ID   SYT13_RAT               Reviewed;         426 AA.
AC   Q925B5; Q9ERD5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Synaptotagmin-13;
DE   AltName: Full=Synaptotagmin XIII;
DE            Short=SytXIII;
GN   Name=Syt13;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=11211934; DOI=10.1078/0171-9335-00133;
RA   von Poser C., Suedhof T.C.;
RT   "Synaptotagmin 13: structure and expression of a novel synaptotagmin.";
RL   Eur. J. Cell Biol. 80:41-47(2001).
CC   -!- FUNCTION: May be involved in transport vesicle docking to the plasma
CC       membrane. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NRXN1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, spleen, kidney and testis.
CC       {ECO:0000269|PubMed:11211934}.
CC   -!- DOMAIN: The first C2 domain/C2A does not mediate Ca(2+)-dependent
CC       phospholipid binding. {ECO:0000250}.
CC   -!- DOMAIN: The second C2 domain/C2B domain binds phospholipids regardless
CC       of whether calcium is present. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR   EMBL; AF313453; AAG30575.1; -; mRNA.
DR   EMBL; AF375466; AAK56961.1; -; mRNA.
DR   RefSeq; NP_110466.2; NM_030839.3.
DR   AlphaFoldDB; Q925B5; -.
DR   SMR; Q925B5; -.
DR   BioGRID; 249494; 1.
DR   STRING; 10116.ENSRNOP00000011459; -.
DR   iPTMnet; Q925B5; -.
DR   PhosphoSitePlus; Q925B5; -.
DR   PaxDb; Q925B5; -.
DR   GeneID; 80977; -.
DR   KEGG; rno:80977; -.
DR   UCSC; RGD:621877; rat.
DR   CTD; 57586; -.
DR   RGD; 621877; Syt13.
DR   eggNOG; KOG1028; Eukaryota.
DR   InParanoid; Q925B5; -.
DR   OrthoDB; 925064at2759; -.
DR   PhylomeDB; Q925B5; -.
DR   TreeFam; TF315600; -.
DR   PRO; PR:Q925B5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; 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:0006906; P:vesicle fusion; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
DR   Gene3D; 2.60.40.150; -; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR028692; SYT13.
DR   PANTHER; PTHR10024:SF250; PTHR10024:SF250; 1.
DR   Pfam; PF00168; C2; 2.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; SSF49562; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..426
FT                   /note="Synaptotagmin-13"
FT                   /id="PRO_0000183977"
FT   TOPO_DOM        1..6
FT                   /note="Vesicular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..426
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          158..275
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          287..422
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   CONFLICT        226
FT                   /note="T -> A (in Ref. 1; AAG30575)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  46881 MW;  84048947BF2AB65B CRC64;
     MVLSVPVIAL GATLGTATSI LALCGVTCLC RHMHPKKGLL PRDREPDPEK ARPGVLQAAQ
     QFNVKKSTEP VQPRPLLKFP DIYGPRPAVT APEVINYADY TLGTTEESAA PASPQAQSDS
     RLKRQVTEEL FILPQNGVVE DVCVMETWNP EKAASWNQAP KLHFRLDYDQ KKAELFVTSL
     EAVTSDHEGG CDCYIQGSVA VKTGSVEAQT ALKKRQLHTT WEEGLTLPLG EEELPTATLT
     LTLRTCDRFS RHSVIGELRL GLNGASVPLG TAQWGELKTT AKEPSAGTGE VLLSISYLPA
     ANRLLVVLIK AKNLHSNQSK ELLGKDVSVK VTLKHQAQKL KKKQTKRAKH KINPVWNEMI
     MFELPDDLLQ ASSVELEVLG QGEEGPSCEL GRCSLGLHAS GSERSHWEEM LKNPRRQIAM
     WHQLHL