SYT1_CHICK
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 03-AUG-2022, entry version 159.
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;
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|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}.
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DR EMBL; S64957; AAB28081.1; -; mRNA.
DR PIR; I51210; I51210.
DR RefSeq; NP_990502.1; NM_205171.1.
DR RefSeq; XP_015134173.1; XM_015278687.1.
DR RefSeq; XP_015134214.1; XM_015278728.1.
DR RefSeq; XP_015134261.1; XM_015278775.1.
DR RefSeq; XP_015134330.1; XM_015278844.1.
DR AlphaFoldDB; P47191; -.
DR SMR; P47191; -.
DR STRING; 9031.ENSGALP00000042075; -.
DR PaxDb; P47191; -.
DR Ensembl; ENSGALT00000059750; ENSGALP00000056597; ENSGALG00000041094.
DR Ensembl; ENSGALT00000106562; ENSGALP00000074181; ENSGALG00000041094.
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; TELRHWM; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; P47191; -.
DR TreeFam; TF315600; -.
DR Reactome; R-GGA-210500; Glutamate 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 PRO; PR:P47191; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000041094; Expressed in brain and 8 other tissues.
DR ExpressionAtlas; P47191; 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: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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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 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; 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 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
