ID   SYT15_RAT               Reviewed;         422 AA.
AC   P59926;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Synaptotagmin-15;
DE   AltName: Full=Synaptotagmin XV;
DE            Short=SytXV;
GN   Name=Syt15; Synonyms=Sytxv;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Lung;
RX   PubMed=12788067; DOI=10.1016/s0006-291x(03)00911-2;
RA   Fukuda M.;
RT   "Molecular cloning and characterization of human, rat, and mouse
RT   synaptotagmin XV.";
RL   Biochem. Biophys. Res. Commun. 306:64-71(2003).
CC   -!- FUNCTION: May be involved in the trafficking and exocytosis of
CC       secretory vesicles in non-neuronal tissues. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type III
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: Neither C2 domains mediates Ca(2+)-dependent or Ca(2+)-
CC       independent phospholipid binding. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR   EMBL; AB109021; BAC76816.1; -; mRNA.
DR   AlphaFoldDB; P59926; -.
DR   SMR; P59926; -.
DR   STRING; 10116.ENSRNOP00000027475; -.
DR   PhosphoSitePlus; P59926; -.
DR   PaxDb; P59926; -.
DR   UCSC; RGD:727964; rat.
DR   RGD; 727964; Syt15.
DR   eggNOG; KOG1028; Eukaryota.
DR   InParanoid; P59926; -.
DR   PhylomeDB; P59926; -.
DR   PRO; PR:P59926; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
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:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
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:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR   GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
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: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; IPR030539; SYT15.
DR   PANTHER; PTHR10024:SF234; PTHR10024:SF234; 1.
DR   Pfam; PF00168; C2; 2.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; SSF49562; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..422
FT                   /note="Synaptotagmin-15"
FT                   /id="PRO_0000183982"
FT   TOPO_DOM        1..4
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        5..27
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          148..267
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          279..400
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ   SEQUENCE   422 AA;  47592 MW;  0D7C21F6CCBE4FEA CRC64;
     MAEQLALVIG CIIGGLLLLI GISCCLWKRL CTTFTYEELP ETADTATSSS FSKKEERPCR
     YAGIPSVRLP SVPFVVPPSH QGRDWVRLHG GDWAVAPQDP CPVPEHITCT SSPAAGQTSL
     PLCVMGSINP ELYKSSEDVS EAGFPDGCLG RLWFSVEYQQ ESERLLVDLI KAQHLQVPAE
     TCSTLVKLHL LPDKRRFLQS KAKRKTCNPQ FDESFIFQVS SKSVAQRVLK FSVYHINKQR
     KHQLLGQVLF PLKNETLAGD RHRVIWRDLE AENLEPLSEF GDLQFCLSYN DYLSRLTVVV
     LRAKGLQLQE DRGVVSVFVK VSLMNHNKFV KCKRTSAVLG SVNPVYNETF SFKADANELD
     TASLSLVVLQ ITEGDKSYPL GRVVVGPYMY TRGKELEHWN EMLRKPKELV KRWHALCRPM
     EP