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Protein

Synaptotagmin-10

Gene

Syt10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ca2+ sensor specifically required for the Ca2+-dependent exocytosis of secretory vesicles containing IGF1 in neurons of the olfactory bulb (PubMed:21496647). Exocytosis of IGF1 is required for sensory perception of smell (PubMed:21496647). Not involved in Ca2+-dependent synaptic vesicle exocytosis (PubMed:21496647). Acts through Ca2+ and phospholipid binding to the C2 domain: Ca2+ induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity).By similarity1 Publication

Cofactori

Ca2+1 PublicationNote: Binds 3 Ca2+ ions per subunit. The ions are bound to the C2 domains.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi262 – 2621Calcium 1By similarity
Metal bindingi262 – 2621Calcium 2By similarity
Metal bindingi268 – 2681Calcium 1By similarity
Metal bindingi320 – 3201Calcium 1By similarity
Metal bindingi320 – 3201Calcium 2By similarity
Metal bindingi321 – 3211Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi322 – 3221Calcium 1By similarity
Metal bindingi322 – 3221Calcium 2By similarity
Metal bindingi322 – 3221Calcium 3By similarity
Metal bindingi325 – 3251Calcium 3By similarity
Metal bindingi328 – 3281Calcium 2By similarity
Metal bindingi328 – 3281Calcium 3By similarity

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: GO_Central
  • calcium ion binding Source: UniProtKB
  • clathrin binding Source: GO_Central
  • identical protein binding Source: IntAct
  • phosphatidylinositol-4,5-bisphosphate binding Source: ParkinsonsUK-UCL
  • phosphatidylserine binding Source: ParkinsonsUK-UCL
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: GO_Central

GO - Biological processi

  • exocytosis Source: UniProtKB-KW
  • positive regulation of calcium ion-dependent exocytosis Source: UniProtKB
  • regulation of calcium ion-dependent exocytosis Source: ParkinsonsUK-UCL
  • sensory perception of smell Source: UniProtKB
  • synaptic transmission Source: UniProtKB
  • vesicle fusion Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Exocytosis

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-10Curated
Alternative name(s):
Synaptotagmin X1 Publication
Short name:
SytX1 Publication
Gene namesi
Name:Syt10Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1859546. Syt10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5555VesicularSequence analysisAdd
BLAST
Transmembranei56 – 7621HelicalSequence analysisAdd
BLAST
Topological domaini77 – 523447CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Disruption phenotypei

Impaired food-finding behaviors due to defects in sensory perception of smell. Decreased number of olfactory bulb synapses in the external plexiform layer, but not the glomerular layer, of the olfactory bulb. The size and dendritic arborization of olfactory bulb neurons are decreased, but not the synapse density per dendritic length. Defects are due to impaired exocytosis of IGF1 in neurons of the olfactory bulb.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi268 – 2681D → A: Loss of function; when associated with A-320; A-322; A-400; A-454 and A-456. 1 Publication
Mutagenesisi320 – 3201D → A: Loss of function; when associated with A-268; A-322; A-400; A-454 and A-456. 1 Publication
Mutagenesisi322 – 3221D → A: Loss of function; when associated with A-268; A-320; A-400; A-454 and A-456. 1 Publication
Mutagenesisi400 – 4001D → A: Loss of function; when associated with A-268; A-320; A-322; A-454 and A-456. 1 Publication
Mutagenesisi454 – 4541D → A: Loss of function; when associated with A-268; A-320; A-322; A-400 and A-456. 1 Publication
Mutagenesisi456 – 4561D → A: Loss of function; when associated with A-268; A-320; A-322; A-400 and A-454. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523Synaptotagmin-10PRO_0000183966Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361PhosphothreonineCombined sources
Modified residuei185 – 1851PhosphoserineBy similarity
Modified residuei218 – 2181PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ9R0N4.
PaxDbiQ9R0N4.
PRIDEiQ9R0N4.

PTM databases

iPTMnetiQ9R0N4.
PhosphoSiteiQ9R0N4.

Expressioni

Tissue specificityi

Highly expressed in the olfactory bulb.1 Publication

Gene expression databases

BgeeiQ9R0N4.
CleanExiMM_SYT10.
ExpressionAtlasiQ9R0N4. baseline and differential.
GenevisibleiQ9R0N4. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked via the cysteine motif (PubMed:10531343). Can also form heterodimers with SYT3, SYT6, SYT7 and SYT9 (PubMed:10531343, PubMed:10531344, PubMed:10871604).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-5239459,EBI-5239459
Syt3O356812EBI-5239459,EBI-457995
Syt6Q9R0N82EBI-5239459,EBI-5239378
Syt9Q9R0N92EBI-5239459,EBI-458006

GO - Molecular functioni

  • clathrin binding Source: GO_Central
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: GO_Central

Protein-protein interaction databases

IntActiQ9R0N4. 3 interactions.
STRINGi10090.ENSMUSP00000029441.

Structurei

3D structure databases

ProteinModelPortaliQ9R0N4.
SMRiQ9R0N4. Positions 232-500.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini233 – 334102C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini365 – 468104C2 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 3523Cysteine motifBy similarityAdd
BLAST

Domaini

The cysteine motif mediates homo- or heterodimer formation via formation of disulfide bonds.By similarity
The first C2 domain mediates Ca2+-dependent phospholipid binding.By similarity

Sequence similaritiesi

Belongs to the synaptotagmin family.Curated
Contains 2 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XQZ9. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232128.
HOVERGENiHBG005010.
InParanoidiQ9R0N4.
KOiK19910.
OMAiPPENVEQ.
OrthoDBiEOG78PV8W.
PhylomeDBiQ9R0N4.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028677. SYT10.
[Graphical view]
PANTHERiPTHR10024:SF46. PTHR10024:SF46. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R0N4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFRKEDGVS SLCQKALHII TELCFAGQVE WDKCSGIFPA DRSGQGGGGT
60 70 80 90 100
DISVSLLAVV VSFCGLALLV VSLFVFWKLC WPCWKSKLVA PNLSVLPQSI
110 120 130 140 150
SSAPTEVFET EEKKEVEENE KPAPKAIEPA IKISHTSPDI PAEVQTALKE
160 170 180 190 200
HLIKHARVQR QTTEPTSSSR HNSFRRHLPR QMNVSSVDFS VGTEPILQRG
210 220 230 240 250
ETRTSIGRIK PELYKQKSVD SEGNRKDDVK TCGKLNFALQ YDYENELLVV
260 270 280 290 300
KIIKALDLPA KDFTGTSDPY VKIYLLPDRK KKFQTRVHRK TLNPLFDELF
310 320 330 340 350
QFPVVYDQLS NRKLHFSIYD FDRFSRHDMI GEVILDNLFE VSDLSREATV
360 370 380 390 400
WKDIHCATTE SIDLGEIMFS LCYLPTAGRM TLTVIKCRNL KAMDITGSSD
410 420 430 440 450
PYVKVSLMCE GRRLKKRKTT TKKNTLNPVY NEAIIFDIPP ENVDQVSLCI
460 470 480 490 500
AVMDYDRVGH NEVIGVCRTG LDAEGLGRDH WNEMLAYHRK PITHWHPLLE
510 520
LPGRATSFDS QGSCSSPRPP STP
Length:523
Mass (Da):59,019
Last modified:May 1, 2000 - v1
Checksum:i1F551F4EF75A0A9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026807 mRNA. Translation: BAA85779.1.
CCDSiCCDS27756.1.
RefSeqiNP_061273.1. NM_018803.2.
UniGeneiMm.261601.

Genome annotation databases

EnsembliENSMUST00000029441; ENSMUSP00000029441; ENSMUSG00000063260.
GeneIDi54526.
KEGGimmu:54526.
UCSCiuc007xhi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB026807 mRNA. Translation: BAA85779.1.
CCDSiCCDS27756.1.
RefSeqiNP_061273.1. NM_018803.2.
UniGeneiMm.261601.

3D structure databases

ProteinModelPortaliQ9R0N4.
SMRiQ9R0N4. Positions 232-500.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R0N4. 3 interactions.
STRINGi10090.ENSMUSP00000029441.

PTM databases

iPTMnetiQ9R0N4.
PhosphoSiteiQ9R0N4.

Proteomic databases

MaxQBiQ9R0N4.
PaxDbiQ9R0N4.
PRIDEiQ9R0N4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029441; ENSMUSP00000029441; ENSMUSG00000063260.
GeneIDi54526.
KEGGimmu:54526.
UCSCiuc007xhi.2. mouse.

Organism-specific databases

CTDi341359.
MGIiMGI:1859546. Syt10.

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XQZ9. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232128.
HOVERGENiHBG005010.
InParanoidiQ9R0N4.
KOiK19910.
OMAiPPENVEQ.
OrthoDBiEOG78PV8W.
PhylomeDBiQ9R0N4.
TreeFamiTF315600.

Miscellaneous databases

PROiQ9R0N4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0N4.
CleanExiMM_SYT10.
ExpressionAtlasiQ9R0N4. baseline and differential.
GenevisibleiQ9R0N4. MM.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028677. SYT10.
[Graphical view]
PANTHERiPTHR10024:SF46. PTHR10024:SF46. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Conserved N-terminal cysteine motif is essential for homo- and heterodimer formation of synaptotagmins III, V, VI, and X."
    Fukuda M., Kanno E., Mikoshiba K.
    J. Biol. Chem. 274:31421-31427(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, DISULFIDE BOND.
    Strain: ICR.
    Tissue: Cerebellum.
  2. "A novel alternatively spliced variant of synaptotagmin VI lacking a transmembrane domain. Implications for distinct functions of the two isoforms."
    Fukuda M., Mikoshiba K.
    J. Biol. Chem. 274:31428-31434(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
    Strain: ICR.
    Tissue: Cerebellum.
  3. "Distinct self-oligomerization activities of synaptotagmin family. Unique calcium-dependent oligomerization properties of synaptotagmin VII."
    Fukuda M., Mikoshiba K.
    J. Biol. Chem. 275:28180-28185(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-136, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Activity-dependent IGF-1 exocytosis is controlled by the Ca(2+)-sensor synaptotagmin-10."
    Cao P., Maximov A., Suedhof T.C.
    Cell 145:300-311(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-268; ASP-320; ASP-322; ASP-400; ASP-454 AND ASP-456.
  6. "Complexin activates exocytosis of distinct secretory vesicles controlled by different synaptotagmins."
    Cao P., Yang X., Suedhof T.C.
    J. Neurosci. 33:1714-1727(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSYT10_MOUSE
AccessioniPrimary (citable) accession number: Q9R0N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.