SYT9_MOUSE
ID SYT9_MOUSE Reviewed; 491 AA.
AC Q9R0N9; Q3U0R7; Q8C280;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Synaptotagmin-9;
DE AltName: Full=Synaptotagmin IX;
DE Short=SytIX;
DE AltName: Full=Synaptotagmin V {ECO:0000303|PubMed:10531343};
GN Name=Syt9; Synonyms=Syt5 {ECO:0000303|PubMed:10531343};
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], SUBUNIT, AND DISULFIDE BOND.
RC STRAIN=ICR; TISSUE=Cerebellum;
RX PubMed=10531343; DOI=10.1074/jbc.274.44.31421;
RA Fukuda M., Kanno E., Mikoshiba K.;
RT "Conserved N-terminal cysteine motif is essential for homo- and heterodimer
RT formation of synaptotagmins III, V, VI, and X.";
RL J. Biol. Chem. 274:31421-31427(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Olfactory bulb, and Spleen;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP SUBUNIT.
RC STRAIN=ICR; TISSUE=Cerebellum;
RX PubMed=10531344; DOI=10.1074/jbc.274.44.31428;
RA Fukuda M., Mikoshiba K.;
RT "A novel alternatively spliced variant of synaptotagmin VI lacking a
RT transmembrane domain. Implications for distinct functions of the two
RT isoforms.";
RL J. Biol. Chem. 274:31428-31434(1999).
RN [6]
RP SUBUNIT.
RX PubMed=10871604; DOI=10.1074/jbc.m001376200;
RA Fukuda M., Mikoshiba K.;
RT "Distinct self-oligomerization activities of synaptotagmin family. Unique
RT calcium-dependent oligomerization properties of synaptotagmin VII.";
RL J. Biol. Chem. 275:28180-28185(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [8]
RP INTERACTION WITH DNAJC5 AND SNAP25, AND LACK OF INTERACTION WITH HSC70.
RX PubMed=20847230; DOI=10.1096/fj.09-152033;
RA Boal F., Laguerre M., Milochau A., Lang J., Scotti P.A.;
RT "A charged prominence in the linker domain of the cysteine-string protein
RT Cspalpha mediates its regulated interaction with the calcium sensor
RT synaptotagmin 9 during exocytosis.";
RL FASEB J. 25:132-143(2011).
CC -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory
CC vesicles through Ca(2+) and phospholipid binding to the C2 domain or
CC may serve as Ca(2+) sensors in the process of vesicular trafficking and
CC exocytosis.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domains. {ECO:0000250|UniProtKB:P40748};
CC -!- SUBUNIT: Homodimer; disulfide-linked via the cysteine motif
CC (PubMed:10531343). Can also form heterodimers with SYT3, SYT6, SYT7 and
CC SYT10 (PubMed:10531343, PubMed:10531344, PubMed:10871604). Interacts
CC with DNAJC5 and SNAP25, but not with HSC70 (PubMed:20847230). The
CC interaction with DNAJC5 is stimulated tenfold in presence of calcium
CC while the interaction with SNAP25 is inhibited (PubMed:20847230).
CC {ECO:0000269|PubMed:10531343, ECO:0000269|PubMed:10531344,
CC ECO:0000269|PubMed:10871604, ECO:0000269|PubMed:20847230}.
CC -!- INTERACTION:
CC Q9R0N9; Q9R0N4: Syt10; NbExp=2; IntAct=EBI-458006, EBI-5239459;
CC Q9R0N9; O35681: Syt3; NbExp=2; IntAct=EBI-458006, EBI-457995;
CC Q9R0N9; Q9R0N8: Syt6; NbExp=2; IntAct=EBI-458006, EBI-5239378;
CC Q9R0N9; Q9R0N9: Syt9; NbExp=2; IntAct=EBI-458006, EBI-458006;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane; Single-pass membrane protein.
CC -!- DOMAIN: The cysteine motif mediates homo- or heterodimer formation via
CC formation of disulfide bonds. {ECO:0000250|UniProtKB:O35681}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AB026802; BAA85774.1; -; mRNA.
DR EMBL; AK089115; BAC40759.1; -; mRNA.
DR EMBL; AK156631; BAE33784.1; -; mRNA.
DR EMBL; CH466531; EDL16861.1; -; Genomic_DNA.
DR EMBL; BC132495; AAI32496.1; -; mRNA.
DR EMBL; BC137904; AAI37905.1; -; mRNA.
DR CCDS; CCDS40078.1; -.
DR RefSeq; NP_068689.2; NM_021889.4.
DR AlphaFoldDB; Q9R0N9; -.
DR SMR; Q9R0N9; -.
DR IntAct; Q9R0N9; 4.
DR STRING; 10090.ENSMUSP00000073164; -.
DR iPTMnet; Q9R0N9; -.
DR PhosphoSitePlus; Q9R0N9; -.
DR MaxQB; Q9R0N9; -.
DR PaxDb; Q9R0N9; -.
DR PeptideAtlas; Q9R0N9; -.
DR PRIDE; Q9R0N9; -.
DR ProteomicsDB; 253448; -.
DR ABCD; Q9R0N9; 1 sequenced antibody.
DR Antibodypedia; 42311; 156 antibodies from 29 providers.
DR DNASU; 60510; -.
DR Ensembl; ENSMUST00000073459; ENSMUSP00000073164; ENSMUSG00000062542.
DR GeneID; 60510; -.
DR KEGG; mmu:60510; -.
DR UCSC; uc009jba.1; mouse.
DR CTD; 143425; -.
DR MGI; MGI:1926373; Syt9.
DR VEuPathDB; HostDB:ENSMUSG00000062542; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000155948; -.
DR HOGENOM; CLU_023008_8_3_1; -.
DR InParanoid; Q9R0N9; -.
DR OMA; NEAMVFD; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q9R0N9; -.
DR TreeFam; TF315600; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 60510; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Syt9; mouse.
DR PRO; PR:Q9R0N9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9R0N9; protein.
DR Bgee; ENSMUSG00000062542; Expressed in habenula and 145 other tissues.
DR ExpressionAtlas; Q9R0N9; baseline and differential.
DR Genevisible; Q9R0N9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031045; C:dense core granule; IDA:MGI.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0030667; C:secretory granule membrane; ISO: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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000149; F:SNARE binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IDA:SynGO.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISO:MGI.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0050796; P:regulation of insulin secretion; ISO:MGI.
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; IPR028691; SYT9.
DR PANTHER; PTHR10024:SF180; PTHR10024:SF180; 1.
DR Pfam; PF00168; C2; 2.
DR PRINTS; PR00360; C2DOMAIN.
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 Calcium; Cytoplasmic vesicle; Disulfide bond; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..491
FT /note="Synaptotagmin-9"
FT /id="PRO_0000183963"
FT TOPO_DOM 1..52
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 220..341
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 352..485
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 9..31
FT /note="Cysteine motif"
FT /evidence="ECO:0000250|UniProtKB:O35681"
FT REGION 91..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 488
FT /note="M -> L (in Ref. 1; BAA85774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 56265 MW; E08ECFD9F4D6EE14 CRC64;
MPGARDALCH QALQLLAELC ARGALEHDSC QDFIYHLRDR ARPRLRDPDI SVSLLTLVVT
ACGLALFGVS LFVSWKLCWV PWRERGLFSG SKDNNQEPLN YTDTETNEQE NSEDFLDPPT
PCPDSSMKIS HTSPDIPLST QPGGQENCAH AVRVQRQVTE PTPSARHNSI RRQLNLSNPD
FNIQQLQRQE QLTGIGRIKP ELYKQRSLDN DDGRRSNSKA CGKLNFILKY DCDLEQLIVK
IHKAVNLPAK DFSGTSDPYV KIYLLPDRKT KHQTKVHRKT LNPVFDEVFL FPVHYNDLEA
RKLHFSVYDF DRFSRHDLIG QVVVDHFFDL ADFPRECILW KDIEYVTNDN VDLGELMFSL
CYLPTAGRLT ITIIKARNLK AMDITGASDP YVKVSLMCDG RRLKKRKTST KRNTLNPVYN
EAIVFDVPPE SIDQIHLSIA VMDYDRVGHN EVIGVCQVGN EAERLGRDHW SEMLSYPRKP
IAHWHSLMEK R
