AEQ2_AEQVI
ID AEQ2_AEQVI Reviewed; 196 AA.
AC P02592;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Aequorin-2;
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=3858813; DOI=10.1073/pnas.82.10.3154;
RA Inouye S., Noguchi M., Sakaki Y., Takagi Y., Miyata T., Iwanaga S.,
RA Miyata T., Tsuji F.I.;
RT "Cloning and sequence analysis of cDNA for the luminescent protein
RT aequorin.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:3154-3158(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-185 (AEQUORIN 2 AND 3).
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 [3]
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 [4]
RP MUTAGENESIS.
RX PubMed=16593774; DOI=10.1073/pnas.83.21.8107;
RA Tsuji F.I., Inouye S., Goto T., Sakaki Y.;
RT "Site-specific mutagenesis of the calcium-binding photoprotein aequorin.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8107-8111(1986).
RN [5]
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 [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10830969; DOI=10.1038/35012659;
RA Head J.F., Inouye S., Teranishi K., Shimomura O.;
RT "The crystal structure of the photoprotein aequorin at 2.3-A resolution.";
RL Nature 405:372-376(2000).
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 -!- SIMILARITY: Belongs to the aequorin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have an internal disulfide bond.
CC {ECO:0000305|PubMed:8405461}.
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DR EMBL; L29571; AAA27720.1; -; mRNA.
DR EMBL; M16104; AAA27717.1; -; mRNA.
DR EMBL; M16105; AAA27718.1; -; mRNA.
DR EMBL; M11394; AAA27719.1; -; mRNA.
DR PIR; A03020; AQJFNV.
DR PDB; 1EJ3; X-ray; 2.30 A; A/B=9-196.
DR PDB; 1UHH; X-ray; 1.80 A; A/B=9-196.
DR PDB; 1UHI; X-ray; 1.80 A; A/B=9-196.
DR PDB; 1UHJ; X-ray; 1.80 A; A/B=9-196.
DR PDB; 1UHK; X-ray; 1.60 A; A/B=9-196.
DR PDB; 5ZAB; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=9-196.
DR PDB; 7EG2; X-ray; 2.22 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=9-196.
DR PDB; 7EG3; X-ray; 2.09 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=9-196.
DR PDBsum; 1EJ3; -.
DR PDBsum; 1UHH; -.
DR PDBsum; 1UHI; -.
DR PDBsum; 1UHJ; -.
DR PDBsum; 1UHK; -.
DR PDBsum; 5ZAB; -.
DR PDBsum; 7EG2; -.
DR PDBsum; 7EG3; -.
DR AlphaFoldDB; P02592; -.
DR BMRB; P02592; -.
DR SMR; P02592; -.
DR KEGG; ag:AAA27720; -.
DR BRENDA; 1.13.12.24; 8923.
DR EvolutionaryTrace; P02592; -.
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_0000004128"
FT CHAIN 8..196
FT /note="Aequorin-2"
FT /id="PRO_0000004129"
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|PubMed:10830969"
FT DOMAIN 117..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 SITE 196
FT /note="Required for bioluminescence"
FT VARIANT 70..71
FT /note="EA -> GD (in aequorin-3)"
FT VARIANT 164
FT /note="S -> N (in aequorin-3)"
FT MUTAGEN 36
FT /note="G->R: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:16593774"
FT MUTAGEN 65
FT /note="H->F: 100% activity loss."
FT /evidence="ECO:0000269|PubMed:16593774"
FT MUTAGEN 129
FT /note="G->R: 51% activity loss."
FT /evidence="ECO:0000269|PubMed:16593774"
FT MUTAGEN 152
FT /note="C->R: 52% activity loss."
FT /evidence="ECO:0000269|PubMed:16593774"
FT MUTAGEN 152
FT /note="C->S: 33% activity loss."
FT /evidence="ECO:0000269|PubMed:16593774"
FT MUTAGEN 159
FT /note="C->S: 41% activity loss."
FT /evidence="ECO:0000269|PubMed:16593774"
FT MUTAGEN 165
FT /note="G->R: No activity loss."
FT /evidence="ECO:0000269|PubMed:16593774"
FT MUTAGEN 187
FT /note="C->S: 71% activity loss."
FT /evidence="ECO:0000269|PubMed:16593774"
FT MUTAGEN 196
FT /note="Missing: Loss of bioluminescence."
FT /evidence="ECO:0000269|PubMed:1765170"
FT CONFLICT 37
FT /note="K -> R (in Ref. 2; AAA27717)"
FT /evidence="ECO:0000305"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1UHK"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1UHK"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:1UHK"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:1UHK"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1UHK"
FT HELIX 86..105
FT /evidence="ECO:0007829|PDB:1UHK"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:1UHK"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1UHK"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:1UHK"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:1UHK"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:1UHK"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1UHK"
FT TURN 188..193
FT /evidence="ECO:0007829|PDB:1UHK"
SQ SEQUENCE 196 AA; 22285 MW; 532DC7A9D29BA80C CRC64;
MTSKQYSVKL TSDFDNPRWI GRHKHMFNFL DVNHNGKISL DEMVYKASDI VINNLGATPE
QAKRHKDAVE AFFGGAGMKY GVETDWPAYI EGWKKLATDE LEKYAKNEPT LIRIWGDALF
DIVDKDQNGA ITLDEWKAYT KAAGIIQSSE DCEETFRVCD IDESGQLDVD EMTRQHLGFW
YTMDPACEKL YGGAVP
