[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1021/bi00379a019; PubMed=2882777 [NCBI, ExPASy, EBI, Israel, Japan] Prasher D.C., McCann R.O., Longiaru M., Cormier M.J.; "Sequence comparisons of complementary DNAs encoding aequorin isotypes."; Biochemistry 26:1326-1332(1987).
[2]	PROTEIN SEQUENCE OF 8-196. DOI=10.1021/bi00345a006; PubMed=2866797 [NCBI, ExPASy, EBI, Israel, Japan] Charbonneau H., Walsh K.A., McCann R.O., Prendergast F.G., Cormier M.J., Vanaman T.C.; "Amino acid sequence of the calcium-dependent photoprotein aequorin."; Biochemistry 24:6762-6771(1985).
[3]	MUTAGENESIS OF PRO-196. DOI=10.1016/0014-5793(91)81385-L; PubMed=1765170 [NCBI, ExPASy, EBI, Israel, Japan] Nomura M., Inouye S., Ohmiya Y., Tsuji F.I.; "A C-terminal proline is required for bioluminescence of the Ca(2+)-binding photoprotein, aequorin."; FEBS Lett. 295:63-66(1991).
[4]	PRELIMINARY DISULFIDE BOND. DOI=10.1016/0014-5793(93)80637-A; PubMed=8405461 [NCBI, ExPASy, EBI, Israel, Japan] Ohmiya Y., Kurono S., Ohashi M., Fagan T.F., Tsuji F.I.; "Mass spectrometric evidence for a disulfide bond in aequorin regeneration."; FEBS Lett. 332:226-228(1993).
[5]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 7-196 IN COMPLEX WITH CALCIUM IONS. DOI=10.1110/ps.041142905; PubMed=15689515 [NCBI, ExPASy, EBI, Israel, Japan] Deng L., Vysotski E.S., Markova S.V., Liu Z.-J., Lee J., Rose J., Wang B.-C.; "All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin."; Protein Sci. 14:663-675(2005).

Comments

FUNCTION: Ca(2+)-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 CO(2) with the concomitant emission of light.
PTM: The reduction of the disulfide bond is necessary to regenerate aequorin from apoaequorin.
BIOTECHNOLOGY: Aequorin is used as an intracellular Ca(2+) indicator. Aequorin has a number of advantages over other Ca(2+) indicators, for example, low leakage rate from cells, lack of intracellular compartmentalization or sequestration and it does not disrupt cell functions or embryo development.
SIMILARITY: Belongs to the aequorin family.
SIMILARITY: Contains 4 EF-hand domains.
CAUTION: Was originally (PubMed:8405461) thought to have a internal disulfide bond.
WEB RESOURCE: Name=Wikipedia; Note=Aequorin entry; URL="http://en.wikipedia.org/wiki/Aequorin";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M16103; AAA27716.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A26623; A26623.

3D structure databases

PDB

1SL8; X-ray; 1.70 A; A=7-196.

[ExPASy / RCSB / EBI]

PDBsum

1SL8; -.

ModBase

P07164.

Enzyme and pathway databases

BRENDA

1.13.12.5; 280134.

Ontologies

GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008218;	Biological process: bioluminescence (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011992; EF-Hand_type.
IPR018248; EF_hand.
IPR018247; EF_HAND_1.
IPR018249; EF_HAND_2.
IPR002048; EF_hand_Ca_bd.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.238.10; EF-Hand_type; 1.

Pfam

PF00036; efhand; 1.
Pfam graphical view of domain structure.

ProDom

PD000012; EF-hand; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00054; EFh; 3.
SMART graphical view of domain structure.

PROSITE

PS00018; EF_HAND_1; 3.
PS50222; EF_HAND_2; 3.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

P07164.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Direct protein sequencing; Disulfide bond; Luminescence; Photoprotein; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 7`	`7`		`PRO_0000004126`
`CHAIN`	`8 196`	`189`	`Aequorin-1.`	`PRO_0000004127`
`DOMAIN`	`18 53`	`36`	`EF-hand 1.`
`DOMAIN`	`54 108`	`55`	`EF-hand 2.`
`DOMAIN`	`111 146`	`36`	`EF-hand 3.`
`DOMAIN`	`147 182`	`36`	`EF-hand 4.`
`CA_BIND`	`31 42`	`12`	`1.`
`CA_BIND`	`124 135`	`12`	`2.`
`CA_BIND`	`160 171`	`12`	`3.`
`REGION`	`47 57`	`11`	`May interact with the chromophore.`
`REGION`	`62 72`	`11`	`May interact with the chromophore.`
`REGION`	`107 117`	`11`	`May interact with the chromophore.`
`MUTAGEN`	`196 196`		`Missing: Loss of bioluminescence.`
`HELIX`	`17 30`	`14`
`STRAND`	`35 39`	`5`
`HELIX`	`40 53`	`14`
`HELIX`	`59 75`	`17`
`STRAND`	`83 85`	`3`
`HELIX`	`86 105`	`20`
`HELIX`	`111 123`	`13`
`STRAND`	`128 131`	`4`
`HELIX`	`133 142`	`10`
`HELIX`	`149 159`	`11`
`STRAND`	`165 167`	`3`
`HELIX`	`169 180`	`12`
`HELIX`	`190 193`	`4`

Sequence information

Length: 196 AA [This is the length of the unprocessed precursor]

Molecular weight: 22514 Da [This is the MW of the unprocessed precursor]

CRC64: 9AA5B636288A5B8F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTSEQYSVKL TPDFDNPKWI GRHKHMFNFL DVNHNGRISL DEMVYKASDI VINNLGATPE 

        70         80         90        100        110        120 
QAKRHKDAVE AFFGGAGMKY GVETEWPEYI EGWKRLASEE LKRYSKNQIT LIRLWGDALF 

       130        140        150        160        170        180 
DIIDKDQNGA ISLDEWKAYT KSDGIIQSSE DCEETFRVCD IDESGQLDVD EMTRQHLGFW 

       190 
YTMDPACEKL YGGAVP

P07164 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools