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Q9Z1X1

- ESYT1_RAT

UniProt

Q9Z1X1 - ESYT1_RAT

Protein

Extended synaptotagmin-1

Gene

Esyt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport By similarity. Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels. Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi336 – 3361Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi337 – 3371Calcium 1By similarity
    Metal bindingi337 – 3371Calcium 2By similarity
    Metal bindingi349 – 3491Calcium 2By similarity
    Metal bindingi396 – 3961Calcium 1By similarity
    Metal bindingi396 – 3961Calcium 2By similarity
    Metal bindingi398 – 3981Calcium 1By similarity
    Metal bindingi398 – 3981Calcium 2By similarity
    Metal bindingi398 – 3981Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi400 – 4001Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi402 – 4021Calcium 3By similarity
    Metal bindingi403 – 4031Calcium 1By similarity

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. lipid transport Source: UniProtKB-KW

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Calcium, Lipid-binding, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Extended synaptotagmin-1
    Short name:
    E-Syt1
    Alternative name(s):
    Membrane-bound C2 domain-containing protein
    vp115
    Gene namesi
    Name:Esyt1
    Synonyms:Fam62a, Mbc2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 7

    Organism-specific databases

    RGDi3053. Esyt1.

    Subcellular locationi

    Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity
    Note: Localizes primarily to the endoplasmic reticulum. Recruited to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels By similarity.By similarity

    GO - Cellular componenti

    1. integral component of endoplasmic reticulum membrane Source: UniProtKB
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10881088Extended synaptotagmin-1PRO_0000234347Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei316 – 3161Phosphoserine; by CDK5By similarity
    Modified residuei806 – 8061N6-acetyllysineBy similarity
    Modified residuei809 – 8091PhosphoserineBy similarity
    Modified residuei947 – 9471PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on Ser residues in insulin-treated adipocytes (in vitro); this promotes interaction with SLC2A4.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9Z1X1.
    PRIDEiQ9Z1X1.

    PTM databases

    PhosphoSiteiQ9Z1X1.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with a higher expression in spleen and white adipose tissue.1 Publication

    Gene expression databases

    GenevestigatoriQ9Z1X1.

    Interactioni

    Subunit structurei

    Interacts with ESYT2 and ESYT3. Interacts (phosphorylated form) with SLC2A4 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi248212. 2 interactions.
    IntActiQ9Z1X1. 1 interaction.
    MINTiMINT-4568934.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z1X1.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3030CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini52 – 543LumenalSequence Analysis
    Topological domaini76 – 10881013CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei31 – 5121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei55 – 7521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini308 – 409102C2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini457 – 55094C2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini623 – 724102C2 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini774 – 86693C2 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini956 – 1061106C2 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni131 – 305175Glycerophospholipid-binding barrel-like domainBy similarityAdd
    BLAST
    Regioni1002 – 10098Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membraneBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi912 – 9176Poly-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 translocation to the cell membrane in response to increased cytosolic calcium levels By similarity.By similarity
    Contains a barrel-like domain that can bind various types of glycerophospholipids in its interior.By similarity

    Sequence similaritiesi

    Belongs to the extended synaptotagmin family.Curated
    Contains 5 C2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5038.
    GeneTreeiENSGT00550000074417.
    HOGENOMiHOG000043080.
    HOVERGENiHBG055795.
    InParanoidiQ9Z1X1.
    OrthoDBiEOG7RNJZK.
    PhylomeDBiQ9Z1X1.
    TreeFamiTF324255.

    Family and domain databases

    Gene3Di2.60.40.150. 5 hits.
    InterProiIPR000008. C2_dom.
    [Graphical view]
    PfamiPF00168. C2. 5 hits.
    [Graphical view]
    PRINTSiPR00360. C2DOMAIN.
    SMARTiSM00239. C2. 5 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 5 hits.
    PROSITEiPS50004. C2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Z1X1-1 [UniParc]FASTAAdd to Basket

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    MERSPEEGAG PEPSGQSPAT DSTRERDGGS GVPPAGPGAA SEALAVLTSF     50
    GRRLLVLVPV YLAGAAGLSV GFVLFGLALY LGWRRVRDGK ERSLRAARQL 100
    LDDEERITAE TLYMSHRELP AWVSFPDVEK AEWLNKIVVQ VWPFLGQYME 150
    KLLAETVAPA VRGANPHLQT FTFTRVELGE KPVRIIGVKV HPSQRKDQIL 200
    LDLNVSYVGD LQIDVEVKKY FCKAGVKGMQ LHGVLRVILE PLIGDLPIVG 250
    AVSMFFIKRP TLDINWTGMT NLLDIPGLSS LSDTMIMDSI AAFLVLPNRL 300
    LVPLVPDLQD VAQLRSPLPR GIIRIHLLAA RGLSSKDKYV KGLIEGKSDP 350
    YALVRVGTQT FCSRVIDEEL NPHWGETYEV IVHEVPGQEI EVEVFDKDPD 400
    KDDFLGRMKL DVGKVLQAGV LDNWYPLQGG QGQVHLRLEW LSLLPDAEKL 450
    DQVLQWNRGI TSRPEPPSAA ILVVYLDRAQ DLPLKKGNKE PNPMVQLSVQ 500
    DVTQESKATY STNCPVWEEA FRFFLQDPRS QELDVQVKDD SRALTLGALT 550
    LPLARLLTAS ELTLDQWFQL SSSGPNSRLY MKLVMRILYL DSSEMRLPTE 600
    PGAQDWDSES PETGSSVDAP PRPYHTTPNS HFGTENVLRI HVLEAQDLIA 650
    KDRFLGGLVK GKSDPYVKLK VAGRSLRTHV VREDLNPRWN EVFEVIVTSI 700
    PGQELDIEVF DKDLDKDDFL GRYKVGLTTV LNSGFLDEWL TLEDVPSGRL 750
    HLRLERLSPR PTAAELEEVL QVNSLIQTQK SSELAAALLS VYLERSEDLP 800
    LRKGTKPPSP YAILTVGETS HKTKTVSQTS APIWEESASF LIRKPHAESL 850
    ELQVRGEGTG TLGSISLPLS ELLQEEQLCL DRWFALSGQG QVLMRVQLGI 900
    LVSQHSGVEA HSHSSSSLNE EPEVLGDPTH TASPVLEVRH RLTHGDSPSE 950
    ALIGPLGQVK LTVWYHSDEQ KLISIIHSCR ALRQNGRDLP DPYVSVLLLP 1000
    DKNRGTKRKT SQKKRTLNPE FNERFEWDLP LDGTLRRKLD VSVKSNSSFM 1050
    SRERELLGKV QLDLAEIDLS QGAAQWYDLI DDRDKGGS 1088
    Length:1,088
    Mass (Da):121,159
    Last modified:May 1, 1999 - v1
    Checksum:iE7E12D9737FFB89D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti373 – 3731H → R in AAI01858. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF099138 mRNA. Translation: AAD10051.1.
    BC101857 mRNA. Translation: AAI01858.1.
    RefSeqiNP_058945.2. NM_017249.2.
    UniGeneiRn.11636.

    Genome annotation databases

    EnsembliENSRNOT00000006119; ENSRNOP00000006119; ENSRNOG00000003909.
    GeneIDi29579.
    KEGGirno:29579.
    UCSCiRGD:3053. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF099138 mRNA. Translation: AAD10051.1 .
    BC101857 mRNA. Translation: AAI01858.1 .
    RefSeqi NP_058945.2. NM_017249.2.
    UniGenei Rn.11636.

    3D structure databases

    ProteinModelPortali Q9Z1X1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248212. 2 interactions.
    IntActi Q9Z1X1. 1 interaction.
    MINTi MINT-4568934.

    PTM databases

    PhosphoSitei Q9Z1X1.

    Proteomic databases

    PaxDbi Q9Z1X1.
    PRIDEi Q9Z1X1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000006119 ; ENSRNOP00000006119 ; ENSRNOG00000003909 .
    GeneIDi 29579.
    KEGGi rno:29579.
    UCSCi RGD:3053. rat.

    Organism-specific databases

    CTDi 23344.
    RGDi 3053. Esyt1.

    Phylogenomic databases

    eggNOGi COG5038.
    GeneTreei ENSGT00550000074417.
    HOGENOMi HOG000043080.
    HOVERGENi HBG055795.
    InParanoidi Q9Z1X1.
    OrthoDBi EOG7RNJZK.
    PhylomeDBi Q9Z1X1.
    TreeFami TF324255.

    Miscellaneous databases

    NextBioi 609682.

    Gene expression databases

    Genevestigatori Q9Z1X1.

    Family and domain databases

    Gene3Di 2.60.40.150. 5 hits.
    InterProi IPR000008. C2_dom.
    [Graphical view ]
    Pfami PF00168. C2. 5 hits.
    [Graphical view ]
    PRINTSi PR00360. C2DOMAIN.
    SMARTi SM00239. C2. 5 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 5 hits.
    PROSITEi PS50004. C2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and preliminary characterization of a 121 kDa protein with multiple predicted C2 domains."
      Morris N.J., Ross S.A., Neveu J.M., Lane W.S., Lienhard G.E.
      Biochim. Biophys. Acta 1431:525-530(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
    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].
      Tissue: Prostate.

    Entry informationi

    Entry nameiESYT1_RAT
    AccessioniPrimary (citable) accession number: Q9Z1X1
    Secondary accession number(s): Q3T1L3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 88 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3