Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9R0N9

- SYT9_MOUSE

UniProt

Q9R0N9 - SYT9_MOUSE

Protein

Synaptotagmin-9

Gene

Syt9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi251 – 2511Calcium 1By similarity
    Metal bindingi251 – 2511Calcium 2By similarity
    Metal bindingi257 – 2571Calcium 1By similarity
    Metal bindingi309 – 3091Calcium 1By similarity
    Metal bindingi309 – 3091Calcium 2By similarity
    Metal bindingi310 – 3101Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi311 – 3111Calcium 1By similarity
    Metal bindingi311 – 3111Calcium 2By similarity
    Metal bindingi311 – 3111Calcium 3By similarity
    Metal bindingi314 – 3141Calcium 3By similarity
    Metal bindingi317 – 3171Calcium 2By similarity
    Metal bindingi317 – 3171Calcium 3By similarity

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. transporter activity Source: InterPro

    GO - Biological processi

    1. positive regulation of calcium ion-dependent exocytosis Source: Ensembl
    2. regulation of insulin secretion Source: Ensembl

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Synaptotagmin-9
    Alternative name(s):
    Synaptotagmin IX
    Short name:
    SytIX
    Synaptotagmin V
    Gene namesi
    Name:Syt9
    Synonyms:Syt5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1926373. Syt9.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. dense core granule Source: MGI
    3. integral component of membrane Source: UniProtKB-KW
    4. secretory granule membrane Source: Ensembl
    5. synaptic vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasmic vesicle, Membrane, Synapse

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 491491Synaptotagmin-9PRO_0000183963Add
    BLAST

    Proteomic databases

    PaxDbiQ9R0N9.
    PRIDEiQ9R0N9.

    PTM databases

    PhosphoSiteiQ9R0N9.

    Expressioni

    Gene expression databases

    BgeeiQ9R0N9.
    CleanExiMM_SYT5.
    MM_SYT9.
    GenevestigatoriQ9R0N9.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-458006,EBI-458006
    Syt10Q9R0N42EBI-458006,EBI-5239459
    Syt3O356812EBI-458006,EBI-457995
    Syt6Q9R0N82EBI-458006,EBI-5239378

    Protein-protein interaction databases

    IntActiQ9R0N9. 4 interactions.
    STRINGi10090.ENSMUSP00000073164.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R0N9.
    SMRiQ9R0N9. Positions 221-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5252VesicularSequence AnalysisAdd
    BLAST
    Topological domaini74 – 491418CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei53 – 7321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini222 – 323102C2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini354 – 457104C2 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the synaptotagmin family.Curated
    Contains 2 C2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG292488.
    GeneTreeiENSGT00710000106556.
    HOGENOMiHOG000232128.
    HOVERGENiHBG005010.
    InParanoidiQ3U0R7.
    OMAiDFPRECV.
    TreeFamiTF315600.

    Family and domain databases

    Gene3Di2.60.40.150. 2 hits.
    InterProiIPR000008. C2_dom.
    IPR001565. Synaptotagmin.
    IPR028691. SYT9.
    [Graphical view]
    PANTHERiPTHR10024:SF174. PTHR10024:SF174. 1 hit.
    PfamiPF00168. C2. 2 hits.
    [Graphical view]
    PRINTSiPR00360. C2DOMAIN.
    PR00399. SYNAPTOTAGMN.
    SMARTiSM00239. C2. 2 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 2 hits.
    PROSITEiPS50004. C2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9R0N9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGARDALCH QALQLLAELC ARGALEHDSC QDFIYHLRDR ARPRLRDPDI    50
    SVSLLTLVVT ACGLALFGVS LFVSWKLCWV PWRERGLFSG SKDNNQEPLN 100
    YTDTETNEQE NSEDFLDPPT PCPDSSMKIS HTSPDIPLST QPGGQENCAH 150
    AVRVQRQVTE PTPSARHNSI RRQLNLSNPD FNIQQLQRQE QLTGIGRIKP 200
    ELYKQRSLDN DDGRRSNSKA CGKLNFILKY DCDLEQLIVK IHKAVNLPAK 250
    DFSGTSDPYV KIYLLPDRKT KHQTKVHRKT LNPVFDEVFL FPVHYNDLEA 300
    RKLHFSVYDF DRFSRHDLIG QVVVDHFFDL ADFPRECILW KDIEYVTNDN 350
    VDLGELMFSL CYLPTAGRLT ITIIKARNLK AMDITGASDP YVKVSLMCDG 400
    RRLKKRKTST KRNTLNPVYN EAIVFDVPPE SIDQIHLSIA VMDYDRVGHN 450
    EVIGVCQVGN EAERLGRDHW SEMLSYPRKP IAHWHSLMEK R 491
    Length:491
    Mass (Da):56,265
    Last modified:July 27, 2011 - v2
    Checksum:iE08ECFD9F4D6EE14
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti488 – 4881M → L in BAA85774. (PubMed:10531343)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS40078.1.
    RefSeqiNP_068689.2. NM_021889.4.
    UniGeneiMm.302793.

    Genome annotation databases

    EnsembliENSMUST00000073459; ENSMUSP00000073164; ENSMUSG00000062542.
    GeneIDi60510.
    KEGGimmu:60510.
    UCSCiuc009jba.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS40078.1.
    RefSeqi NP_068689.2. NM_021889.4.
    UniGenei Mm.302793.

    3D structure databases

    ProteinModelPortali Q9R0N9.
    SMRi Q9R0N9. Positions 221-491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9R0N9. 4 interactions.
    STRINGi 10090.ENSMUSP00000073164.

    PTM databases

    PhosphoSitei Q9R0N9.

    Proteomic databases

    PaxDbi Q9R0N9.
    PRIDEi Q9R0N9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000073459 ; ENSMUSP00000073164 ; ENSMUSG00000062542 .
    GeneIDi 60510.
    KEGGi mmu:60510.
    UCSCi uc009jba.1. mouse.

    Organism-specific databases

    CTDi 143425.
    MGIi MGI:1926373. Syt9.

    Phylogenomic databases

    eggNOGi NOG292488.
    GeneTreei ENSGT00710000106556.
    HOGENOMi HOG000232128.
    HOVERGENi HBG005010.
    InParanoidi Q3U0R7.
    OMAi DFPRECV.
    TreeFami TF315600.

    Miscellaneous databases

    NextBioi 314917.
    PROi Q9R0N9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9R0N9.
    CleanExi MM_SYT5.
    MM_SYT9.
    Genevestigatori Q9R0N9.

    Family and domain databases

    Gene3Di 2.60.40.150. 2 hits.
    InterProi IPR000008. C2_dom.
    IPR001565. Synaptotagmin.
    IPR028691. SYT9.
    [Graphical view ]
    PANTHERi PTHR10024:SF174. PTHR10024:SF174. 1 hit.
    Pfami PF00168. C2. 2 hits.
    [Graphical view ]
    PRINTSi PR00360. C2DOMAIN.
    PR00399. SYNAPTOTAGMN.
    SMARTi SM00239. C2. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 2 hits.
    PROSITEi PS50004. C2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiSYT9_MOUSE
    AccessioniPrimary (citable) accession number: Q9R0N9
    Secondary accession number(s): Q3U0R7, Q8C280
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2003
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3