Cloning, expression and sequence analysis of cDNA for the Ca(2+)-binding photoprotein, mitrocomin.
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.
Fagan
T F
TF
Osaka Bioscience Institute, Japan.
Ohmiya
Y
Y
Blinks
J R
JR
Inouye
S
S
Tsuji
F I
FI
D000331:Aequorin / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002135:Calcium-Binding Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D003001:Cloning, Molecular / Q000379:methods; D016384:Consensus Sequence; D018076:DNA, Complementary / Q000737:chemistry* / Q000235:genetics; D049449:Luminescence; D008164:Luminescent Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D015183:Restriction Mapping; D037401:Scyphozoa / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
D002135:Calcium-Binding Proteins; D018076:DNA, Complementary; D008164:Luminescent Proteins; D011994:Recombinant Proteins; C083952:mitrocomin protein, Mitrocoma celluria; C046165:phialidin; D000331:Aequorin