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Reviewed, UniProtKB/Swiss-Prot P46097 (SYT2_MOUSE)

Last modified June 16, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Synaptotagmin-2
Alternative name(s):
    Synaptotagmin II
      Short name=SytII
Gene names
Name: Syt2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Cofactor

Binds 3 calcium ions per subunit. The ions are bound to the C2 domains By similarity.

Subunit structure

Homotetramer Probable. Interacts with SCAMP5 (Bysimilarity). Interacts with stonin 2.

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 Stonin 2.

Sequence similarities

Belongs to the synaptotagmin family.

Contains 2 C2 domains.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Synaptotagmin-2
PRO_0000183943

Regions

Topological domain1 – 6060Vesicular Potential
Transmembrane61 – 8727 Potential
Topological domain88 – 422335Cytoplasmic Potential
Domain156 – 24590C2 1
Domain287 – 37892C2 2
Region136 – 382247Phospholipid binding Probable

Sites

Metal binding1721Calcium 2; via carbonyl oxygen By similarity
Metal binding1731Calcium 1 By similarity
Metal binding1731Calcium 2 By similarity
Metal binding1791Calcium 1 By similarity
Metal binding2311Calcium 1 By similarity
Metal binding2311Calcium 2 By similarity
Metal binding2321Calcium 1; via carbonyl oxygen By similarity
Metal binding2331Calcium 1 By similarity
Metal binding2331Calcium 2 By similarity
Metal binding2331Calcium 3 By similarity
Metal binding2361Calcium 3 By similarity
Metal binding2371Calcium 3; via carbonyl oxygen By similarity
Metal binding2391Calcium 2 By similarity
Metal binding2391Calcium 3 By similarity

Amino acid modifications

Glycosylation321N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2211A → G Ref.3
Sequence conflict2211A → G Ref.4

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Sequences

Sequence LengthMass (Da)Tools
P46097-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B4BD13FF70E0481B

FASTA42247,263
        10         20         30         40         50         60 
MRNIFKRNQE PNVAPATTTA TMPLAPVAPA DNSTESTGPG ESQEDMFAKL KEKFFNEINK 

        70         80         90        100        110        120 
IPLPPWALIA MAVVAGLLLL TCCFCICKKC CCKKKKNKKE KGKGMKNAMN MKDMKGGQDD 

       130        140        150        160        170        180 
DDAETGLTEG EGEGEEEKEP ENLGKLQFSL DYDFQANQLT VGVLQAAELP ALDMGGTSDP 

       190        200        210        220        230        240 
YVKVFLLPDK KKKYETKVHR KTLNPAFNET FTFKVPYQEL AGKTLVMAIY DFDRFSKHDI 

       250        260        270        280        290        300 
IGEVKVPMNT VDLGQPIEEW RDLQGGEKEE PEKLGDICTS LRYVPTAGKL TVCILEAKNL 

       310        320        330        340        350        360 
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT VKKKTLNPYF NESFSFEIPF EQIQKVQVVV 

       370        380        390        400        410        420 
TVLDYDKLGK NEAIGKIFVG SNATGTELRH WSDMLANPRR PIAQWHSLKP EEEVDALLGK 


NK

« Hide

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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]"Genomic structure of the murine Syt2 gene."
Adachi R., Teich A.H., Nigam R.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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: Cerebellum.
[4]"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.
+Additional computationally mapped references.

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Cross-references

Sequence databases

D37793 mRNA. Translation: BAA07041.1.
AF257303 Genomic DNA. Translation: AAF68987.1.
AF257304 mRNA. Translation: AAF68988.1.
AK036357 mRNA. Translation: BAC29397.1.
BC027019 mRNA. Translation: AAH27019.1.
IPIIPI00129622.
PIRA55417.
RefSeqNP_033333.2.
UniGeneMm.5102

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2NP0X-ray2.62B40-60[»]
ModBaseSearch...

PTM databases

PhosphoSiteP46097.

Proteomic databases

PRIDEP46097.

Genome annotation databases

EnsemblENSMUSG00000026452. Mus musculus. [Contig view]
GeneID20980.
KEGGmmu:20980.

Organism-specific databases

MGIMGI:99666. Syt2.

Phylogenomic databases

HOGENOMP46097.
HOVERGENP46097.

Gene expression databases

ArrayExpressP46097.
BgeeP46097.
CleanExMM_SYT2.
GermOnlineENSMUSG00000026452. Mus musculus.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR018029. C2_membr_targeting.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1_2.
[Graphical view]
PANTHERPTHR10024:SF39. Synaptotagmin1_2. 1 hit.
PfamPF00168. C2. 2 hits.
[Graphical view]
PRINTSPR00399. SYNAPTOTAGMN.
SMARTSM00239. C2. 2 hits.
[Graphical view]
PROSITEPS50004. C2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio299968.
SOURCESearch...

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Entry information

Entry nameSYT2_MOUSE
AccessionPrimary (citable) accession number: P46097
Secondary accession number(s): Q8R0E1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents