AEQ1_AEQVI
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 03-AUG-2022, entry version 112.
DE RecName: Full=Aequorin-1;
DE Flags: Precursor;
OS Aequorea victoria (Water jellyfish) (Mesonema victoria).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Leptothecata;
OC Aequoreidae; Aequorea.
OX NCBI_TaxID=6100;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 isotypes.";
RL Biochemistry 26:1326-1332(1987).
RN [2]
RP PROTEIN SEQUENCE OF 8-196.
RX PubMed=2866797; DOI=10.1021/bi00345a006;
RA Charbonneau H., Walsh K.A., McCann R.O., Prendergast F.G., Cormier M.J.,
RA 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 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+)-binding
RT photoprotein, aequorin.";
RL FEBS Lett. 295:63-66(1991).
RN [4]
RP PRELIMINARY DISULFIDE BOND.
RX 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 an
CC emission peak at 470 nm (blue light). Trace amounts of calcium ion
CC trigger the intramolecular oxidation of the chromophore, coelenterazine
CC into coelenteramide and CO(2) with the concomitant emission of light.
CC -!- PTM: The reduction of the disulfide bond is necessary to regenerate
CC aequorin from apoaequorin.
CC -!- BIOTECHNOLOGY: Aequorin is used as an intracellular Ca(2+) indicator.
CC Aequorin has a number of advantages over other Ca(2+) indicators, for
CC example, low leakage rate from cells, lack of intracellular
CC compartmentalization or sequestration and it does not disrupt cell
CC functions or embryo development.
CC -!- SIMILARITY: Belongs to the aequorin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have an internal disulfide bond.
CC {ECO:0000305|PubMed:8405461}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Aequorin entry;
CC URL="https://en.wikipedia.org/wiki/Aequorin";
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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 AlphaFoldDB; P07164; -.
DR SMR; P07164; -.
DR PRIDE; P07164; -.
DR KEGG; ag:AAA27716; -.
DR BioCyc; MetaCyc:MON-20288; -.
DR BRENDA; 1.13.12.24; 8923.
DR BRENDA; 1.13.12.5; 8923.
DR EvolutionaryTrace; P07164; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13202; EF-hand_5; 2.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
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; Metal-binding; Photoprotein; Repeat.
FT PROPEP 1..7
FT /evidence="ECO:0000269|PubMed:2866797"
FT /id="PRO_0000004126"
FT CHAIN 8..196
FT /note="Aequorin-1"
FT /id="PRO_0000004127"
FT DOMAIN 18..53
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 54..108
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 111..146
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 147..182
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 47..57
FT /note="May interact with the chromophore"
FT REGION 62..72
FT /note="May interact with the chromophore"
FT REGION 107..117
FT /note="May interact with the chromophore"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MUTAGEN 196
FT /note="Missing: Loss of bioluminescence."
FT /evidence="ECO:0000269|PubMed:1765170"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1SL8"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1SL8"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:1SL8"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:1SL8"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1SL8"
FT HELIX 86..105
FT /evidence="ECO:0007829|PDB:1SL8"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:1SL8"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1SL8"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:1SL8"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:1SL8"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1SL8"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:1SL8"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:1SL8"
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
