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P46097 (SYT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Synaptotagmin-2
Alternative name(s):
Synaptotagmin II
Short name=SytII
Gene names
Name:Syt2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length422 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.

Cofactor

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

Subunit structure

Homotetramer Probable. Interacts with SCAMP5 By similarity. Interacts with stonin 2.

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Single-pass membrane protein. Cytoplasmic vesiclesecretory vesiclechromaffin 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SCAMP5Q8TAC92EBI-457969,EBI-2695784From a different organism.
Stx1aO355262EBI-457969,EBI-400878

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Synaptotagmin-2
PRO_0000183943

Regions

Topological domain1 – 6060Vesicular Potential
Transmembrane61 – 8727Helical; 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

Modified residue2301Phosphotyrosine Ref.5
Glycosylation321N-linked (GlcNAc...) Potential

Experimental info

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

Secondary structure

... 422
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46097 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[5]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA55417.
RefSeqNP_033333.2. NM_009307.3.
XP_006529385.1. XM_006529322.1.
XP_006529386.1. XM_006529323.1.
UniGeneMm.5102.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NP0X-ray2.62B40-60[»]
4KBBX-ray2.30C/D8-61[»]
ProteinModelPortalP46097.
SMRP46097. Positions 141-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203612. 3 interactions.
DIPDIP-32645N.
IntActP46097. 9 interactions.
MINTMINT-2411200.

PTM databases

PhosphoSiteP46097.

Proteomic databases

PaxDbP46097.
PRIDEP46097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000121990; ENSMUSP00000112438; ENSMUSG00000026452.
GeneID20980.
KEGGmmu:20980.
UCSCuc007csj.1. mouse.

Organism-specific databases

CTD127833.
MGIMGI:99666. Syt2.

Phylogenomic databases

eggNOGCOG5038.
GeneTreeENSGT00620000087641.
HOGENOMHOG000232127.
HOVERGENHBG005010.
InParanoidP46097.
OrthoDBEOG78PV8W.
PhylomeDBP46097.
TreeFamTF315600.

Gene expression databases

ArrayExpressP46097.
BgeeP46097.
CleanExMM_SYT2.
GenevestigatorP46097.

Family and domain databases

Gene3D2.60.40.150. 2 hits.
InterProIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1/2.
[Graphical view]
PANTHERPTHR10024:SF117. PTHR10024:SF117. 1 hit.
PfamPF00168. C2. 2 hits.
[Graphical view]
PRINTSPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTSM00239. C2. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 2 hits.
PROSITEPS50004. C2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46097.
NextBio299968.
PROP46097.
SOURCESearch...

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: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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