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Q9R0N9 (SYT9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptotagmin-9
Alternative name(s):
Synaptotagmin IX
Short name=SytIX
Synaptotagmin V
Gene names
Name:Syt9
Synonyms:Syt5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Cofactor

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

Subcellular location

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

Sequence similarities

Belongs to the synaptotagmin family.

Contains 2 C2 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Synaptotagmin-9
PRO_0000183963

Regions

Topological domain1 – 5252Vesicular Potential
Transmembrane53 – 7321Helical; Potential
Topological domain74 – 491418Cytoplasmic Potential
Domain222 – 323102C2 1
Domain354 – 457104C2 2

Sites

Metal binding2511Calcium 1 By similarity
Metal binding2511Calcium 2 By similarity
Metal binding2571Calcium 1 By similarity
Metal binding3091Calcium 1 By similarity
Metal binding3091Calcium 2 By similarity
Metal binding3101Calcium 1; via carbonyl oxygen By similarity
Metal binding3111Calcium 1 By similarity
Metal binding3111Calcium 2 By similarity
Metal binding3111Calcium 3 By similarity
Metal binding3141Calcium 3 By similarity
Metal binding3171Calcium 2 By similarity
Metal binding3171Calcium 3 By similarity

Experimental info

Sequence conflict4881M → L in BAA85774. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R0N9 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E08ECFD9F4D6EE14

FASTA49156,265
        10         20         30         40         50         60 
MPGARDALCH QALQLLAELC ARGALEHDSC QDFIYHLRDR ARPRLRDPDI SVSLLTLVVT 

        70         80         90        100        110        120 
ACGLALFGVS LFVSWKLCWV PWRERGLFSG SKDNNQEPLN YTDTETNEQE NSEDFLDPPT 

       130        140        150        160        170        180 
PCPDSSMKIS HTSPDIPLST QPGGQENCAH AVRVQRQVTE PTPSARHNSI RRQLNLSNPD 

       190        200        210        220        230        240 
FNIQQLQRQE QLTGIGRIKP ELYKQRSLDN DDGRRSNSKA CGKLNFILKY DCDLEQLIVK 

       250        260        270        280        290        300 
IHKAVNLPAK DFSGTSDPYV KIYLLPDRKT KHQTKVHRKT LNPVFDEVFL FPVHYNDLEA 

       310        320        330        340        350        360 
RKLHFSVYDF DRFSRHDLIG QVVVDHFFDL ADFPRECILW KDIEYVTNDN VDLGELMFSL 

       370        380        390        400        410        420 
CYLPTAGRLT ITIIKARNLK AMDITGASDP YVKVSLMCDG RRLKKRKTST KRNTLNPVYN 

       430        440        450        460        470        480 
EAIVFDVPPE SIDQIHLSIA VMDYDRVGHN EVIGVCQVGN EAERLGRDHW SEMLSYPRKP 

       490 
IAHWHSLMEK R 

« 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].
Strain: C57BL/6J and NOD.
Tissue: Olfactory bulb and Spleen.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB026802 mRNA. Translation: BAA85774.1.
AK089115 mRNA. Translation: BAC40759.1.
AK156631 mRNA. Translation: BAE33784.1.
CH466531 Genomic DNA. Translation: EDL16861.1.
BC132495 mRNA. Translation: AAI32496.1.
BC137904 mRNA. Translation: AAI37905.1.
CCDSCCDS40078.1.
RefSeqNP_068689.2. NM_021889.4.
UniGeneMm.302793.

3D structure databases

ProteinModelPortalQ9R0N9.
SMRQ9R0N9. Positions 221-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9R0N9. 4 interactions.
STRING10090.ENSMUSP00000073164.

PTM databases

PhosphoSiteQ9R0N9.

Proteomic databases

PaxDbQ9R0N9.
PRIDEQ9R0N9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073459; ENSMUSP00000073164; ENSMUSG00000062542.
GeneID60510.
KEGGmmu:60510.
UCSCuc009jba.1. mouse.

Organism-specific databases

CTD143425.
MGIMGI:1926373. Syt9.

Phylogenomic databases

eggNOGNOG292488.
GeneTreeENSGT00710000106556.
HOGENOMHOG000232128.
HOVERGENHBG005010.
InParanoidQ3U0R7.
OMADFPRECV.
TreeFamTF315600.

Gene expression databases

BgeeQ9R0N9.
CleanExMM_SYT5.
MM_SYT9.
GenevestigatorQ9R0N9.

Family and domain databases

Gene3D2.60.40.150. 2 hits.
InterProIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028691. SYT9.
[Graphical view]
PANTHERPTHR10024:SF174. PTHR10024:SF174. 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

NextBio314917.
PROQ9R0N9.
SOURCESearch...

Entry information

Entry nameSYT9_MOUSE
AccessionPrimary (citable) accession number: Q9R0N9
Secondary accession number(s): Q3U0R7, Q8C280
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: July 27, 2011
Last modified: July 9, 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