SYT5_MOUSE
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 03-AUG-2022, entry version 181.
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;
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: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}.
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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; 3.
DR IntAct; Q9R0N5; 2.
DR STRING; 10090.ENSMUSP00000070322; -.
DR iPTMnet; Q9R0N5; -.
DR PhosphoSitePlus; Q9R0N5; -.
DR SwissPalm; Q9R0N5; -.
DR MaxQB; Q9R0N5; -.
DR PaxDb; Q9R0N5; -.
DR PeptideAtlas; Q9R0N5; -.
DR PRIDE; Q9R0N5; -.
DR ProteomicsDB; 263194; -.
DR Antibodypedia; 2420; 216 antibodies from 33 providers.
DR Ensembl; ENSMUST00000065957; ENSMUSP00000070322; ENSMUSG00000004961.
DR UCSC; uc009exy.1; mouse.
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; 925064at2759; -.
DR PhylomeDB; Q9R0N5; -.
DR TreeFam; TF315600; -.
DR BioGRID-ORCS; 53420; 2 hits in 74 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 105 other tissues.
DR ExpressionAtlas; Q9R0N5; baseline and differential.
DR Genevisible; Q9R0N5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0099066; C:integral component of neuronal dense core vesicle membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
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: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: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 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; IPR028689; SYT5.
DR PANTHER; PTHR10024:SF282; PTHR10024:SF282; 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; 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
