SY63_DIPOM
ID SY63_DIPOM Reviewed; 537 AA.
AC P24507;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Synaptotagmin-C;
DE AltName: Full=Synaptic vesicle protein O-p65-C;
GN Name=P65-C;
OS Diplobatis ommata (Ocellated electric ray) (Discopyge ommata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Narcinidae; Diplobatis.
OX NCBI_TaxID=1870830;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2054189; DOI=10.1016/0896-6273(91)90239-v;
RA Wendland B., Miller K.G., Schilling J., Scheller R.H.;
RT "Differential expression of the p65 gene family.";
RL Neuron 6:993-1007(1991).
CC -!- FUNCTION: May have a regulatory role in the membrane interactions
CC during trafficking of synaptic vesicles at the active zone of the
CC synapse. It binds acidic phospholipids with a specificity that requires
CC the presence of both an acidic head group and a diacyl backbone.
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};
CC -!- SUBUNIT: Homodimer or homotrimer (possible).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane; Single-pass membrane protein. Synapse. Note=Synaptic
CC vesicles in neurons.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; M64277; AAA49229.1; -; mRNA.
DR PIR; JH0415; JH0415.
DR AlphaFoldDB; P24507; -.
DR SMR; P24507; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IEA:InterPro.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR028682; SYT3.
DR PANTHER; PTHR10024:SF176; PTHR10024:SF176; 2.
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; Cytoplasmic vesicle; Membrane; Metal-binding; Repeat; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..537
FT /note="Synaptotagmin-C"
FT /id="PRO_0000183985"
FT TOPO_DOM 1..52
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 236..357
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 368..501
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 92..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..477
FT /note="Phospholipid binding"
FT /evidence="ECO:0000305"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 537 AA; 61301 MW; 2792F910CFBCE682 CRC64;
MSGDGEDELC RNALALVNEL CFSVRGNHNN EKCIEFSYLL RDRDRTRHIE TDISVSLLSV
IVTFCGIVLL GVSLFVSWKL CWIPWRDKGL NPQRRDSQHH PHQHLHHHHS HFTDLTVERV
DCGPEMPERS YLDLESYPES GIKLSQTSPD IPVDTSSGSK ENNIPNAHSQ QQVSAPPPAT
RFNSLPRPIP QQLSSPEFGT QADEKVEQVT SIGQIKPELY KQRSIDTEAK KHQKVNCGRI
NFMLRYTYTT EQLVVKILKA LDLPAKDANG FSDPYVKIYL LPDRKKKFQT KVHRKTLNPI
FNETFQFNVP FNELQNRKLH FSVYDFDRFS RHDLIGQVVL DNLLEFSDFS EDTTIWRDIL
EATSEKADLG EINFSLCYLP TAGRLTITII KATNLKAMDL TGFSDPYVKA SLICDERRLK
KRKTSIKKNT LNPVYNEALV FDIPNENMEH VNVIIAVMDY DCIGHNEVIG MCRVGNATDG
PGREHWNEML ANPRKPIEQW HQLIEEKVMN SYMTKSFAAG TGATKPVTIV VESPHSV
