ID   SYT17_PONAB             Reviewed;         474 AA.
AC   Q5R8Q5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Synaptotagmin-17;
DE   AltName: Full=Synaptotagmin XVII;
DE            Short=SytXVII;
GN   Name=SYT17;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in dendrite formation by melanocytes.
CC       {ECO:0000250|UniProtKB:Q9BSW7}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR   EMBL; CR859696; CAH91855.1; -; mRNA.
DR   RefSeq; NP_001126074.1; NM_001132602.1.
DR   AlphaFoldDB; Q5R8Q5; -.
DR   SMR; Q5R8Q5; -.
DR   STRING; 9601.ENSPPYP00000008076; -.
DR   PRIDE; Q5R8Q5; -.
DR   GeneID; 100173026; -.
DR   KEGG; pon:100173026; -.
DR   CTD; 51760; -.
DR   eggNOG; KOG1028; Eukaryota.
DR   InParanoid; Q5R8Q5; -.
DR   OrthoDB; 925064at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006887; P: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; IPR014705; SYT17.
DR   PANTHER; PTHR10024:SF348; PTHR10024:SF348; 1.
DR   Pfam; PF00168; C2; 2.
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   Differentiation; Membrane; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..474
FT                   /note="Synaptotagmin-17"
FT                   /id="PRO_0000311938"
FT   DOMAIN          184..310
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          321..455
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          60..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q920M7"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q920M7"
SQ   SEQUENCE   474 AA;  53890 MW;  E0050BD485E2FAD4 CRC64;
     MAYIQLEPLN EGFLSRISDL LLCRWTCRHC CQKCYESSCC QSSEDEVEIL GPFPAQTPPW
     LMASRSSDKD GDSVHTASEV PLTPRTNSPD GRRSSSDTSK STYSLTRRIS SLESRRPSSP
     LIDIKPIEFG VLSAKKEPIQ PSVLRRTYTP DDYFRKFEPH LYSLDPNSDD VDSLTDEEIL
     SKYQLGMLHF STQYDLLHNH LTVRVIEARD LPPPISHDGS RQDMAHSNPY VKICLLPDQK
     NSKQTGVKRK TQKPVFEERY TFEIPFLEAQ RRTLLLTVVD FDKFSRHCVI GKVSVPLCEV
     DLVKGGHWWK ALIPSSQNEV ELGELLLSLN YLPSAGRLNV DVIRAKQLLQ TDVSQGSDPF
     VKIQLVHGLK LVKTKKTSFL RGTIDPFYNE SFSFKVPQEE LENASLVFTV FGHNMKSSND
     FIGRIVIGQY SSGPSESNHW RRMLNTHRTA VEQWHSLRSR AECDRVSPAS LEVT