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P07164

- AEQ1_AEQVI

UniProt

P07164 - AEQ1_AEQVI

Protein

Aequorin-1

Gene
N/A
Organism
Aequorea victoria (Jellyfish)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

    Ca2+-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO2 with the concomitant emission of light.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi31 – 42121Add
    BLAST
    Calcium bindingi124 – 135122Add
    BLAST
    Calcium bindingi160 – 171123Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. bioluminescence Source: UniProtKB-KW

    Keywords - Molecular functioni

    Photoprotein

    Keywords - Biological processi

    Luminescence

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.13.12.5. 8923.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aequorin-1
    OrganismiAequorea victoria (Jellyfish)
    Taxonomic identifieri6100 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaCnidariaHydrozoaHydroidaLeptomedusaeAequoreidaeAequorea

    Pathology & Biotechi

    Biotechnological usei

    Aequorin is used as an intracellular Ca2+ indicator. Aequorin has a number of advantages over other Ca2+ indicators, for example, low leakage rate from cells, lack of intracellular compartmentalization or sequestration and it does not disrupt cell functions or embryo development.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi196 – 1961Missing: Loss of bioluminescence. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 771 PublicationPRO_0000004126
    Chaini8 – 196189Aequorin-1PRO_0000004127Add
    BLAST

    Post-translational modificationi

    The reduction of the disulfide bond is necessary to regenerate aequorin from apoaequorin.

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    196
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 3014
    Beta strandi35 – 395
    Helixi40 – 5314
    Helixi59 – 7517
    Beta strandi83 – 853
    Helixi86 – 10520
    Helixi111 – 12313
    Beta strandi128 – 1314
    Helixi133 – 14210
    Helixi149 – 15911
    Beta strandi165 – 1673
    Helixi169 – 18012
    Helixi190 – 1934

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SL8X-ray1.70A7-196[»]
    ProteinModelPortaliP07164.
    SMRiP07164. Positions 16-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07164.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 5336EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini54 – 10855EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini111 – 14636EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini147 – 18236EF-hand 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni47 – 5711May interact with the chromophoreAdd
    BLAST
    Regioni62 – 7211May interact with the chromophoreAdd
    BLAST
    Regioni107 – 11711May interact with the chromophoreAdd
    BLAST

    Sequence similaritiesi

    Belongs to the aequorin family.Curated
    Contains 4 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF13202. EF-hand_5. 1 hit.
    PF13499. EF-hand_7. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 3 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 3 hits.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P07164-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSEQYSVKL TPDFDNPKWI GRHKHMFNFL DVNHNGRISL DEMVYKASDI    50
    VINNLGATPE QAKRHKDAVE AFFGGAGMKY GVETEWPEYI EGWKRLASEE 100
    LKRYSKNQIT LIRLWGDALF DIIDKDQNGA ISLDEWKAYT KSDGIIQSSE 150
    DCEETFRVCD IDESGQLDVD EMTRQHLGFW YTMDPACEKL YGGAVP 196
    Length:196
    Mass (Da):22,514
    Last modified:April 1, 1988 - v1
    Checksum:i9AA5B636288A5B8F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16103 mRNA. Translation: AAA27716.1.
    PIRiA26623.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Aequorin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16103 mRNA. Translation: AAA27716.1 .
    PIRi A26623.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SL8 X-ray 1.70 A 7-196 [» ]
    ProteinModelPortali P07164.
    SMRi P07164. Positions 16-196.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 1.13.12.5. 8923.

    Miscellaneous databases

    EvolutionaryTracei P07164.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF13202. EF-hand_5. 1 hit.
    PF13499. EF-hand_7. 1 hit.
    [Graphical view ]
    SMARTi SM00054. EFh. 3 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 3 hits.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence comparisons of complementary DNAs encoding aequorin isotypes."
      Prasher D.C., McCann R.O., Longiaru M., Cormier M.J.
      Biochemistry 26:1326-1332(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Amino acid sequence of the calcium-dependent photoprotein aequorin."
      Charbonneau H., Walsh K.A., McCann R.O., Prendergast F.G., Cormier M.J., Vanaman T.C.
      Biochemistry 24:6762-6771(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 8-196.
    3. "A C-terminal proline is required for bioluminescence of the Ca(2+)-binding photoprotein, aequorin."
      Nomura M., Inouye S., Ohmiya Y., Tsuji F.I.
      FEBS Lett. 295:63-66(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-196.
    4. "Mass spectrometric evidence for a disulfide bond in aequorin regeneration."
      Ohmiya Y., Kurono S., Ohashi M., Fagan T.F., Tsuji F.I.
      FEBS Lett. 332:226-228(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY DISULFIDE BOND.
    5. "All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin."
      Deng L., Vysotski E.S., Markova S.V., Liu Z.-J., Lee J., Rose J., Wang B.-C.
      Protein Sci. 14:663-675(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 7-196 IN COMPLEX WITH CALCIUM IONS.

    Entry informationi

    Entry nameiAEQ1_AEQVI
    AccessioniPrimary (citable) accession number: P07164
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    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)

    Miscellaneousi

    Caution

    Was originally thought to have a internal disulfide bond.1 Publication

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3