SYT1_BOVIN
ID SYT1_BOVIN Reviewed; 422 AA.
AC P48018;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Synaptotagmin-1;
DE AltName: Full=Synaptotagmin I;
DE Short=SytI;
DE AltName: Full=p65;
GN Name=SYT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8454654; DOI=10.1016/s0021-9258(18)53322-6;
RA Davletov B., Sontag J.M., Hata Y., Petrenko A.G., Fykse E.M., Jahn R.,
RA Suedhof T.C.;
RT "Phosphorylation of synaptotagmin I by casein kinase II.";
RL J. Biol. Chem. 268:6816-6822(1993).
RN [2]
RP PROTEIN SEQUENCE OF 113-132, INTERACTION WITH CALMODULIN, AND
RP GLYCOSYLATION.
RC TISSUE=Adrenal gland;
RX PubMed=1719959; DOI=10.1042/bj2790699;
RA Tugal H.B., van Leeuwen F., Apps D.K., Haywood J., Phillips J.H.;
RT "Glycosylation and transmembrane topography of bovine chromaffin granule
RT p65.";
RL Biochem. J. 279:699-703(1991).
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 (By similarity). It
CC binds acidic phospholipids with a specificity that requires the
CC presence of both an acidic head group and a diacyl backbone. A Ca(2+)-
CC dependent interaction between synaptotagmin and putative receptors for
CC activated protein kinase C has also been reported. It can bind to at
CC least three additional proteins in a Ca(2+)-independent manner; these
CC are neurexins, syntaxin and AP2. Plays a role in dendrite formation by
CC melanocytes (By similarity). {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 (Probable). Interacts with SCAMP5 (By
CC similarity). Interacts with STON2 (By similarity). Forms a complex with
CC SV2B, syntaxin 1 and SNAP25 (By similarity). Interacts with SV2A, SV2B
CC and SV2C (By similarity). Interacts with RIMS1 (By similarity).
CC Interacts with PRRT2 (By similarity). Interacts with DNAJC5 in a
CC phosphorylation-dependent manner (By similarity). Interacts (via N-
CC terminus) with RAB3A (By similarity). Interacts with SYT12 (By
CC similarity). Interacts with calmodulin (PubMed:1719959).
CC {ECO:0000250|UniProtKB:P21579, ECO:0000250|UniProtKB:P21707,
CC ECO:0000250|UniProtKB:P46096, ECO:0000269|PubMed:1719959, 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 -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P21707}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; L05922; AAA87360.1; -; mRNA.
DR PIR; A45486; A45486.
DR RefSeq; NP_776617.1; NM_174192.3.
DR RefSeq; XP_005206087.1; XM_005206030.3.
DR AlphaFoldDB; P48018; -.
DR SMR; P48018; -.
DR CORUM; P48018; -.
DR IntAct; P48018; 1.
DR MINT; P48018; -.
DR STRING; 9913.ENSBTAP00000008338; -.
DR iPTMnet; P48018; -.
DR PaxDb; P48018; -.
DR PRIDE; P48018; -.
DR Ensembl; ENSBTAT00000072222; ENSBTAP00000065714; ENSBTAG00000034693.
DR GeneID; 281511; -.
DR KEGG; bta:281511; -.
DR CTD; 6857; -.
DR VEuPathDB; HostDB:ENSBTAG00000034693; -.
DR VGNC; VGNC:35535; SYT1.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000155394; -.
DR HOGENOM; CLU_023008_0_1_1; -.
DR InParanoid; P48018; -.
DR OMA; TELRHWM; -.
DR OrthoDB; 925064at2759; -.
DR TreeFam; TF315600; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000034693; Expressed in occipital lobe and 79 other tissues.
DR ExpressionAtlas; P48018; 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:0030136; C:clathrin-coated vesicle; IDA:AgBase.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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:1903235; P:positive regulation of calcium ion-dependent exocytosis of neurotransmitter; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Calcium; Calmodulin-binding; Cytoplasm; Cytoplasmic vesicle;
KW Differentiation; Direct protein sequencing; Glycoprotein; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..422
FT /note="Synaptotagmin-1"
FT /id="PRO_0000183935"
FT TOPO_DOM 1..57
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 142..261
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 273..406
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 113..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..382
FT /note="Phospholipid binding"
FT /evidence="ECO:0000305"
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 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
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 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 237
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="2"
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 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
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 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21579"
FT MOD_RES 230
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46096"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46096"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 75
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 76
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 83
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 422 AA; 47623 MW; C158C34DAAE456EA CRC64;
MVSESHHEAL AAPPVTTVAT VLPHNATEPA SPGEGKEDAF SKLKEKFMNE LHKIPLPPWA
LIAIAIVAVL LVLTCCFCIC KKCLFKKKNK KKGKEKGGKN AINMKDVKDL GKTMKDQALK
DDDAETGLTD GEEKEEPKEE EKLGKLQYSL DYDFQNNQLL VGIIQAAELP ALDMGGTSDP
YVKVFLLPDK KKKFETKVHR KTLNPVFNEQ FTFKVPYSEL GGKTLVMAVY DFDRFSKHDI
IGEFKVPMNT VDFGHVTEEW RDLQSAEKEE QEKLGDICFS LRYVPTAGKL TVVILEAKNL
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT IKKNTLNPYY NESFSFEVPF EQIQKVQVVV
TVLDYDKIGK NDAIGKVFVG YNSTGAELRH WSDMLANPRR PIAQWHTLQV EEEVDAMLAV
KK
