SYT9_HUMAN
ID SYT9_HUMAN Reviewed; 491 AA.
AC Q86SS6;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Synaptotagmin-9;
DE AltName: Full=Synaptotagmin IX;
DE Short=SytIX;
GN Name=SYT9;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [2]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-445.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [3]
RP VARIANTS MET-154; VAL-238 AND VAL-353.
RX PubMed=21220648; DOI=10.1001/archneurol.2010.351;
RA Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D.,
RA Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A.,
RA Rouleau G.A.;
RT "Resequencing of 29 candidate genes in patients with familial and sporadic
RT amyotrophic lateral sclerosis.";
RL Arch. Neurol. 68:587-593(2011).
CC -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory
CC vesicles through Ca(2+) and phospholipid binding to the C2 domain or
CC may serve as Ca(2+) sensors in the process of vesicular trafficking and
CC exocytosis.
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 SYT10.
CC {ECO:0000250|UniProtKB:Q9R0N9}.
CC -!- INTERACTION:
CC Q86SS6; P55061: TMBIM6; NbExp=3; IntAct=EBI-19129467, EBI-1045825;
CC Q86SS6; O95807: TMEM50A; NbExp=3; IntAct=EBI-19129467, EBI-12903814;
CC Q86SS6; O75841: UPK1B; NbExp=3; IntAct=EBI-19129467, EBI-12237619;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250}; Single-pass membrane protein
CC {ECO:0000250}.
CC -!- DOMAIN: The cysteine motif mediates homo- or heterodimer formation via
CC formation of disulfide bonds. {ECO:0000250|UniProtKB:O35681}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; BC046367; AAH46367.1; -; mRNA.
DR CCDS; CCDS7778.1; -.
DR RefSeq; NP_783860.1; NM_175733.3.
DR AlphaFoldDB; Q86SS6; -.
DR SMR; Q86SS6; -.
DR BioGRID; 126802; 18.
DR ELM; Q86SS6; -.
DR IntAct; Q86SS6; 3.
DR STRING; 9606.ENSP00000324419; -.
DR iPTMnet; Q86SS6; -.
DR PhosphoSitePlus; Q86SS6; -.
DR BioMuta; SYT9; -.
DR DMDM; 33112457; -.
DR EPD; Q86SS6; -.
DR MassIVE; Q86SS6; -.
DR MaxQB; Q86SS6; -.
DR PaxDb; Q86SS6; -.
DR PeptideAtlas; Q86SS6; -.
DR PRIDE; Q86SS6; -.
DR ProteomicsDB; 69631; -.
DR Antibodypedia; 42311; 156 antibodies from 29 providers.
DR DNASU; 143425; -.
DR Ensembl; ENST00000318881.11; ENSP00000324419.6; ENSG00000170743.17.
DR GeneID; 143425; -.
DR KEGG; hsa:143425; -.
DR MANE-Select; ENST00000318881.11; ENSP00000324419.6; NM_175733.4; NP_783860.1.
DR UCSC; uc001mfe.4; human.
DR CTD; 143425; -.
DR DisGeNET; 143425; -.
DR GeneCards; SYT9; -.
DR HGNC; HGNC:19265; SYT9.
DR HPA; ENSG00000170743; Tissue enhanced (brain, retina).
DR MIM; 613528; gene.
DR neXtProt; NX_Q86SS6; -.
DR OpenTargets; ENSG00000170743; -.
DR PharmGKB; PA134984583; -.
DR VEuPathDB; HostDB:ENSG00000170743; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000155948; -.
DR HOGENOM; CLU_023008_8_3_1; -.
DR InParanoid; Q86SS6; -.
DR OMA; NEAMVFD; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q86SS6; -.
DR TreeFam; TF315600; -.
DR PathwayCommons; Q86SS6; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q86SS6; -.
DR BioGRID-ORCS; 143425; 8 hits in 1068 CRISPR screens.
DR ChiTaRS; SYT9; human.
DR GeneWiki; SYT9; -.
DR GenomeRNAi; 143425; -.
DR Pharos; Q86SS6; Tbio.
DR PRO; PR:Q86SS6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86SS6; protein.
DR Bgee; ENSG00000170743; Expressed in medial globus pallidus and 122 other tissues.
DR ExpressionAtlas; Q86SS6; baseline and differential.
DR Genevisible; Q86SS6; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0031045; C:dense core granule; IBA:GO_Central.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030667; C:secretory granule membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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; IEA:Ensembl.
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:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IEA:Ensembl.
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:0045956; P:positive regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
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:0050796; P:regulation of insulin secretion; IEA:Ensembl.
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; IPR028691; SYT9.
DR PANTHER; PTHR10024:SF180; PTHR10024:SF180; 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; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..491
FT /note="Synaptotagmin-9"
FT /id="PRO_0000183962"
FT TOPO_DOM 1..52
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 220..341
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 352..485
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 9..31
FT /note="Cysteine motif"
FT /evidence="ECO:0000250|UniProtKB:O35681"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0N9"
FT VARIANT 154
FT /note="V -> M (in dbSNP:rs78477754)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065760"
FT VARIANT 238
FT /note="I -> V (in dbSNP:rs1001166978)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065761"
FT VARIANT 353
FT /note="L -> V (in dbSNP:rs117876446)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065762"
FT VARIANT 445
FT /note="D -> N (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036390"
SQ SEQUENCE 491 AA; 56188 MW; A9808E5E49153BB3 CRC64;
MPGARDALCH QALQLLAELC ARGALEHDSC QDFIYHLRDR ARPRLRDPDI SVSLLTLVVT
ACGLALFGVS LFVSWKLCWV PWRERGLPSG SKDNNQEPLN YMDTETNEQE NSEDFLDPPT
PCPDSSMKIS HTSPDIPLST QTGIQENCAH GVRVQRQVTE PTSSARHNSI RRQLNLSNPD
FNIQQLQKQE QLTGIGRIKP ELYKQRSLDN DDGRRSNSKA CGKLNFILKY DCDLEQLIVK
IHKAVNLPAK DFSGTSDPYV KIYLLPDRKT KHQTKVHRKT LNPVFDEVFL FPVPYNDLEA
RKLHFSVYDF DRFSRHDLIG QVVVDHFLDL ADFPRECILW KDIEYVTNDN VDLGELMFSL
CYLPTAGRLT ITIIKARNLK AMDITGASDP YVKVSLMCDG RRLKKRKTST KRNTLNPVYN
EAIVFDVPPE NIDQIHLSIA VMDYDRVGHN EIIGVCQVGN EAERLGRDHW SEMLSYPRKP
IAHWHSLVEK R
