SYT17_RAT
ID SYT17_RAT Reviewed; 474 AA.
AC Q62807;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Synaptotagmin-17;
DE AltName: Full=Protein B/K;
DE AltName: Full=Synaptotagmin XVII;
DE Short=SytXVII;
GN Name=Syt17; Synonyms=Bk;
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 STRAIN=Sprague-Dawley; TISSUE=Brain, and Hypothalamus;
RX PubMed=8549819; DOI=10.1016/0014-5793(95)01430-6;
RA Kwon O.J., Gainer H., Wray S., Chin H.;
RT "Identification of a novel protein containing two C2 domains selectively
RT expressed in the rat brain and kidney.";
RL FEBS Lett. 378:135-139(1996).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Expressed in brain and kidney.
CC {ECO:0000269|PubMed:8549819}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; U30831; AAC52379.1; -; mRNA.
DR PIR; S68695; S68695.
DR RefSeq; NP_620204.1; NM_138849.1.
DR AlphaFoldDB; Q62807; -.
DR SMR; Q62807; -.
DR STRING; 10116.ENSRNOP00000023090; -.
DR iPTMnet; Q62807; -.
DR PhosphoSitePlus; Q62807; -.
DR SwissPalm; Q62807; -.
DR PaxDb; Q62807; -.
DR PRIDE; Q62807; -.
DR Ensembl; ENSRNOT00000023090; ENSRNOP00000023090; ENSRNOG00000017136.
DR GeneID; 192189; -.
DR KEGG; rno:192189; -.
DR UCSC; RGD:708576; rat.
DR CTD; 51760; -.
DR RGD; 708576; Syt17.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000158939; -.
DR HOGENOM; CLU_023008_9_0_1; -.
DR InParanoid; Q62807; -.
DR OMA; LIPSSQX; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q62807; -.
DR TreeFam; TF315600; -.
DR PRO; PR:Q62807; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017136; Expressed in frontal cortex and 18 other tissues.
DR ExpressionAtlas; Q62807; baseline and differential.
DR Genevisible; Q62807; RN.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
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:1903861; P:positive regulation of dendrite extension; ISO:RGD.
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 1: Evidence at protein level;
KW Differentiation; Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..474
FT /note="Synaptotagmin-17"
FT /id="PRO_0000311939"
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..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 474 AA; 53827 MW; 048ACA8CE20D3F2F CRC64;
MAYIQLEPLN EGFLSRISDV LLCGWTCQHC CQRCYESSCC QSSEDEVEIL GPFPAQTPPW
LMASRSNDKD GDSVHTASDV PLTPRTNSPD GRRSSSDTSK STYSLTRRIS SLDSRRPSSP
LIDIKPIEFG VLSAKKEPIQ PSVLRRTYTP DDYFRKFEPR LYSLDSNLDD VDSLTDEEIM
SKYQLGMLHF STQYDLLHNH LTVRVIEARD LPPPISHDGS RQDMAHSNPY VKICLLPDQK
NSKQTGVKRK TQKPVFEERY TFEIPFLEAQ RRTLLLTVVD FDKFSRHCVI GKVAVPLCEV
DLVKGGHWWK ALIPSSQNEV ELGELLLSLN YLPSAGRLNV DIIRAKQLLQ TDVSQGSDPF
VKIQLVHGLK LVKTKKTSFL RGTIDPFYNE SFSFKVPQEE LENASLVFTV FGHNMKSSND
FIGRIVIGQY SSGPSESNHW RRMLNTHRTA VEQWHSLRSR AECDRVSPAS LEVT
