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P46096 (SYT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptotagmin-1
Alternative name(s):
Synaptotagmin I
Short name=SytI
p65
Gene names
Name:Syt1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 Ca2+-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 Ca2+-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 structure

Homotetramer Probable. Interacts with SCAMP5, STON2, SV2A, SV2B, SV2C and RIMS1 By similarity. Forms a complex with SV2B, syntaxin 1 and SNAP25. Ref.5

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 Ca2+-dependent phospholipid binding.

The second C2 domain mediates interaction with SV2A and STN2 By similarity.

Sequence similarities

Belongs to the synaptotagmin family.

Contains 2 C2 domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SCAMP5Q8TAC92EBI-445340,EBI-2695784From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Synaptotagmin-1
PRO_0000183938

Regions

Topological domain1 – 5757Vesicular Potential
Transmembrane58 – 7922Helical; Potential
Topological domain80 – 421342Cytoplasmic Potential
Domain143 – 244102C2 1
Domain274 – 377104C2 2
Region135 – 381247Phospholipid binding Probable
Compositional bias80 – 11940Lys-rich

Sites

Metal binding1711Calcium 2; via carbonyl oxygen By similarity
Metal binding1721Calcium 1 By similarity
Metal binding1721Calcium 2 By similarity
Metal binding1781Calcium 1 By similarity
Metal binding2301Calcium 1 By similarity
Metal binding2301Calcium 2 By similarity
Metal binding2311Calcium 1; via carbonyl oxygen By similarity
Metal binding2321Calcium 1 By similarity
Metal binding2321Calcium 2 By similarity
Metal binding2321Calcium 3 By similarity
Metal binding2351Calcium 3 By similarity
Metal binding2361Calcium 3; via carbonyl oxygen By similarity
Metal binding2381Calcium 2 By similarity
Metal binding2381Calcium 3 By similarity

Amino acid modifications

Modified residue1281Phosphothreonine Ref.7
Modified residue2291Phosphotyrosine Ref.6
Modified residue2361N6-acetyllysine By similarity
Modified residue3641Phosphotyrosine Ref.8
Modified residue3801Phosphotyrosine Ref.6
Lipidation741S-palmitoyl cysteine By similarity
Lipidation751S-palmitoyl cysteine By similarity
Lipidation771S-palmitoyl cysteine By similarity
Lipidation791S-palmitoyl cysteine By similarity
Lipidation821S-palmitoyl cysteine By similarity
Glycosylation241N-linked (GlcNAc...) By similarity

Sequences

Sequence LengthMass (Da)Tools
P46096 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7FDEFF37170BD169

FASTA42147,418
        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

« Hide

References

« Hide 'large scale' references
[1]"Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II."
Fukuda M., Aruga J., Niinobe M., Aimoto S., Mikoshiba K.
J. Biol. Chem. 269:29206-29211(1994) [PubMed: 7961887] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[4]Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 183-189; 201-233; 245-260; 273-281; 289-297; 302-313; 333-366 AND 376-388, MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[5]"SV2B regulates synaptotagmin 1 by direct interaction."
Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.
J. Biol. Chem. 279:52124-52131(2004) [PubMed: 15466855] [Abstract]
Cited for: INTERACTION WITH SV2B; SYNTAXIN-1 AND SNAP25.
[6]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-229 AND TYR-380, MASS SPECTROMETRY.
Tissue: Brain.
[7]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
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.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128, MASS SPECTROMETRY.
Tissue: Brain cortex.
[8]Lubec G., Kang S.
Submitted (APR-2007) to UniProtKB
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D37792 mRNA. Translation: BAA07040.1.
AK078790 mRNA. Translation: BAC37395.1.
BC042519 mRNA. Translation: AAH42519.1.
IPIIPI00129618.
RefSeqNP_001239270.1. NM_001252341.1.
NP_033332.1. NM_009306.3.
UniGeneMm.289702.

3D structure databases

ProteinModelPortalP46096.
SMRP46096. Positions 140-418.
ModBaseSearch...

Protein-protein interaction databases

IntActP46096. 9 interactions.
MINTMINT-4136555.
STRINGP46096.

Protein family/group databases

TCDB9.A.48.1.1. unconventional protein secretion (UPS) system.

PTM databases

PhosphoSiteP46096.

Proteomic databases

PRIDEP46096.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064054; ENSMUSP00000063293; ENSMUSG00000035864.
ENSMUST00000105276; ENSMUSP00000100912; ENSMUSG00000035864.
GeneID20979.
KEGGmmu:20979.
UCSCuc007gzg.1. mouse.

Organism-specific databases

CTD6857.
MGIMGI:99667. Syt1.

Phylogenomic databases

eggNOGroNOG10139.
HOGENOMHBG716633.
HOVERGENHBG005010.
InParanoidP46096.
OMAHDIIGEY.
OrthoDBEOG4MGS7Q.
PhylomeDBP46096.

Gene expression databases

ArrayExpressP46096.
BgeeP46096.
CleanExMM_SYT1.
GenevestigatorP46096.
GermOnlineENSMUSG00000035864. Mus musculus.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR020477. C2_dom.
IPR018029. C2_membr_targeting.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1.
[Graphical view]
KOK15290.
PANTHERPTHR10024:SF39. Synaptotagmin1_2. 1 hit.
PfamPF00168. C2. 2 hits.
[Graphical view]
PRINTSPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTSM00239. C2. 2 hits.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 2 hits.
PROSITEPS50004. C2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio299964.
SOURCESearch...

Entry information

Entry nameSYT1_MOUSE
AccessionPrimary (citable) accession number: P46096
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents