 other cell types or tissues. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0031045; C:dense core granule; IBA:GO_Central. 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:0061891; F:calcium ion sensor activity; IBA:GO_Central. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central. DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central. DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IBA:GO_Central. DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IBA:GO_Central. DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central. DR CDD; cd08385; C2A_Synaptotagmin-1-5-6-9-10; 1. DR CDD; cd08402; C2B_Synaptotagmin-1; 1. DR CDD; cd21963; Syt1_N; 1. DR FunFam; 2.60.40.150:FF:000007; Synaptotagmin 1; 1. DR FunFam; 2.60.40.150:FF:000016; Synaptotagmin 1; 1. DR Gene3D; 2.60.40.150; C2 domain; 2. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR001565; Synaptotagmin. DR PANTHER; PTHR10024; SYNAPTOTAGMIN; 1. DR PANTHER; PTHR10024:SF239; SYNAPTOTAGMIN-1; 1. DR Pfam; PF00168; C2; 2. DR PRINTS; PR00360; C2DOMAIN. DR PRINTS; PR00399; SYNAPTOTAGMN. DR SMART; SM00239; C2; 2. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR PROSITE; PS50004; C2; 2. PE 2: Evidence at transcript level; KW Calcium; Cytoplasm; Cytoplasmic vesicle; Differentiation; Glycoprotein; KW Lipoprotein; Membrane; Metal-binding; Palmitate; Reference proteome; KW Repeat; Synapse; Transmembrane; Transmembrane helix. FT CHAIN 1..424 FT /note="Synaptotagmin-1" FT /id="PRO_0000183941" FT TOPO_DOM 1..60 FT /note="Vesicular" FT /evidence="ECO:0000255" FT TRANSMEM 61..82 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 83..424 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 144..263 FT /note="C2 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 275..408 FT /note="C2 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 117..142 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 138..384 FT /note="Phospholipid binding" FT /evidence="ECO:0000305" FT COMPBIAS 124..136 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 175 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 175 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 181 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 234 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 235 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 235 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 235 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 238 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="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 241 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 241 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 306 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 306 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 312 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 BINDING 366 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 368 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 368 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 374 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT LIPID 77 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P21707" FT LIPID 78 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P21707" FT LIPID 80 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P21707" FT LIPID 82 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P21707" FT LIPID 85 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P21707" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 424 AA; 47505 MW; C602676F8F679718 CRC64; MVSESHHEAL AAPPATTVAA ALPSNVTEPA APGGGGGKED AFSNLKKKFM NELNKIPLPP WALIAIAIVA VLLILTCCFC LCKKCLFKKK NKKKGKEKGG KNAINMKDVK DLGKTMKDQA LKDDDAETGL TDGEEKEEPK EVEKLGKIQY SLDYDFQNNQ LLVGIIQAAE LPALDMGGTS DPYVKVFLLP DKKKKYETKV HRKTLNPVFN EQFTFKVPYS ELGGKTLVMA VYDFDRFSKH DIIGEYKVAM NTVDFGHVTE EWRDLQSAEK EEQEKLGDIC FSLRYVPTAG KLTVVILEAK NLKKMDVGGL SDPYVKIHLM QNGKRLKKKK TTIKKNTLNP YYNESFSFEV PFEQIQKVQI VVTVLDYDKI GKNDAIGKVF VGYNSTGAEL RHWSDMLANP RRPIAQWHTL QPEEEVDAML AVKK //