Abstract
The primary structure of mitrocomin consists of 190 amino acid residues, with three Ca(2+)-binding sites and a tyrosine residue at the C-terminus. Mitrocomin shows an amino acid sequence homology of 67.9% and 60.7% when compared with aequorin and clytin, respectively. The amino acid residues Cys152, His58, His169, Trp12, Trp86, Trp108, Trp129 and Trp173 are conserved in all three photoproteins, suggesting that they play a role in light emission.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Aequorin / chemistry
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Amino Acid Sequence
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Animals
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Base Sequence
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Calcium-Binding Proteins / biosynthesis*
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Calcium-Binding Proteins / chemistry
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Calcium-Binding Proteins / genetics
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Cloning, Molecular / methods
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Consensus Sequence
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DNA, Complementary / chemistry*
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DNA, Complementary / genetics
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Luminescence
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Luminescent Proteins / biosynthesis*
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Luminescent Proteins / chemistry
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Luminescent Proteins / genetics
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Molecular Sequence Data
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Restriction Mapping
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Scyphozoa / genetics
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Scyphozoa / metabolism*
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Sequence Homology, Amino Acid
Substances
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Calcium-Binding Proteins
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DNA, Complementary
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Luminescent Proteins
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Recombinant Proteins
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mitrocomin protein, Mitrocoma celluria
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phialidin
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Aequorin