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Q9R0N3 (SYT11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptotagmin-11
Alternative name(s):
Synaptotagmin XI
Short name=SytXI
Gene names
Name:Syt11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may serve as Ca2+ sensors in the process of vesicular trafficking and exocytosis By similarity.

Cofactor

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

Subunit structure

Homodimer. Can also form heterodimers. Interacts with PARK2 By similarity.

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Single-pass membrane protein By similarity.

Post-translational modification

Ubiquitinated and targeted to the proteasome complex for degradation By similarity.

Sequence similarities

Belongs to the synaptotagmin family.

Contains 2 C2 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Synaptotagmin-11
PRO_0000183970

Regions

Topological domain1 – 1515Vesicular Potential
Transmembrane16 – 3621Helical; Potential
Topological domain37 – 430394Cytoplasmic Potential
Domain173 – 26189C2 1
Domain303 – 39694C2 2

Sites

Metal binding1871Calcium 1 By similarity
Metal binding1871Calcium 2 By similarity
Metal binding1941Calcium 1 By similarity
Metal binding2481Calcium 1; via carbonyl oxygen By similarity
Metal binding2491Calcium 1 By similarity
Metal binding2491Calcium 2 By similarity
Metal binding2491Calcium 3 By similarity
Metal binding2521Calcium 3 By similarity
Metal binding2551Calcium 2 By similarity
Metal binding2551Calcium 3 By similarity

Experimental info

Sequence conflict1451A → P in BAA85780. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R0N3 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 4E989259BE4FB423

FASTA43048,333
        10         20         30         40         50         60 
MAEITNIRPS FDVSPVAAGL IGASVLVVCV SVTVFVWTCC HQQAEKKHKT PPYKFIHMLK 

        70         80         90        100        110        120 
GISIYPETLS NKKKIIKVRR DKDGPRRESG RGNLLINAES GLLSHDKDPR GPSPASCMDQ 

       130        140        150        160        170        180 
LPIKRDYGEE LRSPMTSLTP GESKATSPSS PEEDVMLGSL TFSVDYNFPK KALVVTIQEA 

       190        200        210        220        230        240 
HGLPVMDDQT QGSDPYIKMT ILPDKRHRVK TRVLRKTLDP VFDETFTFYG IPYSQLQDLV 

       250        260        270        280        290        300 
LHFLVLSFDR FSRDDVIGEV MVPLAGVDPS TGKVQLTRDI IKRNIQKCIS RGELQVSLSY 

       310        320        330        340        350        360 
QPVAQRMTVV VLKARHLPKM DITGLSGNPY VKVNVYYGRK RIAKKKTHVK KCTLNPVFNE 

       370        380        390        400        410        420 
SFIYDIPTDL LPDISIEFLV IDFDRTTKNE VVGRLILGAH SVTTSGAEHW REVCESPRKP 

       430 
IAKWHSLSEY 

« Hide

References

« Hide 'large scale' references
[1]"Conserved N-terminal cysteine motif is essential for homo- and heterodimer formation of synaptotagmins III, V, VI, and X."
Fukuda M., Kanno E., Mikoshiba K.
J. Biol. Chem. 274:31421-31427(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
Tissue: Cerebellum.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB026808 mRNA. Translation: BAA85780.1.
AK144169 mRNA. Translation: BAE25745.1.
BC054526 mRNA. Translation: AAH54526.1.
RefSeqNP_061274.2. NM_018804.3.
XP_006501411.1. XM_006501348.1.
XP_006501412.1. XM_006501349.1.
UniGeneMm.379376.

3D structure databases

ProteinModelPortalQ9R0N3.
SMRQ9R0N3. Positions 157-429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9R0N3. 2 interactions.
MINTMINT-4136545.

PTM databases

PhosphoSiteQ9R0N3.

Proteomic databases

PaxDbQ9R0N3.
PRIDEQ9R0N3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090945; ENSMUSP00000088464; ENSMUSG00000068923.
ENSMUST00000107505; ENSMUSP00000103129; ENSMUSG00000068923.
GeneID229521.
KEGGmmu:229521.
UCSCuc008pwk.1. mouse.

Organism-specific databases

CTD23208.
MGIMGI:1859547. Syt11.

Phylogenomic databases

eggNOGNOG292488.
GeneTreeENSGT00750000117274.
HOGENOMHOG000232126.
HOVERGENHBG005010.
InParanoidQ7TQG8.
OMAIKVDYGD.
TreeFamTF315600.

Gene expression databases

ArrayExpressQ9R0N3.
BgeeQ9R0N3.
CleanExMM_SYT11.
GenevestigatorQ9R0N3.

Family and domain databases

Gene3D2.60.40.150. 2 hits.
InterProIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028699. SYT11.
[Graphical view]
PANTHERPTHR10024:SF115. PTHR10024:SF115. 1 hit.
PfamPF00168. C2. 2 hits.
[Graphical view]
PRINTSPR00399. SYNAPTOTAGMN.
SMARTSM00239. C2. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 2 hits.
PROSITEPS50004. C2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSYT11. mouse.
NextBio379479.
PROQ9R0N3.
SOURCESearch...

Entry information

Entry nameSYT11_MOUSE
AccessionPrimary (citable) accession number: Q9R0N3
Secondary accession number(s): Q7TQG8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 117 of the entry and version 2 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

MGD cross-references

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