SYT17_HUMAN
ID SYT17_HUMAN Reviewed; 474 AA.
AC Q9BSW7; O43330; Q9NZ18;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Synaptotagmin-17;
DE AltName: Full=Protein B/K;
DE AltName: Full=Synaptotagmin XVII;
DE Short=SytXVII;
GN Name=SYT17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16672768; DOI=10.1038/emm.2006.18;
RA Chin H., Choi S.-H., Jang Y.-S., Cho S.-M., Kim H.-S., Lee J.-H.,
RA Jeong S.-W., Kim I.-K., Kim G.J., Kwon O.-J.;
RT "Protein kinase A-dependent phosphorylation of B/K protein.";
RL Exp. Mol. Med. 38:144-152(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 114-474.
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
RA Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y.,
RA Yoon T.J.;
RT "SYT14L, especially its C2 domain, is involved in regulating melanocyte
RT differentiation.";
RL J. Dermatol. Sci. 72:246-251(2013).
RN [6]
RP STRUCTURE BY NMR OF 181-315.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first C2 domain from human B/K protein.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Plays a role in dendrite formation by melanocytes
CC (PubMed:23999003). {ECO:0000269|PubMed:23999003}.
CC -!- INTERACTION:
CC Q9BSW7; Q96MA6: AK8; NbExp=3; IntAct=EBI-745392, EBI-8466265;
CC Q9BSW7; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-745392, EBI-2548012;
CC Q9BSW7; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-745392, EBI-11524851;
CC Q9BSW7; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-745392, EBI-10171570;
CC Q9BSW7; Q9NPC3: CCNB1IP1; NbExp=3; IntAct=EBI-745392, EBI-745269;
CC Q9BSW7; Q96MT8: CEP63; NbExp=3; IntAct=EBI-745392, EBI-741977;
CC Q9BSW7; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-745392, EBI-739624;
CC Q9BSW7; Q9BY43: CHMP4A; NbExp=6; IntAct=EBI-745392, EBI-747981;
CC Q9BSW7; Q9BY43-2: CHMP4A; NbExp=3; IntAct=EBI-745392, EBI-12178895;
CC Q9BSW7; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-745392, EBI-3866319;
CC Q9BSW7; O75140-2: DEPDC5; NbExp=3; IntAct=EBI-745392, EBI-12366971;
CC Q9BSW7; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-745392, EBI-742102;
CC Q9BSW7; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-745392, EBI-10175124;
CC Q9BSW7; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-745392, EBI-10172181;
CC Q9BSW7; Q96NE9-2: FRMD6; NbExp=3; IntAct=EBI-745392, EBI-13213391;
CC Q9BSW7; Q08379: GOLGA2; NbExp=3; IntAct=EBI-745392, EBI-618309;
CC Q9BSW7; Q9NYA3: GOLGA6A; NbExp=5; IntAct=EBI-745392, EBI-11163335;
CC Q9BSW7; O00291: HIP1; NbExp=3; IntAct=EBI-745392, EBI-473886;
CC Q9BSW7; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-745392, EBI-10961706;
CC Q9BSW7; Q13422: IKZF1; NbExp=3; IntAct=EBI-745392, EBI-745305;
CC Q9BSW7; Q9UK45: LSM7; NbExp=3; IntAct=EBI-745392, EBI-348372;
CC Q9BSW7; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-745392, EBI-1216080;
CC Q9BSW7; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-745392, EBI-741037;
CC Q9BSW7; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-745392, EBI-742610;
CC Q9BSW7; Q3KP22-3: MAJIN; NbExp=3; IntAct=EBI-745392, EBI-18015780;
CC Q9BSW7; P23508: MCC; NbExp=3; IntAct=EBI-745392, EBI-307531;
CC Q9BSW7; P50221: MEOX1; NbExp=3; IntAct=EBI-745392, EBI-2864512;
CC Q9BSW7; P50222: MEOX2; NbExp=3; IntAct=EBI-745392, EBI-748397;
CC Q9BSW7; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-745392, EBI-16439278;
CC Q9BSW7; Q9UJV3-2: MID2; NbExp=10; IntAct=EBI-745392, EBI-10172526;
CC Q9BSW7; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-745392, EBI-740897;
CC Q9BSW7; Q99471: PFDN5; NbExp=3; IntAct=EBI-745392, EBI-357275;
CC Q9BSW7; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-745392, EBI-14066006;
CC Q9BSW7; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-745392, EBI-79165;
CC Q9BSW7; Q8WVV4-1: POF1B; NbExp=3; IntAct=EBI-745392, EBI-11986735;
CC Q9BSW7; Q59EK9: RUNDC3A; NbExp=3; IntAct=EBI-745392, EBI-747225;
CC Q9BSW7; Q9H190: SDCBP2; NbExp=3; IntAct=EBI-745392, EBI-742426;
CC Q9BSW7; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-745392, EBI-12938570;
CC Q9BSW7; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-745392, EBI-2212028;
CC Q9BSW7; Q12933: TRAF2; NbExp=6; IntAct=EBI-745392, EBI-355744;
CC Q9BSW7; P14373: TRIM27; NbExp=3; IntAct=EBI-745392, EBI-719493;
CC Q9BSW7; Q99598: TSNAX; NbExp=3; IntAct=EBI-745392, EBI-742638;
CC Q9BSW7; Q9Y2B5: VPS9D1; NbExp=3; IntAct=EBI-745392, EBI-9031083;
CC Q9BSW7; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-745392, EBI-11962468;
CC Q9BSW7; Q96LX8: ZNF597; NbExp=3; IntAct=EBI-745392, EBI-9091553;
CC Q9BSW7; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-745392, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in brain (frontal and temporal
CC lobes, hippocampus, hypothalamus, amygdala, substantia nigra, and
CC pituitary), kidney, and prostate. Expressed in fetal brain, kidney and
CC lung (PubMed:16672768). Expressed in melanocytes (PubMed:23999003).
CC {ECO:0000269|PubMed:16672768, ECO:0000269|PubMed:23999003}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AF220560; AAF37825.1; -; mRNA.
DR EMBL; CH471186; EAW50274.1; -; Genomic_DNA.
DR EMBL; BC004518; AAH04518.1; -; mRNA.
DR EMBL; AC003003; AAC05436.1; -; Genomic_DNA.
DR CCDS; CCDS10575.1; -.
DR RefSeq; NP_057608.2; NM_016524.3.
DR PDB; 2ENP; NMR; -; A=181-315.
DR PDBsum; 2ENP; -.
DR AlphaFoldDB; Q9BSW7; -.
DR SMR; Q9BSW7; -.
DR BioGRID; 119717; 61.
DR IntAct; Q9BSW7; 50.
DR STRING; 9606.ENSP00000347538; -.
DR iPTMnet; Q9BSW7; -.
DR PhosphoSitePlus; Q9BSW7; -.
DR BioMuta; SYT17; -.
DR DMDM; 74752317; -.
DR MassIVE; Q9BSW7; -.
DR MaxQB; Q9BSW7; -.
DR PaxDb; Q9BSW7; -.
DR PeptideAtlas; Q9BSW7; -.
DR PRIDE; Q9BSW7; -.
DR ProteomicsDB; 78932; -.
DR Antibodypedia; 25349; 148 antibodies from 22 providers.
DR DNASU; 51760; -.
DR Ensembl; ENST00000355377.7; ENSP00000347538.2; ENSG00000103528.17.
DR GeneID; 51760; -.
DR KEGG; hsa:51760; -.
DR MANE-Select; ENST00000355377.7; ENSP00000347538.2; NM_016524.4; NP_057608.2.
DR UCSC; uc002dfw.4; human.
DR CTD; 51760; -.
DR DisGeNET; 51760; -.
DR GeneCards; SYT17; -.
DR HGNC; HGNC:24119; SYT17.
DR HPA; ENSG00000103528; Tissue enhanced (brain, parathyroid gland).
DR neXtProt; NX_Q9BSW7; -.
DR OpenTargets; ENSG00000103528; -.
DR PharmGKB; PA142670841; -.
DR VEuPathDB; HostDB:ENSG00000103528; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000158939; -.
DR InParanoid; Q9BSW7; -.
DR OMA; LIPSSQX; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q9BSW7; -.
DR TreeFam; TF315600; -.
DR PathwayCommons; Q9BSW7; -.
DR SignaLink; Q9BSW7; -.
DR BioGRID-ORCS; 51760; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; SYT17; human.
DR EvolutionaryTrace; Q9BSW7; -.
DR GenomeRNAi; 51760; -.
DR Pharos; Q9BSW7; Tbio.
DR PRO; PR:Q9BSW7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BSW7; protein.
DR Bgee; ENSG00000103528; Expressed in middle temporal gyrus and 179 other tissues.
DR ExpressionAtlas; Q9BSW7; baseline and differential.
DR Genevisible; Q9BSW7; HS.
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; IEA:Ensembl.
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; IDA:UniProtKB.
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 3D-structure; Differentiation; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..474
FT /note="Synaptotagmin-17"
FT /id="PRO_0000311936"
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"
FT CONFLICT 66
FT /note="S -> G (in Ref. 1; AAF37825)"
FT /evidence="ECO:0000305"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:2ENP"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:2ENP"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:2ENP"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:2ENP"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:2ENP"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:2ENP"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:2ENP"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:2ENP"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:2ENP"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2ENP"
SQ SEQUENCE 474 AA; 53849 MW; F5D2E86665BCEC8C CRC64;
MAYIQLEPLN EGFLSRISGL LLCRWTCRHC CQKCYESSCC QSSEDEVEIL GPFPAQTPPW
LMASRSSDKD GDSVHTASEV PLTPRTNSPD GRRSSSDTSK STYSLTRRIS SLESRRPSSP
LIDIKPIEFG VLSAKKEPIQ PSVLRRTYNP DDYFRKFEPH LYSLDSNSDD 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 SSGPSETNHW RRMLNTHRTA VEQWHSLRSR AECDRVSPAS LEVT
