SYT17_XENTR
ID SYT17_XENTR Reviewed; 474 AA.
AC A4IJ05;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Synaptotagmin-17;
DE AltName: Full=Synaptotagmin XVII;
DE Short=SytXVII;
GN Name=syt17;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play 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; BC136225; AAI36226.1; -; mRNA.
DR RefSeq; NP_001096478.1; NM_001103008.1.
DR AlphaFoldDB; A4IJ05; -.
DR SMR; A4IJ05; -.
DR STRING; 8364.ENSXETP00000061793; -.
DR PaxDb; A4IJ05; -.
DR PRIDE; A4IJ05; -.
DR DNASU; 100125097; -.
DR Ensembl; ENSXETT00000066337; ENSXETP00000061793; ENSXETG00000032441.
DR GeneID; 100125097; -.
DR KEGG; xtr:100125097; -.
DR CTD; 51760; -.
DR Xenbase; XB-GENE-949409; syt17.
DR eggNOG; KOG1028; Eukaryota.
DR HOGENOM; CLU_023008_9_0_1; -.
DR InParanoid; A4IJ05; -.
DR OMA; LIPSSQX; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; A4IJ05; -.
DR TreeFam; TF315600; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000032441; Expressed in brain and 3 other tissues.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
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:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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; 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; Reference proteome; Repeat.
FT CHAIN 1..474
FT /note="Synaptotagmin-17"
FT /id="PRO_0000311940"
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 54..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 54060 MW; 6DFAB77C3AF1B3FB CRC64;
MAYIQLEPIN EGFLSKISDL LLCRWTCRNC CQKCYECSCC QSSEDEVEIL GPFPAQTPPW
LVSNRSEDKE GDSDNTTSEP PATPQDTSPD RRRSSSDTSR STYSLTRRIS SLESRRPSSP
LIDIKPIEFG ALGAKKEIVQ PTVLRKSYTP EDYFRKFEPR LYSLDSSNDD VDSLTDDEIL
TKYQLGMLHF STQYDLLHNY LNVRVIEARD LPPPISYDGS RQDMAHSNPY VKICLLPDQK
NSKQTGVKRK TQNPVFEERY TFEIQFLEAQ RRTLLLTIVD FDKFSRHCVI GKVAMPLNEV
DLVKGGHWWK AIIPSSQNEV ELGELLLSLN YLPSAGRLNV DIIRAKQLLQ TDMSQGSDPF
VKIQLVHGLK LAKTKKTSCM RGTIDPFYNE SFSFKVPQEE LENVSLVFTV YGHNMKTSND
FIGRIVIGQY ASGSPESNHW RRMLNSNRTA VEQWHSLRSR AECDRVSPAS LEVT