ID   AEQ1_AEQVI              Reviewed;         196 AA.
AC   P07164;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   31-MAY-2011, entry version 81.
DE   RecName: Full=Aequorin-1;
DE   Flags: Precursor;
OS   Aequorea victoria (Jellyfish).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroida; Leptomedusae;
OC   Aequoreidae; Aequorea.
OX   NCBI_TaxID=6100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87185437; PubMed=2882777; DOI=10.1021/bi00379a019;
RA   Prasher D.C., McCann R.O., Longiaru M., Cormier M.J.;
RT   "Sequence comparisons of complementary DNAs encoding aequorin
RT   isotypes.";
RL   Biochemistry 26:1326-1332(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 8-196.
RX   MEDLINE=86077721; PubMed=2866797; DOI=10.1021/bi00345a006;
RA   Charbonneau H., Walsh K.A., McCann R.O., Prendergast F.G.,
RA   Cormier M.J., Vanaman T.C.;
RT   "Amino acid sequence of the calcium-dependent photoprotein aequorin.";
RL   Biochemistry 24:6762-6771(1985).
RN   [3]
RP   MUTAGENESIS OF PRO-196.
RX   MEDLINE=92111761; PubMed=1765170; DOI=10.1016/0014-5793(91)81385-L;
RA   Nomura M., Inouye S., Ohmiya Y., Tsuji F.I.;
RT   "A C-terminal proline is required for bioluminescence of the Ca(2+)-
RT   binding photoprotein, aequorin.";
RL   FEBS Lett. 295:63-66(1991).
RN   [4]
RP   PRELIMINARY DISULFIDE BOND.
RX   MEDLINE=94009705; PubMed=8405461; DOI=10.1016/0014-5793(93)80637-A;
RA   Ohmiya Y., Kurono S., Ohashi M., Fagan T.F., Tsuji F.I.;
RT   "Mass spectrometric evidence for a disulfide bond in aequorin
RT   regeneration.";
RL   FEBS Lett. 332:226-228(1993).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 7-196 IN COMPLEX WITH CALCIUM
RP   IONS.
RX   PubMed=15689515; DOI=10.1110/ps.041142905;
RA   Deng L., Vysotski E.S., Markova S.V., Liu Z.-J., Lee J., Rose J.,
RA   Wang B.-C.;
RT   "All three Ca2+-binding loops of photoproteins bind calcium ions: the
RT   crystal structures of calcium-loaded apo-aequorin and apo-obelin.";
RL   Protein Sci. 14:663-675(2005).
CC   -!- FUNCTION: Ca(2+)-dependent bioluminescence photoprotein. Displays
CC       an emission peak at 470 nm (blue light). Trace amounts of calcium
CC       ion trigger the intramolecular oxidation of the chromophore,
CC       coelenterazine into coelenteramide and CO(2) with the concomitant
CC       emission of light.
CC   -!- PTM: The reduction of the disulfide bond is necessary to
CC       regenerate aequorin from apoaequorin.
CC   -!- BIOTECHNOLOGY: Aequorin is used as an intracellular Ca(2+)
CC       indicator. Aequorin has a number of advantages over other Ca(2+)
CC       indicators, for example, low leakage rate from cells, lack of
CC       intracellular compartmentalization or sequestration and it does
CC       not disrupt cell functions or embryo development.
CC   -!- SIMILARITY: Belongs to the aequorin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
CC   -!- CAUTION: Was originally (PubMed:8405461) thought to have a
CC       internal disulfide bond.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Aequorin entry;
CC       URL="http://en.wikipedia.org/wiki/Aequorin";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M16103; AAA27716.1; -; mRNA.
DR   PIR; A26623; A26623.
DR   PDB; 1SL8; X-ray; 1.70 A; A=7-196.
DR   PDBsum; 1SL8; -.
DR   ProteinModelPortal; P07164; -.
DR   SMR; P07164; 16-196.
DR   BRENDA; 1.13.12.5; 8923.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW   Luminescence; Photoprotein; Repeat.
FT   PROPEP        1      7
FT                                /FTId=PRO_0000004126.
FT   CHAIN         8    196       Aequorin-1.
FT                                /FTId=PRO_0000004127.
FT   DOMAIN       18     53       EF-hand 1.
FT   DOMAIN       54    108       EF-hand 2.
FT   DOMAIN      111    146       EF-hand 3.
FT   DOMAIN      147    182       EF-hand 4.
FT   CA_BIND      31     42       1.
FT   CA_BIND     124    135       2.
FT   CA_BIND     160    171       3.
FT   REGION       47     57       May interact with the chromophore.
FT   REGION       62     72       May interact with the chromophore.
FT   REGION      107    117       May interact with the chromophore.
FT   MUTAGEN     196    196       Missing: Loss of bioluminescence.
FT   HELIX        17     30
FT   STRAND       35     39
FT   HELIX        40     53
FT   HELIX        59     75
FT   STRAND       83     85
FT   HELIX        86    105
FT   HELIX       111    123
FT   STRAND      128    131
FT   HELIX       133    142
FT   HELIX       149    159
FT   STRAND      165    167
FT   HELIX       169    180
FT   HELIX       190    193
SQ   SEQUENCE   196 AA;  22514 MW;  9AA5B636288A5B8F CRC64;
     MTSEQYSVKL TPDFDNPKWI GRHKHMFNFL DVNHNGRISL DEMVYKASDI VINNLGATPE
     QAKRHKDAVE AFFGGAGMKY GVETEWPEYI EGWKRLASEE LKRYSKNQIT LIRLWGDALF
     DIIDKDQNGA ISLDEWKAYT KSDGIIQSSE DCEETFRVCD IDESGQLDVD EMTRQHLGFW
     YTMDPACEKL YGGAVP
//