ID SYT5_MOUSE Reviewed; 386 AA. AC Q9R0N5; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 189. DE RecName: Full=Synaptotagmin-5; DE AltName: Full=Synaptotagmin IX {ECO:0000303|PubMed:10531343}; DE AltName: Full=Synaptotagmin V; DE Short=SytV; GN Name=Syt5; Synonyms=Syt9 {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]. 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 TISSUE=Eye; 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 [3] RP PROTEIN SEQUENCE OF 57-61; 240-248; 256-264 AND 269-280, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11751925; DOI=10.1074/jbc.c100588200; RA Fukuda M., Kowalchyk J.A., Zhang X., Martin T.F.J., Mikoshiba K.; RT "Synaptotagmin IX regulates Ca2+-dependent secretion in PC12 cells."; RL J. Biol. Chem. 277:4601-4604(2002). 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. Regulates the Ca(2+)-dependent secretion of norepinephrine CC in PC12 cells. Required for export from the endocytic recycling CC compartment to the cell surface. {ECO:0000269|PubMed:11751925}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00041}; CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 CC domains. {ECO:0000250|UniProtKB:O00445}; CC -!- SUBUNIT: Homodimer (By similarity). Interacts with both alpha- and CC beta-tubulin (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P47861}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic CC vesicle membrane {ECO:0000269|PubMed:11751925}; Single-pass membrane CC protein {ECO:0000269|PubMed:11751925}. Recycling endosome membrane CC {ECO:0000269|PubMed:11751925}; Single-pass membrane protein CC {ECO:0000269|PubMed:11751925}. Note=In mast cells, localizes to the CC endocytic recycling compartment. CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB026806; BAA85778.1; -; mRNA. DR EMBL; BC047148; AAH47148.1; -; mRNA. DR CCDS; CCDS20738.1; -. DR RefSeq; NP_058604.1; NM_016908.2. DR RefSeq; XP_006540252.1; XM_006540189.3. DR RefSeq; XP_006540253.1; XM_006540190.3. DR AlphaFoldDB; Q9R0N5; -. DR SMR; Q9R0N5; -. DR BioGRID; 207314; 4. DR IntAct; Q9R0N5; 2. DR STRING; 10090.ENSMUSP00000070322; -. DR iPTMnet; Q9R0N5; -. DR PhosphoSitePlus; Q9R0N5; -. DR SwissPalm; Q9R0N5; -. DR MaxQB; Q9R0N5; -. DR PaxDb; 10090-ENSMUSP00000070322; -. DR PeptideAtlas; Q9R0N5; -. DR ProteomicsDB; 263194; -. DR Antibodypedia; 2420; 235 antibodies from 33 providers. DR Ensembl; ENSMUST00000065957.7; ENSMUSP00000070322.6; ENSMUSG00000004961.8. DR UCSC; uc009exy.1; mouse. DR AGR; MGI:1926368; -. DR MGI; MGI:1926368; Syt5. DR VEuPathDB; HostDB:ENSMUSG00000004961; -. DR eggNOG; KOG1028; Eukaryota. DR GeneTree; ENSGT00940000161816; -. DR HOGENOM; CLU_023008_0_1_1; -. DR InParanoid; Q9R0N5; -. DR OMA; CLCRKRC; -. DR OrthoDB; 590187at2759; -. DR PhylomeDB; Q9R0N5; -. DR TreeFam; TF315600; -. DR BioGRID-ORCS; 53420; 2 hits in 79 CRISPR screens. DR ChiTaRS; Syt5; mouse. DR PRO; PR:Q9R0N5; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q9R0N5; Protein. DR Bgee; ENSMUSG00000004961; Expressed in superior frontal gyrus and 108 other cell types or tissues. DR ExpressionAtlas; Q9R0N5; baseline and differential. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0031045; C:dense core granule; IDA:MGI. DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0099012; C:neuronal dense core vesicle membrane; IDA:SynGO. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:1990769; C:proximal neuron projection; IDA:ParkinsonsUK-UCL. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0030276; F:clathrin binding; ISO:MGI. 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:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0000149; F:SNARE binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0019905; F:syntaxin binding; ISO:MGI. DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central. DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central. 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:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central. DR Gene3D; 2.60.40.150; C2 domain; 2. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR001565; Synaptotagmin. DR PANTHER; PTHR10024; SYNAPTOTAGMIN; 1. DR PANTHER; PTHR10024:SF282; SYNAPTOTAGMIN-5; 1. DR Pfam; PF00168; C2; 2. DR PRINTS; PR00360; C2DOMAIN. DR PRINTS; PR00399; SYNAPTOTAGMN. DR SMART; SM00239; C2; 2. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR PROSITE; PS50004; C2; 2. DR Genevisible; Q9R0N5; MM. PE 1: Evidence at protein level; KW Calcium; Cytoplasmic vesicle; Direct protein sequencing; Endosome; KW Membrane; Metal-binding; Reference proteome; Repeat; Synapse; KW Transmembrane; Transmembrane helix. FT CHAIN 1..386 FT /note="Synaptotagmin-5" FT /id="PRO_0000183952" FT TOPO_DOM 1..24 FT /note="Vesicular" FT /evidence="ECO:0000255" FT TRANSMEM 25..45 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 46..386 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 108..227 FT /note="C2 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 239..372 FT /note="C2 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 138 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 139 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 139 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 145 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 197 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 197 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 198 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 199 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 199 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 199 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 202 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 270 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 276 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 330 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 332 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" SQ SEQUENCE 386 AA; 43130 MW; F884902E032082F6 CRC64; MFPEPPTLGS PAPKTPPDSS RIRQGAVPAW VLATIVLGSG LLVFSSCFCL YRKRCRRRMG KKSQAQAQVH LQEVKELGRS YIDKVQPEIE ELDRSPSMPG QQVSDKHQLG RLQYSLDYDF QTGQLLVGIL QAQGLAALDL GGSSDPYVSV YLLPDKRRRH ETKVHRQTLN PHFGETFAFK VPYVELGGRV LVMAVYDFDR FSRNDAIGEV RVPMSSVNLG RPVQAWRELQ VAPKEEQEKL GDICFSLRYV PTAGKLTVIV LEAKNLKKMD VGGLSDPYVK VHLLQGGKKV RKKKTTIKKN TLNPYYNEAF SFEVPCDQVQ KVQVELTVLD YDKLGKNEAI GRVAVGAAVG GAGLRHWADM LANPRRPIAQ WHSLRPPDRA RPIPAP //