SYT10_RAT
ID SYT10_RAT Reviewed; 523 AA.
AC O08625; Q925B8;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Synaptotagmin-10;
DE AltName: Full=Synaptotagmin X;
DE Short=SytX;
GN Name=Syt10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shin O.-H., Suedhof T.C.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-498.
RC STRAIN=Sprague-Dawley;
RX PubMed=9122248; DOI=10.1073/pnas.94.6.2638;
RA Babity J.M., Armstrong J.N., Plumier J.C., Currie R.W., Robertson H.A.;
RT "A novel seizure-induced synaptotagmin gene identified by differential
RT display.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2638-2641(1997).
RN [3]
RP COFACTOR, AND DOMAIN.
RX PubMed=11823420; DOI=10.1093/emboj/21.3.270;
RA Sugita S., Shin O.H., Han W., Lao Y., Suedhof T.C.;
RT "Synaptotagmins form a hierarchy of exocytotic Ca(2+) sensors with distinct
RT Ca(2+) affinities.";
RL EMBO J. 21:270-280(2002).
RN [4]
RP FUNCTION.
RX PubMed=18508778; DOI=10.1074/jbc.m709628200;
RA Bhalla A., Chicka M.C., Chapman E.R.;
RT "Analysis of the synaptotagmin family during reconstituted membrane fusion.
RT Uncovering a class of inhibitory isoforms.";
RL J. Biol. Chem. 283:21799-21807(2008).
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. Exocytosis of IGF1 is required for sensory perception
CC of smell. Not involved in Ca(2+)-dependent synaptic vesicle exocytosis
CC (By similarity). Acts through Ca(2+) and phospholipid binding to the C2
CC domain: Ca(2+) induces binding of the C2-domains to phospholipid
CC membranes and to assembled SNARE-complexes; both actions contribute to
CC triggering exocytosis (PubMed:18508778). {ECO:0000250|UniProtKB:Q9R0N4,
CC ECO:0000269|PubMed:18508778}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:11823420};
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. Can also
CC form heterodimers with SYT3, SYT6, SYT7 and SYT9.
CC {ECO:0000250|UniProtKB:Q9R0N4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250|UniProtKB:Q9R0N4}; Single-pass membrane protein
CC {ECO:0000255}. Note=Localizes to neuronal vesicles containing IGF1 that
CC are not enriched at synapses. Does not colocalize with synaptic
CC vesicles or with the Golgi apparatus. {ECO:0000250|UniProtKB:Q9R0N4}.
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:0000269|PubMed:11823420}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AF375463; AAK56958.1; -; mRNA.
DR EMBL; U85513; AAB51686.1; -; mRNA.
DR PIR; PC6300; PC6300.
DR RefSeq; NP_113854.1; NM_031666.1.
DR AlphaFoldDB; O08625; -.
DR SMR; O08625; -.
DR STRING; 10116.ENSRNOP00000019406; -.
DR PaxDb; O08625; -.
DR ABCD; O08625; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000098923; ENSRNOP00000091005; ENSRNOG00000014296.
DR GeneID; 60567; -.
DR KEGG; rno:60567; -.
DR CTD; 341359; -.
DR RGD; 62041; Syt10.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000158899; -.
DR HOGENOM; CLU_023008_8_3_1; -.
DR InParanoid; O08625; -.
DR OMA; IWKDIHC; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; O08625; -.
DR TreeFam; TF315600; -.
DR PRO; PR:O08625; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000014296; Expressed in brain and 5 other tissues.
DR Genevisible; O08625; RN.
DR GO; GO:0070382; C:exocytic vesicle; ISS: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; ISS: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; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; ISO:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0007608; P:sensory perception of smell; ISS: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 2: Evidence at transcript 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_0000183968"
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:0000250|UniProtKB:Q9R0N4"
FT CONFLICT 263
FT /note="F -> S (in Ref. 2; AAB51686)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="I -> M (in Ref. 2; AAB51686)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 59011 MW; 48F42A2D19517A3B CRC64;
MSFRKEDGVS SLCQKALHII TELCFAGQVE WDKCSGIFPA DRSGQGGGGT DISVSLLAVV
VSFCGLALLV VSLFVFWKLC WPCWKSKLVA PNVSTLPQSI SSAPTEVFET EEKKEVEENE
KPAPKAIEPA IKISHTSPDI PAEVQTALKE HLIKHARVQR QTTDPTSSSR HNSFRRHLPR
QMNVSSVDFS MGTEPVLQRG 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
