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P07164

- AEQ1_AEQVI

UniProt

P07164 - AEQ1_AEQVI

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Protein
Aequorin-1
Gene
N/A
Organism
Aequorea victoria (Jellyfish)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 – 42121
Add
BLAST
Calcium bindingi124 – 135122
Add
BLAST
Calcium bindingi160 – 171123
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. bioluminescence Source: UniProtKB-KW
Complete GO annotation...

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 – 77
PRO_0000004126
Chaini8 – 196189Aequorin-1
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP07164.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the aequorin family.
Contains 4 EF-hand domains.

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: September 18, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Caution

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

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

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