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UniProtKB/Swiss-Prot entry P46096


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SYT1_MOUSE
Primary accession number P46096
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 89)
Name and origin of the protein
Protein name Synaptotagmin-1
Synonyms Synaptotagmin I
SytI
p65
Gene name
Name: Syt1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7961887 [NCBI, ExPASy, EBI, Israel, Japan]
Fukuda M., Aruga J., Niinobe M., Aimoto S., Mikoshiba K.;
"Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II.";
J. Biol. Chem. 269:29206-29211(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Testis;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 183-189; 201-233; 245-260; 273-281; 289-297; 302-313; 333-366 AND 376-388, AND MASS SPECTROMETRY.
STRAIN=C57BL/6, and OF1;
TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
INTERACTION WITH SV2B; SYNTAXIN-1 AND SNAP25.
DOI=10.1074/jbc.M407502200; PubMed=15466855 [NCBI, ExPASy, EBI, Israel, Japan]
Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.;
"SV2B regulates synaptotagmin 1 by direct interaction.";
J. Biol. Chem. 279:52124-52131(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-229 AND TYR-380, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128, AND MASS SPECTROMETRY.
TISSUE=Brain cortex;
DOI=10.1074/mcp.M600046-MCP200; PubMed=17114649 [NCBI, ExPASy, EBI, Israel, Japan]
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364, AND MASS SPECTROMETRY.
TISSUE=Brain;
Lubec G., Kang S.;
Submitted (APR-2007) to UniProtKB.
Comments
  • FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
  • COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to the C2 domains (By similarity).
  • SUBUNIT: Homotetramer (Probable). Interacts with SCAMP5, STN2, SV2A, SV2B, SV2C and RIMS1 (By similarity). Forms a complex with SV2B, syntaxin 1 and SNAP25.
  • INTERACTION:
    Q8JZZ9:Sv2b; NbExp=1; IntAct=EBI-445340, EBI-466179;
  • SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Single-pass membrane protein. Cytoplasm. Note=Synaptic vesicles and chromaffin granules.
  • DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid binding.
  • DOMAIN: The second C2 domain mediates interaction with SV2A and STN2 (By similarity).
  • SIMILARITY: Belongs to the synaptotagmin family.
  • SIMILARITY: Contains 2 C2 domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D37792; BAA07040.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK078790; BAC37395.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC042519; AAH42519.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00129618; -.
RefSeq NP_033332.1; -.
UniGene Mm.289702
3D structure databases
HSSP P21707; 1K5W. [HSSP ENTRY / PDB]
SMR P46096; 271-418.
ModBase P46096.
Protein-protein interaction databases
IntAct P46096; 4.
Protein family/group databases
TCDB 9.A.48.1.1; unconventional protein secretion (UPS) system.
PTM databases
PhosphoSite P46096; -.
Organism-specific databases
MGI MGI:99667; Syt1.
Gene expression databases
ArrayExpress P46096; -.
Bgee P46096; -.
CleanEx MM_SYT1; -.
GermOnline ENSMUSG00000035864; Mus musculus.
Ontologies
GO
GO:0030054; Cellular component: cell junction (inferred from electronic annotation from UniProtKB-KW).
GO:0042584; Cellular component: chromaffin granule membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0043005; Cellular component: neuron projection (inferred from direct assay from MGI).
GO:0042734; Cellular component: presynaptic membrane (inferred from direct assay from MGI).
GO:0030672; Cellular component: synaptic vesicle membrane (inferred from direct assay from MGI).
GO:0005509; Molecular function: calcium ion binding (inferred from direct assay from MGI).
GO:0005544; Molecular function: calcium-dependent phospholipid binding (traceable author statement from MGI).
GO:0048306; Molecular function: calcium-dependent protein binding (inferred from physical interaction from HGNC).
GO:0005215; Molecular function: transporter activity (inferred from electronic annotation from InterPro).
GO:0007269; Biological process: neurotransmitter secretion (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000008; C2_Ca-dep.
IPR018029; C2_membr_targeting.
IPR001565; Synaptotagmin.
IPR015428; Synaptotagmin1_2.
Graphical view of domain structure.
PANTHER PTHR10024:SF39; Synaptotagmin1_2; 1.
Pfam PF00168; C2; 2.
Pfam graphical view of domain structure.
PRINTS PR00399; SYNAPTOTAGMN.
SMART SM00239; C2; 2.
SMART graphical view of domain structure.
PROSITE PS50004; C2; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P46096; -.
Genome annotation databases
Ensembl ENSMUSG00000035864; Mus musculus. [Contig view]
GeneID 20979; -.
KEGG mmu:20979; -.
Phylogenomic databases
HOGENOM P46096; -.
HOVERGEN P46096; -.
OMA P46096; VPHNATE.
Other
NextBio 299964; -.
SOURCE Syt1; Mus musculus.
ProtoNet P46096.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Cell junction; Cytoplasmic vesicle; Direct protein sequencing; Glycoprotein; Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; Repeat; Synapse; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   421  421     Synaptotagmin-1. PRO_0000183938
TOPO_DOM   1    57  57     Vesicular (Potential). 
TRANSMEM   58    79  22     Potential. 
TOPO_DOM   80   421  342     Cytoplasmic (Potential). 
DOMAIN   143   244  102     C2 1. 
DOMAIN   274   377  104     C2 2. 
REGION   135   381  247     Phospholipid binding (Probable). 
COMPBIAS   80   119  40     Lys-rich. 
METAL   171   171        Calcium 2; via carbonyl oxygen (By similarity). 
METAL   172   172        Calcium 1 (By similarity). 
METAL   172   172        Calcium 2 (By similarity). 
METAL   178   178        Calcium 1 (By similarity). 
METAL   230   230        Calcium 1 (By similarity). 
METAL   230   230        Calcium 2 (By similarity). 
METAL   231   231        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   232   232        Calcium 1 (By similarity). 
METAL   232   232        Calcium 2 (By similarity). 
METAL   232   232        Calcium 3 (By similarity). 
METAL   235   235        Calcium 3 (By similarity). 
METAL   236   236        Calcium 3; via carbonyl oxygen (By similarity). 
METAL   238   238        Calcium 2 (By similarity). 
METAL   238   238        Calcium 3 (By similarity). 
MOD_RES   128   128        Phosphothreonine. 
MOD_RES   229   229        Phosphotyrosine. 
MOD_RES   364   364        Phosphotyrosine. 
MOD_RES   380   380        Phosphotyrosine. 
LIPID   74    74        S-palmitoyl cysteine (By similarity). 
LIPID   75    75        S-palmitoyl cysteine (By similarity). 
LIPID   77    77        S-palmitoyl cysteine (By similarity). 
LIPID   79    79        S-palmitoyl cysteine (By similarity). 
LIPID   82    82        S-palmitoyl cysteine (By similarity). 
CARBOHYD   24    24        N-linked (GlcNAc...) (By similarity). 
Sequence information
Length: 421 AA [This is the length of the unprocessed precursor] Molecular weight: 47418 Da [This is the MW of the unprocessed precursor] CRC64: 7FDEFF37170BD169 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVSASRPEAL AAPVTTVATL VPHNATEPAS PGEGKEDAFS KLKQKFMNEL HKIPLPPWAL 

        70         80         90        100        110        120 
IAIAIVAVLL VVTCCFCVCK KCLFKKKNKK KGKEKGGKNA INMKDVKDLG KTMKDQALKD 

       130        140        150        160        170        180 
DDAETGLTDG EEKEEPKEEE KLGKLQYSLD YDFQNNQLLV GIIQAAELPA LDMGGTSDPY 

       190        200        210        220        230        240 
VKVFLLPDKK KKFETKVHRK TLNPVFNEQF TFKVPYSELG GKTLVMAVYD FDRFSKHDII 

       250        260        270        280        290        300 
GEFKVPMNTV DFGHVTEEWR DLQSAEKEEQ EKLGDICFSL RYVPTAGKLT VVILEAKNLK 

       310        320        330        340        350        360 
KMDVGGLSDP YVKIHLMQNG KRLKKKKTTI KKNTLNPYYN ESFSFEVPFE QIQKVQVVVT 

       370        380        390        400        410        420 
VLDYDKIGKN DAIGKVFVGY NSTGAELRHW SDMLANPRRP IAQWHTLQVE EEVDAMLAVK 


K 

P46096 in FASTA format

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