SY61_DIPOM
ID SY61_DIPOM Reviewed; 427 AA.
AC P24505;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Synaptotagmin-A;
DE AltName: Full=Synaptic vesicle protein O-p65-A;
GN Name=P65-A;
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 -!- TISSUE SPECIFICITY: Forebrain, cerebellum and neuroendocrine cells.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; M64275; AAA49227.1; -; mRNA.
DR PIR; JH0413; JH0413.
DR AlphaFoldDB; P24505; -.
DR SMR; P24505; -.
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:0005544; F:calcium-dependent phospholipid binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007269; P:neurotransmitter secretion; 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; 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; Cytoplasmic vesicle; Glycoprotein; Membrane; Metal-binding;
KW Repeat; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..427
FT /note="Synaptotagmin-A"
FT /id="PRO_0000183983"
FT TOPO_DOM 1..57
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 147..266
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 278..411
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 96..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..387
FT /note="Phospholipid binding"
FT /evidence="ECO:0000305"
FT COMPBIAS 100..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
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 BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 427 AA; 47768 MW; D23F9488A8A8600A CRC64;
MKLTEAYHDA LAALPATPPL PTAVANATEA AAGSEEGKQD GFSKVKVKEK FMNELNKIPL
PPWALVAIAI VAIILGLTCC FCICKKCLLK KKNKKKGKEK GGKNAMTMKD VKEMGKSGKE
QALKDEDEDA ETGLTTDGKE EEKEDEKLGK LQFSLDYDFQ NNQLIVGIIQ AAELPALDVG
GTSDPYVKVF VLPDKKKKYE TKVHRKTLNP VFNESFIFKI PYSELGGKTL VMAVYDFDRF
SKHDVIGEAK VPMNTVDFGH VTEEWRDLQG AEKEEQEKLG DICFSLRYVP TAGKLTVVIL
EAKNLKKMDV GGLSDPYVKI HLMQNGKRLK KKKTTIKKNT LNPYYNESFS FEVPFEQIQK
VQVVVTVLDY DKIGKNDAIG KVFVGYNSTA AELRHWSDML ANPRRPIAQW HTLQPEEEVD
ATLGMKK
