SYT17_MOUSE
ID SYT17_MOUSE Reviewed; 470 AA.
AC Q920M7; Q3UXZ2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11716773; DOI=10.1042/0264-6021:3600441;
RA Fukuda M., Mikoshiba K.;
RT "The N-terminal cysteine cluster is essential for membrane targeting of B/K
RT protein.";
RL Biochem. J. 360:441-448(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-470.
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-115, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in dendrite formation by melanocytes.
CC {ECO:0000250|UniProtKB:Q9BSW7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11716773};
CC Peripheral membrane protein {ECO:0000269|PubMed:11716773}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AB069667; BAB69676.1; -; mRNA.
DR EMBL; AK135098; BAE22421.1; -; mRNA.
DR CCDS; CCDS40103.1; -.
DR RefSeq; NP_619590.1; NM_138649.1.
DR AlphaFoldDB; Q920M7; -.
DR SMR; Q920M7; -.
DR BioGRID; 225262; 2.
DR STRING; 10090.ENSMUSP00000080284; -.
DR iPTMnet; Q920M7; -.
DR PhosphoSitePlus; Q920M7; -.
DR SwissPalm; Q920M7; -.
DR PaxDb; Q920M7; -.
DR PRIDE; Q920M7; -.
DR ProteomicsDB; 253444; -.
DR Antibodypedia; 25349; 148 antibodies from 22 providers.
DR Ensembl; ENSMUST00000081574; ENSMUSP00000080284; ENSMUSG00000058420.
DR GeneID; 110058; -.
DR KEGG; mmu:110058; -.
DR UCSC; uc009jjt.1; mouse.
DR CTD; 51760; -.
DR MGI; MGI:104966; Syt17.
DR VEuPathDB; HostDB:ENSMUSG00000058420; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000158939; -.
DR HOGENOM; CLU_023008_9_0_1; -.
DR InParanoid; Q920M7; -.
DR OMA; LIPSSQX; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q920M7; -.
DR TreeFam; TF315600; -.
DR BioGRID-ORCS; 110058; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q920M7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q920M7; protein.
DR Bgee; ENSMUSG00000058420; Expressed in subiculum and 136 other tissues.
DR ExpressionAtlas; Q920M7; baseline and differential.
DR Genevisible; Q920M7; MM.
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; IDA:MGI.
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:MGI.
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..470
FT /note="Synaptotagmin-17"
FT /id="PRO_0000311937"
FT DOMAIN 180..306
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 317..451
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 75..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 2..7
FT /note="LEPLNE -> PPQWPQ (in Ref. 2; BAE22421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 53293 MW; 7F3C3036901D9D1C CRC64;
MLEPLNEGLL SRISDVLLCG WTCQHCCQRC YESSCCQSSE DEVEILGPFP AQTPPWLMAS
RSNDKDGDSV HTASDVPLTP RTNSPDGRRS SSDTSKSTYS LTRRISSLDS RRPSSPLIDI
KPVEFGVLSA KKESIQPSVL RRTYTPDDYF RKFEPRLYSL DSNLDDVDSL TDEEIMSKYQ
LGMLHFSTQY DLLHNHLTVR VIEARDLPPP ISHDGSRQDM AHSNPYVKIC LLPDQKNSKQ
TGVKRKTQKP VFEERYTFEI PFLEAQRRTL LLTVVDFDKF SRHCVIGKVA VPLCEVDLVK
GGHWWKALIP SSQNEVELGE LLLSLNYLPS AGRLNVDIIR AKQLLQTDVS QGSDPFVKIQ
LVHGLKLVKT KKTSFLRGTI DPFYNESFSF KVPQEELENA SLVFTVFGHN MKSSNDFIGR
IVIGQYSSGP SESNHWRRML NTHRTAVEQW HSLRSRAECD RVSPASLEVT
