OBL_OBELO
ID OBL_OBELO Reviewed; 195 AA.
AC Q27709;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Obelin;
DE Short=OBL;
DE Flags: Precursor;
OS Obelia longissima (Black sea hydrozoan) (Laomedea longissima).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Leptothecata;
OC Obeliida; Obeliidae; Obelia.
OX NCBI_TaxID=32570;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7875600; DOI=10.1016/0378-1119(94)00797-v;
RA Illarionov B.A., Bondar V.S., Illarionova V.A., Vysotski E.S.;
RT "Sequence of the cDNA encoding the Ca(2+)-activated photoprotein obelin
RT from the hydroid polyp Obelia longissima.";
RL Gene 153:273-274(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS).
RX PubMed=11152120; DOI=10.1110/ps.9.11.2085;
RA Liu Z.J., Vysotski E.S., Chen C.J., Rose J.P., Lee J., Wang B.C.;
RT "Structure of the Ca2+-regulated photoprotein obelin at 1.7 A resolution
RT determined directly from its sulfur substructure.";
RL Protein Sci. 9:2085-2093(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
RX PubMed=14592432; DOI=10.1016/j.bbrc.2003.09.231;
RA Liu Z.J., Vysotski E.S., Deng L., Lee J., Rose J., Wang B.C.;
RT "Atomic resolution structure of obelin: soaking with calcium enhances
RT electron density of the second oxygen atom substituted at the C2-position
RT of coelenterazine.";
RL Biochem. Biophys. Res. Commun. 311:433-439(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS), AND MUTAGENESIS OF TRP-92.
RX PubMed=15155735; DOI=10.1074/jbc.m402427200;
RA Deng L., Markova S.V., Vysotski E.S., Liu Z.J., Lee J., Rose J., Wang B.C.;
RT "Crystal structure of a Ca2+-discharged photoprotein: implications for
RT mechanisms of the calcium trigger and bioluminescence.";
RL J. Biol. Chem. 279:33647-33652(2004).
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 -!- SIMILARITY: Belongs to the aequorin family. {ECO:0000305}.
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DR EMBL; U07128; AAA67708.1; -; mRNA.
DR PDB; 1EL4; X-ray; 1.73 A; A=1-195.
DR PDB; 1JF0; X-ray; 1.82 A; A=1-195.
DR PDB; 1JF2; X-ray; 1.72 A; A=1-195.
DR PDB; 1QV0; X-ray; 1.10 A; A=1-195.
DR PDB; 1QV1; X-ray; 1.10 A; A=1-195.
DR PDB; 1S36; X-ray; 1.96 A; A=1-195.
DR PDB; 1SL7; X-ray; 2.20 A; A=1-195.
DR PDB; 1SL9; X-ray; 1.17 A; A=1-195.
DR PDB; 2F8P; X-ray; 1.93 A; A=1-195.
DR PDB; 4MRX; X-ray; 1.72 A; A=1-195.
DR PDB; 4MRY; X-ray; 1.30 A; A=1-195.
DR PDB; 4N1F; X-ray; 2.09 A; A=1-195.
DR PDB; 4N1G; X-ray; 1.50 A; A/B=1-195.
DR PDB; 7O3U; X-ray; 1.80 A; A=1-195.
DR PDBsum; 1EL4; -.
DR PDBsum; 1JF0; -.
DR PDBsum; 1JF2; -.
DR PDBsum; 1QV0; -.
DR PDBsum; 1QV1; -.
DR PDBsum; 1S36; -.
DR PDBsum; 1SL7; -.
DR PDBsum; 1SL9; -.
DR PDBsum; 2F8P; -.
DR PDBsum; 4MRX; -.
DR PDBsum; 4MRY; -.
DR PDBsum; 4N1F; -.
DR PDBsum; 4N1G; -.
DR PDBsum; 7O3U; -.
DR AlphaFoldDB; Q27709; -.
DR SMR; Q27709; -.
DR MINT; Q27709; -.
DR BRENDA; 1.13.12.24; 15411.
DR EvolutionaryTrace; Q27709; -.
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; PF00036; EF-hand_1; 1.
DR Pfam; PF13202; EF-hand_5; 1.
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; Luminescence; Metal-binding; Photoprotein; Repeat.
FT PROPEP 1..6
FT /evidence="ECO:0000255"
FT /id="PRO_0000004136"
FT CHAIN 7..195
FT /note="Obelin"
FT /id="PRO_0000004137"
FT DOMAIN 17..52
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 53..88
FT /note="EF-hand 2"
FT /evidence="ECO:0000250|UniProtKB:P02592"
FT DOMAIN 110..145
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 146..181
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MUTAGEN 92
FT /note="W->F: Shifts luminescence to violet by adding a new
FT band at 410 nm."
FT /evidence="ECO:0000269|PubMed:15155735"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4N1G"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:1QV0"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1SL9"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:1QV0"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1QV0"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:1QV0"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1S36"
FT HELIX 85..104
FT /evidence="ECO:0007829|PDB:1QV0"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:1QV0"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:4MRY"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:1QV0"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4N1G"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1QV0"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4MRY"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:1QV0"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1QV0"
FT TURN 187..192
FT /evidence="ECO:0007829|PDB:1QV0"
SQ SEQUENCE 195 AA; 22226 MW; 5D002270B73D3663 CRC64;
MSSKYAVKLK TDFDNPRWIK RHKHMFDFLD INGNGKITLD EIVSKASDDI CAKLEATPEQ
TKRHQVCVEA FFRGCGMEYG KEIAFPQFLD GWKQLATSEL KKWARNEPTL IREWGDAVFD
IFDKDGSGTI TLDEWKAYGK ISGISPSQED CEATFRHCDL DNSGDLDVDE MTRQHLGFWY
TLDPEADGLY GNGVP
