SYT1_MACFA
ID SYT1_MACFA Reviewed; 419 AA.
AC Q60HC0; Q4R4H8;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Synaptotagmin-1;
DE AltName: Full=Synaptotagmin I;
DE Short=SytI;
GN Name=SYT1; ORFNames=QnpA-13075;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P21579, ECO:0000250|UniProtKB:P21707,
CC ECO:0000250|UniProtKB:P46096, ECO:0000250|UniProtKB:P48018,
CC 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; AB125207; BAD51995.1; -; mRNA.
DR EMBL; AB169916; BAE01997.1; -; mRNA.
DR RefSeq; NP_001271971.1; NM_001285042.1.
DR RefSeq; XP_015286111.1; XM_015430625.1.
DR RefSeq; XP_015286112.1; XM_015430626.1.
DR AlphaFoldDB; Q60HC0; -.
DR SMR; Q60HC0; -.
DR STRING; 9541.XP_005571675.1; -.
DR Ensembl; ENSMFAT00000100771; ENSMFAP00000056158; ENSMFAG00000003495.
DR GeneID; 101865424; -.
DR KEGG; mcf:101865424; -.
DR CTD; 6857; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000155394; -.
DR Proteomes; UP000233100; Chromosome 11.
DR Bgee; ENSMFAG00000003495; Expressed in frontal cortex and 8 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031045; C:dense core granule; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061891; F:calcium ion sensor activity; IEA:Ensembl.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0098746; P:fast, calcium ion-dependent exocytosis of neurotransmitter; IEA:Ensembl.
DR GO; GO:1903235; P:positive regulation of calcium ion-dependent exocytosis of neurotransmitter; ISS:UniProtKB.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IEA:Ensembl.
DR GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0071911; P:synchronous neurotransmitter secretion; IEA:Ensembl.
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; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..419
FT /note="Synaptotagmin-1"
FT /id="PRO_0000183937"
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..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 139..258
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 270..403
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 108..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..379
FT /note="Phospholipid binding"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 234
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="2"
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 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 126
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21579"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46096"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46096"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT MOD_RES 342
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 419 AA; 47261 MW; 146FA2B8897EADDB CRC64;
MVSESHHEAL AAPPVTTVAT VLPSNATEPA SPGEGKEDAF SKLKEKFMNE LHKIPLPPWA
LIAIAIVAVL LVLTCCFCIC KKCLFKKKNK KKGKEKGGKN AINMKDVKDL GKTMKDQDDD
AETGLTDGEE KEEPKEEEKL GKLQYSLDYD FQNNQLLVGI IQAAELPALD MGGTSDPYVK
VFLLPDKKKK FETKVHRKTL NPVFNEQFTF KVPYSELGGK TLVMAVYDFD RFSKHDIIGE
FKVPMNTVDF GHVTEEWRDL QSAEKEEQEK LGDICFSLRY VPTAGKLTVV ILEAKNLKKM
DVGGLSDPYV KIHLMQNGKR LKKKKTTIKK NTLNPYYNES FSFEVPFEQI QKVQVVVTVL
DYDKIGKNDA IGKVFVGYNS TGAELRHWSD MLANPRRPIA QWHTLQVEEE VDAMLAVKK
