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Obelin (OBL)

 OBL_OBELO               Reviewed;         195 AA.
Q27709;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
07-NOV-2018, entry version 92.
RecName: Full=Obelin;
Short=OBL;
Flags: Precursor;
Obelia longissima (Black sea hydrozoan) (Laomedea longissima).
Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Leptothecata;
Campanulariidae; Obelia.
NCBI_TaxID=32570;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7875600; DOI=10.1016/0378-1119(94)00797-V;
Illarionov B.A., Bondar V.S., Illarionova V.A., Vysotski E.S.;
"Sequence of the cDNA encoding the Ca(2+)-activated photoprotein
obelin from the hydroid polyp Obelia longissima.";
Gene 153:273-274(1995).
[2]
X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS).
PubMed=11152120; DOI=10.1110/ps.9.11.2085;
Liu Z.J., Vysotski E.S., Chen C.J., Rose J.P., Lee J., Wang B.C.;
"Structure of the Ca2+-regulated photoprotein obelin at 1.7 A
resolution determined directly from its sulfur substructure.";
Protein Sci. 9:2085-2093(2000).
[3]
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
PubMed=14592432; DOI=10.1016/j.bbrc.2003.09.231;
Liu Z.J., Vysotski E.S., Deng L., Lee J., Rose J., Wang B.C.;
"Atomic resolution structure of obelin: soaking with calcium enhances
electron density of the second oxygen atom substituted at the C2-
position of coelenterazine.";
Biochem. Biophys. Res. Commun. 311:433-439(2003).
[4]
X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS), AND MUTAGENESIS OF TRP-92.
PubMed=15155735; DOI=10.1074/jbc.M402427200;
Deng L., Markova S.V., Vysotski E.S., Liu Z.J., Lee J., Rose J.,
Wang B.C.;
"Crystal structure of a Ca2+-discharged photoprotein: implications for
mechanisms of the calcium trigger and bioluminescence.";
J. Biol. Chem. 279:33647-33652(2004).
-!- FUNCTION: Ca(2+)-dependent bioluminescence photoprotein. Displays
an emission peak at 470 nm (blue light). Trace amounts of calcium
ion trigger the intramolecular oxidation of the chromophore,
coelenterazine into coelenteramide and CO(2) with the concomitant
emission of light.
-!- SIMILARITY: Belongs to the aequorin family. {ECO:0000305}.
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EMBL; U07128; AAA67708.1; -; mRNA.
PDB; 1EL4; X-ray; 1.73 A; A=1-195.
PDB; 1JF0; X-ray; 1.82 A; A=1-195.
PDB; 1JF2; X-ray; 1.72 A; A=1-195.
PDB; 1QV0; X-ray; 1.10 A; A=1-195.
PDB; 1QV1; X-ray; 1.10 A; A=1-195.
PDB; 1S36; X-ray; 1.96 A; A=1-195.
PDB; 1SL7; X-ray; 2.20 A; A=1-195.
PDB; 1SL9; X-ray; 1.17 A; A=1-195.
PDB; 2F8P; X-ray; 1.93 A; A=1-195.
PDB; 4MRX; X-ray; 1.72 A; A=1-195.
PDB; 4MRY; X-ray; 1.30 A; A=1-195.
PDB; 4N1F; X-ray; 2.09 A; A=1-195.
PDB; 4N1G; X-ray; 1.50 A; A/B=1-195.
PDBsum; 1EL4; -.
PDBsum; 1JF0; -.
PDBsum; 1JF2; -.
PDBsum; 1QV0; -.
PDBsum; 1QV1; -.
PDBsum; 1S36; -.
PDBsum; 1SL7; -.
PDBsum; 1SL9; -.
PDBsum; 2F8P; -.
PDBsum; 4MRX; -.
PDBsum; 4MRY; -.
PDBsum; 4N1F; -.
PDBsum; 4N1G; -.
ProteinModelPortal; Q27709; -.
SMR; Q27709; -.
MINT; Q27709; -.
EvolutionaryTrace; Q27709; -.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR039647; EF_hand_pair_protein_CML-like.
PANTHER; PTHR10891; PTHR10891; 1.
Pfam; PF00036; EF-hand_1; 1.
Pfam; PF13202; EF-hand_5; 1.
SMART; SM00054; EFh; 3.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 3.
PROSITE; PS50222; EF_HAND_2; 3.
1: Evidence at protein level;
3D-structure; Calcium; Luminescence; Metal-binding; Photoprotein;
Repeat.
PROPEP 1 6 {ECO:0000255}.
/FTId=PRO_0000004136.
CHAIN 7 195 Obelin.
/FTId=PRO_0000004137.
DOMAIN 17 52 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 53 88 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 110 145 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 146 181 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 30 41 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 123 134 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 159 170 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
MUTAGEN 92 92 W->F: Shifts luminescence to violet by
adding a new band at 410 nm.
{ECO:0000269|PubMed:15155735}.
HELIX 3 5 {ECO:0000244|PDB:4N1G}.
HELIX 16 29 {ECO:0000244|PDB:1QV0}.
STRAND 33 35 {ECO:0000244|PDB:1SL9}.
HELIX 39 48 {ECO:0000244|PDB:1QV0}.
HELIX 50 53 {ECO:0000244|PDB:1QV0}.
HELIX 58 74 {ECO:0000244|PDB:1QV0}.
STRAND 82 84 {ECO:0000244|PDB:1S36}.
HELIX 85 104 {ECO:0000244|PDB:1QV0}.
HELIX 110 121 {ECO:0000244|PDB:1QV0}.
STRAND 125 131 {ECO:0000244|PDB:4MRY}.
HELIX 132 142 {ECO:0000244|PDB:1QV0}.
STRAND 143 145 {ECO:0000244|PDB:4N1G}.
HELIX 148 157 {ECO:0000244|PDB:1QV0}.
STRAND 164 166 {ECO:0000244|PDB:4MRY}.
HELIX 168 179 {ECO:0000244|PDB:1QV0}.
HELIX 184 186 {ECO:0000244|PDB:1QV0}.
TURN 187 192 {ECO:0000244|PDB:1QV0}.
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


Related products :

Catalog number Product name Quantity
L001-100UG Recombinant Obelin (100 ìg) 100 µg
L001-50UG Recombinant Obelin (50 μg)
L001-100UG Recombinant Obelin 100
L001-50UG Recombinant Obelin 50 μg
L001-100UG Recombinant Obelin (100 μg) 100
L001-100UG Recombinant Obelin (100 μg) 100
L001-50UG Recombinant Obelin (50 μg)
L001-50UG Recombinant Obelin (50 ìg)
X008-5ML Obelin Conjugate Diluent, 5 mL 5 pack
X008-5ML Obelin Conjugate Diluent, 5 mL 1 pack
X006-100ML Obelin Trigger Solution, 100 mL 5 pack
X006-15ML Obelin Trigger Solution, 15 mL 1 pack
X006-100ML Obelin Trigger Solution, 100 mL 1 pack
L001-100UG Recombinant Obelin (100 μg) Reagent 100
L001-50UG Recombinant Obelin (50 μg) Reagent
L001-100UG Reagent Recombinant Obelin (100 μg) 100
L001-50UG Reagent Recombinant Obelin (50 μg) 50 ug
L001-100UG Recombinant Obelin (100 μg), Reagent 100
X006-15ML Obelin Trigger Solution, 15 mL 5 pack
L001-50UG Recombinant Obelin (50 μg), Reagent


 

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