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Protein

Aequorin-2

Gene
N/A
Organism
Aequorea victoria (Jellyfish)
Status
Reviewed-Annotation score: Annotation score: 5 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei196 – 1961Required for bioluminescence

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi31 – 42121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi124 – 135122PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi160 – 171123PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Photoprotein

Keywords - Biological processi

Luminescence

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Aequorin-2
OrganismiAequorea victoria (Jellyfish)
Taxonomic identifieri6100 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaHydrozoaHydroidolinaLeptothecataAequoreidaeAequorea

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361G → R: 100% activity loss. 1 Publication
Mutagenesisi65 – 651H → F: 100% activity loss. 1 Publication
Mutagenesisi129 – 1291G → R: 51% activity loss. 1 Publication
Mutagenesisi152 – 1521C → R: 52% activity loss. 1 Publication
Mutagenesisi152 – 1521C → S: 33% activity loss. 1 Publication
Mutagenesisi159 – 1591C → S: 41% activity loss. 1 Publication
Mutagenesisi165 – 1651G → R: No activity loss. 1 Publication
Mutagenesisi187 – 1871C → S: 71% activity loss. 1 Publication
Mutagenesisi196 – 1961Missing : Loss of bioluminescence. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 771 PublicationPRO_0000004128
Chaini8 – 196189Aequorin-2PRO_0000004129Add
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 strandi36 – 394Combined sources
Helixi40 – 5314Combined sources
Helixi59 – 7517Combined sources
Beta strandi83 – 853Combined sources
Helixi86 – 10520Combined sources
Helixi111 – 12313Combined sources
Beta strandi128 – 1314Combined sources
Helixi133 – 14311Combined sources
Helixi149 – 15810Combined sources
Helixi169 – 18012Combined sources
Helixi185 – 1873Combined sources
Turni188 – 1936Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ3X-ray2.30A/B9-196[»]
1UHHX-ray1.80A/B9-196[»]
1UHIX-ray1.80A/B9-196[»]
1UHJX-ray1.80A/B9-196[»]
1UHKX-ray1.60A/B9-196[»]
ProteinModelPortaliP02592.
SMRiP02592. Positions 9-196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02592.

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. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
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.

P02592-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSKQYSVKL TSDFDNPRWI GRHKHMFNFL DVNHNGKISL DEMVYKASDI
60 70 80 90 100
VINNLGATPE QAKRHKDAVE AFFGGAGMKY GVETDWPAYI EGWKKLATDE
110 120 130 140 150
LEKYAKNEPT LIRIWGDALF DIVDKDQNGA ITLDEWKAYT KAAGIIQSSE
160 170 180 190
DCEETFRVCD IDESGQLDVD EMTRQHLGFW YTMDPACEKL YGGAVP
Length:196
Mass (Da):22,285
Last modified:July 21, 1986 - v1
Checksum:i532DC7A9D29BA80C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371K → R in AAA27717 (PubMed:2882777).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 712EA → GD in aequorin-3.
Natural varianti164 – 1641S → N in aequorin-3.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29571 mRNA. Translation: AAA27720.1.
M16104 mRNA. Translation: AAA27717.1.
M16105 mRNA. Translation: AAA27718.1.
M11394 mRNA. Translation: AAA27719.1.
PIRiA03020. AQJFNV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29571 mRNA. Translation: AAA27720.1.
M16104 mRNA. Translation: AAA27717.1.
M16105 mRNA. Translation: AAA27718.1.
M11394 mRNA. Translation: AAA27719.1.
PIRiA03020. AQJFNV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJ3X-ray2.30A/B9-196[»]
1UHHX-ray1.80A/B9-196[»]
1UHIX-ray1.80A/B9-196[»]
1UHJX-ray1.80A/B9-196[»]
1UHKX-ray1.60A/B9-196[»]
ProteinModelPortaliP02592.
SMRiP02592. Positions 9-196.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02592.

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. 2 hits.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 3 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAEQ2_AEQVI
AccessioniPrimary (citable) accession number: P02592
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 11, 2016
This is version 95 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.