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Database: UniProt
Entry: A0A3Q0TC63_AMPCI
LinkDB: A0A3Q0TC63_AMPCI
Original site: A0A3Q0TC63_AMPCI 
ID   A0A3Q0TC63_AMPCI        Unreviewed;       354 AA.
AC   A0A3Q0TC63;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Synaptotagmin {ECO:0000256|RuleBase:RU367154};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000029686.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000029686.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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       {ECO:0000256|RuleBase:RU367154}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|RuleBase:RU367154};
CC       Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC       domains. {ECO:0000256|RuleBase:RU367154};
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004160}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004160}. Cytoplasmic vesicle, secretory
CC       vesicle, chromaffin granule membrane {ECO:0000256|ARBA:ARBA00004349};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004349}.
CC       Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004254, ECO:0000256|RuleBase:RU367154}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004254,
CC       ECO:0000256|RuleBase:RU367154}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family.
CC       {ECO:0000256|ARBA:ARBA00006996, ECO:0000256|RuleBase:RU367154}.
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DR   AlphaFoldDB; A0A3Q0TC63; -.
DR   STRING; 61819.ENSACIP00000029686; -.
DR   Ensembl; ENSACIT00000030466.1; ENSACIP00000029686.1; ENSACIG00000022976.1.
DR   GeneTree; ENSGT00940000155394; -.
DR   OMA; FVPTAGK; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd08402; C2B_Synaptotagmin-1; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001565; Synaptotagmin.
DR   PANTHER; PTHR10024; SYNAPTOTAGMIN; 1.
DR   PANTHER; PTHR10024:SF239; SYNAPTOTAGMIN-1; 1.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   PROSITE; PS50004; C2; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU367154};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|RuleBase:RU367154};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Metal-binding {ECO:0000256|RuleBase:RU367154};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Synapse {ECO:0000256|RuleBase:RU367154}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..354
FT                   /note="Synaptotagmin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018685405"
FT   DOMAIN          65..193
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          205..338
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          29..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..51
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  39919 MW;  550418960FE9FC3F CRC64;
     AALCIVSLCM VLSCAVCVWK KFLKKKDKGK EKEKDKKKGK EKSKGDFDTE MDGGYNEVSC
     NTATPPPHPP QTHWPYSLFS PLHSPVIMFQ LVVGILQAAE LPAMDVGGSS DPYVKLYLLP
     DKKKKFETKV HRKTLEPNFN ETFTFKVPYT ELGGKTLVMT VYDFDRFSKH DAIGAVKIPM
     SGVDFSQSLQ EWRDLQKAEK EESERLGDIC LSLRYVPTAG KLTVVILEAK NLKKMDVGGL
     SDPYVKIHLM QNGKRLKKKK TTIKKNTLNP YYNESFSFEV PCEQIEKVQV AVTVLDYDKI
     GKNDAIGKML LGGNSTGTEQ RHWSDMLANP RRPIAQWHSL QPEDEVNALI SSKK
//
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