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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 – 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
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 – 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 – 3014Combined sources
Beta strandi35 – 395Combined sources
Helixi40 – 5314Combined sources
Helixi59 – 7517Combined sources
Beta strandi83 – 853Combined sources
Helixi86 – 10520Combined sources
Helixi111 – 12313Combined sources
Beta strandi128 – 1314Combined sources
Helixi133 – 14210Combined sources
Helixi149 – 15911Combined sources
Beta strandi165 – 1673Combined sources
Helixi169 – 18012Combined sources
Helixi190 – 1934Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MTSEQYSVKL TPDFDNPKWI GRHKHMFNFL DVNHNGRISL DEMVYKASDI
60 70 80 90 100
VINNLGATPE QAKRHKDAVE AFFGGAGMKY GVETEWPEYI EGWKRLASEE
110 120 130 140 150
LKRYSKNQIT LIRLWGDALF DIIDKDQNGA ISLDEWKAYT KSDGIIQSSE
160 170 180 190
DCEETFRVCD IDESGQLDVD EMTRQHLGFW YTMDPACEKL YGGAVP
Length:196
Mass (Da):22,514
Last modified:April 1, 1988 - v1
Checksum:i9AA5B636288A5B8F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16103 mRNA. Translation: AAA27716.1.
PIRiA26623.

Cross-referencesi

Web resourcesi

Wikipedia

Aequorin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16103 mRNA. Translation: AAA27716.1 .
PIRi A26623.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 89 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