SYT10_PONAB
ID SYT10_PONAB Reviewed; 523 AA.
AC Q5RCK6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Synaptotagmin-10;
DE AltName: Full=Synaptotagmin X;
DE Short=SytX;
GN Name=SYT10;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:O08625,
CC ECO:0000250|UniProtKB:Q9R0N4}.
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};
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:0000250|UniProtKB:O08625}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; CR858264; CAH90501.1; -; mRNA.
DR RefSeq; NP_001125263.1; NM_001131791.1.
DR AlphaFoldDB; Q5RCK6; -.
DR SMR; Q5RCK6; -.
DR STRING; 9601.ENSPPYP00000005031; -.
DR Ensembl; ENSPPYT00000005229; ENSPPYP00000005031; ENSPPYG00000004408.
DR GeneID; 100172160; -.
DR KEGG; pon:100172160; -.
DR CTD; 341359; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000158899; -.
DR InParanoid; Q5RCK6; -.
DR OrthoDB; 925064at2759; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0070382; C:exocytic vesicle; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0007268; P:chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR GO; GO:0007608; P:sensory perception of smell; ISS:UniProtKB.
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_0000183967"
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"
SQ SEQUENCE 523 AA; 59186 MW; 5A114EF76991499C CRC64;
MSFHKEDGVN SLCQKALHIV TELCFAGQVE WEKCSGIFPR DRGSQGGSST DISVSLLAVV
VSFCGLALLV VSLFVFWKLC WPCWKSKPVT SNITTLPQSI SSAPTEVFET EEKKEIKENE
KPAMKAIEPA IKISHTSPDI PAEVQTALKE HLIKHARVQR QITEPTSSSR HNSFRRHLPR
QMQVSSVDFS MGTEPVLQRG ETTTSIGRIK PELYKQKSVD SEGNQKEDVK ICGKLNFTLQ
YDYENELLVV KIIKALDLPA KDFTGTSDPY VKMYLLPDRK KKFQTRVHRK TLNPLFDETF
QFPVAYDQLS NRKLHFSVYD FDRFSRHDMI GEVILDNLFE VSDLSREATV WKDIHCATTE
SIDLGEIMFS LCYLPTAGRM TLTVIKCRNL KAMDITGSSD PYVKVSLMCE GRRLKKRKTT
TKKNTLNPVY NEAIIFDIPP ENVDQVSLSI AVMDYDRVGH NEVIGVCRTG LDAEGLGRDH
WNEMLAYHRK PITHWHPLLE LPGRATSFDS QGSCPSPKPP STP
