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Q3TZZ7

- ESYT2_MOUSE

UniProt

Q3TZZ7 - ESYT2_MOUSE

Protein

Extended synaptotagmin-2

Gene

Esyt2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
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    Functioni

    Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi324 – 3241Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi325 – 3251Calcium 1By similarity
    Metal bindingi325 – 3251Calcium 2By similarity
    Metal bindingi337 – 3371Calcium 2By similarity
    Metal bindingi384 – 3841Calcium 1By similarity
    Metal bindingi384 – 3841Calcium 2By similarity
    Metal bindingi385 – 3851Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi386 – 3861Calcium 1By similarity
    Metal bindingi386 – 3861Calcium 2By similarity
    Metal bindingi386 – 3861Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi388 – 3881Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi390 – 3901Calcium 3By similarity
    Metal bindingi391 – 3911Calcium 1By similarity

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: Ensembl
    2. calcium ion binding Source: UniProtKB
    3. phosphatidylcholine binding Source: UniProtKB
    4. phosphatidylethanolamine binding Source: UniProtKB
    5. phosphatidylinositol binding Source: UniProtKB

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. lipid transport Source: UniProtKB-KW

    Keywords - Biological processi

    Endocytosis, Lipid transport, Transport

    Keywords - Ligandi

    Calcium, Lipid-binding, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Extended synaptotagmin-2
    Short name:
    E-Syt2
    Gene namesi
    Name:Esyt2
    Synonyms:D12Ertd551e, Fam62b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1261845. Esyt2.

    Subcellular locationi

    Cell membrane By similarity; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
    Note: Detected at sites of contact between the endoplasmic reticulum membrane and the cell membrane. Recruited to the cell membrane via the third C2 domain By similarity.By similarity

    GO - Cellular componenti

    1. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    2. integral component of plasma membrane Source: Ensembl
    3. intrinsic component of endoplasmic reticulum membrane Source: UniProtKB
    4. organelle membrane contact site Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 845845Extended synaptotagmin-2PRO_0000278259Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei615 – 6151PhosphoserineBy similarity
    Modified residuei662 – 6621Phosphoserine1 Publication
    Modified residuei663 – 6631PhosphoserineBy similarity
    Modified residuei667 – 6671PhosphoserineBy similarity
    Modified residuei679 – 6791PhosphoserineBy similarity
    Modified residuei682 – 6821Phosphoserine1 Publication
    Modified residuei685 – 6851Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ3TZZ7.
    PaxDbiQ3TZZ7.
    PRIDEiQ3TZZ7.

    PTM databases

    PhosphoSiteiQ3TZZ7.

    Expressioni

    Gene expression databases

    BgeeiQ3TZZ7.
    CleanExiMM_D12ERTD551E.
    GenevestigatoriQ3TZZ7.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with ESYT1 and ESYT3. Interacts with FGFR1 that has been activated by FGF1 binding. Interacts with the AP-2 complex; identified in a complex with the AP-2 complex and FGFR1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ3TZZ7. 1 interaction.
    MINTiMINT-4392453.
    STRINGi10090.ENSMUSP00000098548.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3TZZ7.
    SMRiQ3TZZ7. Positions 287-583, 680-841.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2727CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini49 – 513LumenalSequence Analysis
    Topological domaini73 – 845773CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei28 – 4821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei52 – 7221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini296 – 397102C2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini447 – 54195C2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini712 – 816105C2 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 294176Glycerophospholipid-binding barrel-like domainBy similarityAdd
    BLAST
    Regioni757 – 7648Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membraneBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi660 – 6634Poly-Ser

    Domaini

    Anchored to the endoplasmic reticulum membrane by a transmembrane hairpin structure; both N-terminus and C-terminus are cytoplasmic.By similarity
    The C2 domains mediate lipid and calcium binding. The N-terminal C2 domain binds calcium ions and is important for calcium-dependent lipid binding and interaction with membranes. Two calcium ions are bound at a high-affinity site and a third calcium ion is bound with lower affinity. May bind up to four calcium ions. In contrast, the second C2 domain apparently does not bind calcium. The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate and is required for location at the cell membrane By similarity.By similarity
    Contains a barrel-like domain that binds glycerophospholipids in its interior; can bind two lipid molecules simultaneously. Binds a variety of lipids, including phosphatidylethanolamine, phosphatidylcholine and phosphatidylinositol (By similarity).By similarity

    Sequence similaritiesi

    Belongs to the extended synaptotagmin family.Curated
    Contains 3 C2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5038.
    GeneTreeiENSGT00550000074417.
    HOGENOMiHOG000043080.
    HOVERGENiHBG055795.
    InParanoidiB2RSN5.
    OMAiVDVGQQP.
    OrthoDBiEOG7RNJZK.
    PhylomeDBiQ3TZZ7.
    TreeFamiTF324255.

    Family and domain databases

    Gene3Di2.60.40.150. 3 hits.
    InterProiIPR000008. C2_dom.
    [Graphical view]
    PfamiPF00168. C2. 3 hits.
    [Graphical view]
    SMARTiSM00239. C2. 3 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 3 hits.
    PROSITEiPS50004. C2. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3TZZ7-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSSAGGEGPE AGPGRAGGRS EPEAPGSALS VDLPGLLGQL ARSFALLLPV    50
    YALGYLGLSF SWVLLALGLL AWCRRSRGLK ASRLCRALAL LEDEEQAVRL 100
    GVRACDLPAW VHFPDTERAE WLNKTVKHMW PFICQFIEKL FRETIEPAVR 150
    GANAHLSTFS FTKVDVGQQP LRVNGVKVYT ENVDKRQIIL DLQISFVGNC 200
    EIDLEIKRYF CRAGVKSIQI HGTMRVILEP LIGDMPLVGA LSIFFLRKPL 250
    LEINWTGLTN LLDIPGLNGL SDTIILDIIS NYLVLPNRIT VPLVSEVQIA 300
    QLRFPIPKGV LRIHFIEAQD LQGKDTYLKG LVKGKSDPYG IIRVGNQIFQ 350
    SKVIKENLSP KWNEVYEALV YEHPGQELEI ELFDEDPDKD DFLGSLMIDL 400
    IEVEKERLLD EWFTLDEVPK GKLHLKLEWL TLMPDAANLD KVLADIRADK 450
    DQASDGLSSA LLILYLDSAR NLPSGKKINS NPNPLVQMSV GHKAQESKIR 500
    YKTSEPVWEE NFTFFIHNPR RQDLEVEVKD EQHQCSLGSL RIPLSQLLTS 550
    DNMTINQRFQ LSNSGPNSTL KMKIALRVLH LEKQERPPDY QHSAQVKRPS 600
    VSKEGRKMPI KSQMSASPGT GGANTAPSTP VMGVDDKPAM EEKPQPPEAS 650
    PLGHRDLGRS SSSLLASPSH IAAKEPTPSI ASDISLPIAT QELRQRLRQL 700
    ENGTTLGQSP LGQIQLTIRH SSQRNKLIVV VHSCRNLIAF SEDGSDPYVR 750
    MYLLPDKRRS GRRKTHVSKK TLNPVFDQSF DFSVSLPEVQ RRTLDVAVKN 800
    SGGFLSKDKG LLGKVLVVLA SEELAKGWTQ WYDLTEDGTR PQVIT 845
    Length:845
    Mass (Da):94,139
    Last modified:October 11, 2005 - v1
    Checksum:i988F3D97D7F3CF6C
    GO
    Isoform 2 (identifier: Q3TZZ7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-487: Missing.

    Show »
    Length:358
    Mass (Da):39,884
    Checksum:i6AE8B94A52027E24
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 487487Missing in isoform 2. 2 PublicationsVSP_023243Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014813 mRNA. Translation: BAB29565.1.
    AK044360 mRNA. Translation: BAC31884.1.
    AK157352 mRNA. Translation: BAE34059.1.
    BC052440 mRNA. Translation: AAH52440.1.
    BC054797 mRNA. Translation: AAH54797.1.
    BC059230 mRNA. Translation: AAH59230.1.
    BC138937 mRNA. Translation: AAI38938.1.
    CCDSiCCDS26211.1. [Q3TZZ7-1]
    RefSeqiNP_083007.2. NM_028731.5. [Q3TZZ7-1]
    XP_006516136.1. XM_006516073.1. [Q3TZZ7-1]
    UniGeneiMm.273755.

    Genome annotation databases

    EnsembliENSMUST00000100986; ENSMUSP00000098548; ENSMUSG00000021171. [Q3TZZ7-1]
    GeneIDi52635.
    KEGGimmu:52635.
    UCSCiuc007pho.1. mouse. [Q3TZZ7-1]
    uc007phq.1. mouse. [Q3TZZ7-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014813 mRNA. Translation: BAB29565.1 .
    AK044360 mRNA. Translation: BAC31884.1 .
    AK157352 mRNA. Translation: BAE34059.1 .
    BC052440 mRNA. Translation: AAH52440.1 .
    BC054797 mRNA. Translation: AAH54797.1 .
    BC059230 mRNA. Translation: AAH59230.1 .
    BC138937 mRNA. Translation: AAI38938.1 .
    CCDSi CCDS26211.1. [Q3TZZ7-1 ]
    RefSeqi NP_083007.2. NM_028731.5. [Q3TZZ7-1 ]
    XP_006516136.1. XM_006516073.1. [Q3TZZ7-1 ]
    UniGenei Mm.273755.

    3D structure databases

    ProteinModelPortali Q3TZZ7.
    SMRi Q3TZZ7. Positions 287-583, 680-841.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q3TZZ7. 1 interaction.
    MINTi MINT-4392453.
    STRINGi 10090.ENSMUSP00000098548.

    PTM databases

    PhosphoSitei Q3TZZ7.

    Proteomic databases

    MaxQBi Q3TZZ7.
    PaxDbi Q3TZZ7.
    PRIDEi Q3TZZ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000100986 ; ENSMUSP00000098548 ; ENSMUSG00000021171 . [Q3TZZ7-1 ]
    GeneIDi 52635.
    KEGGi mmu:52635.
    UCSCi uc007pho.1. mouse. [Q3TZZ7-1 ]
    uc007phq.1. mouse. [Q3TZZ7-2 ]

    Organism-specific databases

    CTDi 57488.
    MGIi MGI:1261845. Esyt2.

    Phylogenomic databases

    eggNOGi COG5038.
    GeneTreei ENSGT00550000074417.
    HOGENOMi HOG000043080.
    HOVERGENi HBG055795.
    InParanoidi B2RSN5.
    OMAi VDVGQQP.
    OrthoDBi EOG7RNJZK.
    PhylomeDBi Q3TZZ7.
    TreeFami TF324255.

    Miscellaneous databases

    NextBioi 309245.
    PROi Q3TZZ7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3TZZ7.
    CleanExi MM_D12ERTD551E.
    Genevestigatori Q3TZZ7.

    Family and domain databases

    Gene3Di 2.60.40.150. 3 hits.
    InterProi IPR000008. C2_dom.
    [Graphical view ]
    Pfami PF00168. C2. 3 hits.
    [Graphical view ]
    SMARTi SM00239. C2. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 3 hits.
    PROSITEi PS50004. C2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Retina and Testis.
    2. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6.
      Tissue: Brain.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    4. Cited for: CALCIUM BINDING.
    5. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-682 AND SER-685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiESYT2_MOUSE
    AccessioniPrimary (citable) accession number: Q3TZZ7
    Secondary accession number(s): B2RSN5, Q9D5Y7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 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