title: Cloning and sequence analysis of cDNA for the Ca(2+)-activated photoprotein, clytin.
abstract: Clytin is a member of the aequorin family of photoproteins. It is made up of 189 amino acid residues, contains 3 Ca(2+)-binding sites, and shows 62% homology in amino acid residues to those in aequorin. The cysteine, tryptophan, and histidine residues, and the C-terminal proline, that are conserved in aequorin and clytin may be involved in the Ca(2+)-activated bioluminescence of the two proteins. Clytin may also prove useful in the determination of Ca2+.
authors.affiliation: Marine Biology Research Division 0202, Scripps Institution of Oceanography, University of California, San Diego, La Jolla 92093.
authors.forename: S
authors.initials: S
authors.lastname: Inouye
authors.forename: F I
authors.initials: FI
authors.lastname: Tsuji
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D002413:Cations, Divalent; D003001:Cloning, Molecular; D004247:DNA; D004926:Escherichia coli; D008164:Luminescent Proteins / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data
chemical_list: D002413:Cations, Divalent; D008164:Luminescent Proteins; C046165:phialidin; D004247:DNA; D002118:Calcium