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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)DescriptionActionsGraphical viewLength
Sitei196Required for bioluminescence1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi31 – 421PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi124 – 1352PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi160 – 1713PROSITE-ProRule annotationAdd BLAST12

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)DescriptionActionsGraphical viewLength
Mutagenesisi36G → R: 100% activity loss. 1 Publication1
Mutagenesisi65H → F: 100% activity loss. 1 Publication1
Mutagenesisi129G → R: 51% activity loss. 1 Publication1
Mutagenesisi152C → R: 52% activity loss. 1 Publication1
Mutagenesisi152C → S: 33% activity loss. 1 Publication1
Mutagenesisi159C → S: 41% activity loss. 1 Publication1
Mutagenesisi165G → R: No activity loss. 1 Publication1
Mutagenesisi187C → S: 71% activity loss. 1 Publication1
Mutagenesisi196Missing : Loss of bioluminescence. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000041281 – 71 Publication7
ChainiPRO_00000041298 – 196Aequorin-2Add BLAST189

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 30Combined sources14
Beta strandi36 – 39Combined sources4
Helixi40 – 53Combined sources14
Helixi59 – 75Combined sources17
Beta strandi83 – 85Combined sources3
Helixi86 – 105Combined sources20
Helixi111 – 123Combined sources13
Beta strandi128 – 131Combined sources4
Helixi133 – 143Combined sources11
Helixi149 – 158Combined sources10
Helixi169 – 180Combined sources12
Helixi185 – 187Combined sources3
Turni188 – 193Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02592.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 53EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini54 – 108EF-hand 2PROSITE-ProRule annotationAdd BLAST55
Domaini111 – 146EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini147 – 182EF-hand 4PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 57May interact with the chromophoreAdd BLAST11
Regioni62 – 72May interact with the chromophoreAdd BLAST11
Regioni107 – 117May interact with the chromophoreAdd BLAST11

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Family and domain databases

CDDicd00051. EFh. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti37K → R in AAA27717 (PubMed:2882777).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti70 – 71EA → GD in aequorin-3. 2
Natural varianti164S → N in aequorin-3. 1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02592.

Family and domain databases

CDDicd00051. EFh. 1 hit.
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: November 30, 2016
This is version 98 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.