SYT10_HUMAN
ID SYT10_HUMAN Reviewed; 523 AA.
AC Q6XYQ8; Q495U2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Synaptotagmin-10;
DE AltName: Full=Synaptotagmin X;
DE Short=SytX;
GN Name=SYT10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=14756426; DOI=10.1080/10425170310001608407;
RA Zhao E., Li Y., Fu X., Zeng L., Zeng H., Jin W., Chen J., Yin G., Qian J.,
RA Ying K., Xie Y., Zhao R.C., Mao Y.;
RT "Cloning and characterization of human synaptotagmin 10 gene.";
RL DNA Seq. 14:393-398(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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|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 -!- TISSUE SPECIFICITY: Expressed only in pancreas, lung and kidney.
CC {ECO:0000269|PubMed:14756426}.
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}.
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; AY198413; AAP37477.1; -; mRNA.
DR EMBL; BC101024; AAI01025.1; -; mRNA.
DR CCDS; CCDS8732.1; -.
DR RefSeq; NP_945343.1; NM_198992.3.
DR AlphaFoldDB; Q6XYQ8; -.
DR SMR; Q6XYQ8; -.
DR BioGRID; 131131; 6.
DR IntAct; Q6XYQ8; 2.
DR STRING; 9606.ENSP00000228567; -.
DR iPTMnet; Q6XYQ8; -.
DR PhosphoSitePlus; Q6XYQ8; -.
DR BioMuta; SYT10; -.
DR DMDM; 52783447; -.
DR jPOST; Q6XYQ8; -.
DR MassIVE; Q6XYQ8; -.
DR MaxQB; Q6XYQ8; -.
DR PaxDb; Q6XYQ8; -.
DR PeptideAtlas; Q6XYQ8; -.
DR PRIDE; Q6XYQ8; -.
DR ProteomicsDB; 67825; -.
DR Antibodypedia; 67234; 168 antibodies from 27 providers.
DR DNASU; 341359; -.
DR Ensembl; ENST00000228567.7; ENSP00000228567.3; ENSG00000110975.8.
DR GeneID; 341359; -.
DR KEGG; hsa:341359; -.
DR MANE-Select; ENST00000228567.7; ENSP00000228567.3; NM_198992.4; NP_945343.1.
DR UCSC; uc001rll.2; human.
DR CTD; 341359; -.
DR DisGeNET; 341359; -.
DR GeneCards; SYT10; -.
DR HGNC; HGNC:19266; SYT10.
DR HPA; ENSG00000110975; Group enriched (brain, fallopian tube).
DR neXtProt; NX_Q6XYQ8; -.
DR OpenTargets; ENSG00000110975; -.
DR PharmGKB; PA134866255; -.
DR VEuPathDB; HostDB:ENSG00000110975; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000158899; -.
DR HOGENOM; CLU_023008_8_3_1; -.
DR InParanoid; Q6XYQ8; -.
DR OMA; IWKDIHC; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q6XYQ8; -.
DR TreeFam; TF315600; -.
DR PathwayCommons; Q6XYQ8; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q6XYQ8; -.
DR BioGRID-ORCS; 341359; 4 hits in 1074 CRISPR screens.
DR GenomeRNAi; 341359; -.
DR Pharos; Q6XYQ8; Tbio.
DR PRO; PR:Q6XYQ8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6XYQ8; protein.
DR Bgee; ENSG00000110975; Expressed in sural nerve and 72 other tissues.
DR ExpressionAtlas; Q6XYQ8; baseline and differential.
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:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
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; IBA:GO_Central.
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_0000183965"
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 VARIANT 172
FT /note="S -> I (in dbSNP:rs12317722)"
FT /id="VAR_059826"
FT VARIANT 420
FT /note="T -> S (in dbSNP:rs35190376)"
FT /id="VAR_034529"
FT VARIANT 488
FT /note="H -> P (in dbSNP:rs34190017)"
FT /id="VAR_034530"
FT VARIANT 505
FT /note="A -> V (in dbSNP:rs34361405)"
FT /id="VAR_034531"
SQ SEQUENCE 523 AA; 59127 MW; D5A10D9A2BA9BF62 CRC64;
MSFHKEDGVN SLCQKALHIV TELCFAGQVE WEKCSGIFPR DRGSQGGSST DISVSLLAVV
VSFCGLALLV VSLFVFWKLC WPCWKSKPVT SNITTLPQSI SSAPTEVFET EEKKEIKENE
KPAVKAIEPA IKISHTSPDI PAEVQTALKE HLIKHARVQR QITEPTSSTR HSSFRRHLPR
QMQVSSVDFS MGTEPVLQRG ETTTSIGRIK PELYKQKSVD SEGNQNEDVK 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
