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 27-MAR-2024, entry version 110. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8A9S; X-ray; 2.10 A; A/B=1-195. DR PDB; 8C6O; X-ray; 2.20 A; A/B=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 PDBsum; 8A9S; -. DR PDBsum; 8C6O; -. 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 Gene3D; 1.10.238.10; EF-hand; 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; 1. DR Pfam; PF13499; EF-hand_7; 1. DR SMART; SM00054; EFh; 3. DR SUPFAM; SSF47473; EF-hand; 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 STRAND 6..8 FT /evidence="ECO:0007829|PDB:8A9S" 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:7O3U" 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 //