SYT10_MOUSE
ID SYT10_MOUSE Reviewed; 523 AA.
AC Q9R0N4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Synaptotagmin-10 {ECO:0000305};
DE AltName: Full=Synaptotagmin X {ECO:0000303|PubMed:10531343};
DE Short=SytX {ECO:0000303|PubMed:10531343};
GN Name=Syt10 {ECO:0000312|MGI:MGI:1859546};
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 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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-136, 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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-268; ASP-320; ASP-322; ASP-400; ASP-454 AND ASP-456.
RX PubMed=21496647; DOI=10.1016/j.cell.2011.03.034;
RA Cao P., Maximov A., Suedhof T.C.;
RT "Activity-dependent IGF-1 exocytosis is controlled by the Ca(2+)-sensor
RT synaptotagmin-10.";
RL Cell 145:300-311(2011).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=23345244; DOI=10.1523/jneurosci.4087-12.2013;
RA Cao P., Yang X., Suedhof T.C.;
RT "Complexin activates exocytosis of distinct secretory vesicles controlled
RT by different synaptotagmins.";
RL J. Neurosci. 33:1714-1727(2013).
CC -!- FUNCTION: Ca(2+) sensor specifically required for the Ca(2+)-dependent
CC exocytosis of secretory vesicles containing IGF1 in neurons of the
CC olfactory bulb (PubMed:21496647). Exocytosis of IGF1 is required for
CC sensory perception of smell (PubMed:21496647). Not involved in Ca(2+)-
CC dependent synaptic vesicle exocytosis (PubMed:21496647). Acts through
CC Ca(2+) and phospholipid binding to the C2 domain: Ca(2+) induces
CC binding of the C2-domains to phospholipid membranes and to assembled
CC SNARE-complexes; both actions contribute to triggering exocytosis (By
CC similarity). {ECO:0000250|UniProtKB:O08625,
CC ECO:0000269|PubMed:21496647}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000305|PubMed:21496647};
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 SYT9 (PubMed:10531343, PubMed:10531344, PubMed:10871604).
CC {ECO:0000269|PubMed:10531343, ECO:0000269|PubMed:10531344,
CC ECO:0000269|PubMed:10871604}.
CC -!- INTERACTION:
CC Q9R0N4; Q9R0N4: Syt10; NbExp=2; IntAct=EBI-5239459, EBI-5239459;
CC Q9R0N4; O35681: Syt3; NbExp=2; IntAct=EBI-5239459, EBI-457995;
CC Q9R0N4; Q9R0N8: Syt6; NbExp=2; IntAct=EBI-5239459, EBI-5239378;
CC Q9R0N4; Q9R0N9: Syt9; NbExp=2; IntAct=EBI-5239459, EBI-458006;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:21496647, ECO:0000269|PubMed:23345244}; Single-pass
CC membrane protein {ECO:0000255}. Note=Localizes to neuronal vesicles
CC containing IGF1 that are not enriched at synapses (PubMed:21496647,
CC PubMed:23345244). Does not colocalize with synaptic vesicles or with
CC the Golgi apparatus (PubMed:21496647, PubMed:23345244).
CC {ECO:0000269|PubMed:21496647, ECO:0000269|PubMed:23345244}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the olfactory bulb.
CC {ECO:0000305|PubMed:21496647}.
CC -!- DOMAIN: The cysteine motif mediates homo- or heterodimer formation via
CC formation of disulfide bonds. {ECO:0000250|UniProtKB:O35681}.
CC -!- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid
CC binding. {ECO:0000250|UniProtKB:O08625}.
CC -!- DISRUPTION PHENOTYPE: Impaired food-finding behaviors due to defects in
CC sensory perception of smell. Decreased number of olfactory bulb
CC synapses in the external plexiform layer, but not the glomerular layer,
CC of the olfactory bulb. The size and dendritic arborization of olfactory
CC bulb neurons are decreased, but not the synapse density per dendritic
CC length. Defects are due to impaired exocytosis of IGF1 in neurons of
CC the olfactory bulb. {ECO:0000269|PubMed:21496647}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AB026807; BAA85779.1; -; mRNA.
DR CCDS; CCDS27756.1; -.
DR RefSeq; NP_061273.1; NM_018803.2.
DR AlphaFoldDB; Q9R0N4; -.
DR SMR; Q9R0N4; -.
DR BioGRID; 207674; 1.
DR IntAct; Q9R0N4; 3.
DR STRING; 10090.ENSMUSP00000029441; -.
DR iPTMnet; Q9R0N4; -.
DR PhosphoSitePlus; Q9R0N4; -.
DR PaxDb; Q9R0N4; -.
DR PRIDE; Q9R0N4; -.
DR ProteomicsDB; 263192; -.
DR ABCD; Q9R0N4; 1 sequenced antibody.
DR Antibodypedia; 67234; 168 antibodies from 27 providers.
DR DNASU; 54526; -.
DR Ensembl; ENSMUST00000029441; ENSMUSP00000029441; ENSMUSG00000063260.
DR GeneID; 54526; -.
DR KEGG; mmu:54526; -.
DR UCSC; uc007xhi.2; mouse.
DR CTD; 341359; -.
DR MGI; MGI:1859546; Syt10.
DR VEuPathDB; HostDB:ENSMUSG00000063260; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000158899; -.
DR HOGENOM; CLU_023008_8_3_1; -.
DR InParanoid; Q9R0N4; -.
DR OMA; IWKDIHC; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q9R0N4; -.
DR TreeFam; TF315600; -.
DR BioGRID-ORCS; 54526; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Syt10; mouse.
DR PRO; PR:Q9R0N4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9R0N4; protein.
DR Bgee; ENSMUSG00000063260; Expressed in urethra and 46 other tissues.
DR ExpressionAtlas; Q9R0N4; baseline and differential.
DR Genevisible; Q9R0N4; MM.
DR GO; GO:0070382; C:exocytic vesicle; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IMP:UniProtKB.
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:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0000149; F:SNARE binding; IDA:ParkinsonsUK-UCL.
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:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:UniProtKB.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IMP:UniProtKB.
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:0007608; P:sensory perception of smell; IMP:UniProtKB.
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; IPR028677; SYT10.
DR PANTHER; PTHR10024:SF46; PTHR10024:SF46; 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; Exocytosis; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..523
FT /note="Synaptotagmin-10"
FT /id="PRO_0000183966"
FT TOPO_DOM 1..55
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 231..352
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 363..496
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 13..35
FT /note="Cysteine motif"
FT /evidence="ECO:0000250|UniProtKB:O35681"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 268
FT /note="D->A: Loss of function; when associated with A-320;
FT A-322; A-400; A-454 and A-456."
FT /evidence="ECO:0000269|PubMed:21496647"
FT MUTAGEN 320
FT /note="D->A: Loss of function; when associated with A-268;
FT A-322; A-400; A-454 and A-456."
FT /evidence="ECO:0000269|PubMed:21496647"
FT MUTAGEN 322
FT /note="D->A: Loss of function; when associated with A-268;
FT A-320; A-400; A-454 and A-456."
FT /evidence="ECO:0000269|PubMed:21496647"
FT MUTAGEN 400
FT /note="D->A: Loss of function; when associated with A-268;
FT A-320; A-322; A-454 and A-456."
FT /evidence="ECO:0000269|PubMed:21496647"
FT MUTAGEN 454
FT /note="D->A: Loss of function; when associated with A-268;
FT A-320; A-322; A-400 and A-456."
FT /evidence="ECO:0000269|PubMed:21496647"
FT MUTAGEN 456
FT /note="D->A: Loss of function; when associated with A-268;
FT A-320; A-322; A-400 and A-454."
FT /evidence="ECO:0000269|PubMed:21496647"
SQ SEQUENCE 523 AA; 59019 MW; 1F551F4EF75A0A9B CRC64;
MSFRKEDGVS SLCQKALHII TELCFAGQVE WDKCSGIFPA DRSGQGGGGT DISVSLLAVV
VSFCGLALLV VSLFVFWKLC WPCWKSKLVA PNLSVLPQSI SSAPTEVFET EEKKEVEENE
KPAPKAIEPA IKISHTSPDI PAEVQTALKE HLIKHARVQR QTTEPTSSSR HNSFRRHLPR
QMNVSSVDFS VGTEPILQRG ETRTSIGRIK PELYKQKSVD SEGNRKDDVK TCGKLNFALQ
YDYENELLVV KIIKALDLPA KDFTGTSDPY VKIYLLPDRK KKFQTRVHRK TLNPLFDELF
QFPVVYDQLS NRKLHFSIYD FDRFSRHDMI GEVILDNLFE VSDLSREATV WKDIHCATTE
SIDLGEIMFS LCYLPTAGRM TLTVIKCRNL KAMDITGSSD PYVKVSLMCE GRRLKKRKTT
TKKNTLNPVY NEAIIFDIPP ENVDQVSLCI AVMDYDRVGH NEVIGVCRTG LDAEGLGRDH
WNEMLAYHRK PITHWHPLLE LPGRATSFDS QGSCSSPRPP STP
