Cloning, expression and sequence analysis of cDNA for the Ca(2+)-binding photoprotein, mitrocomin

FEBS Lett. 1993 Nov 1;333(3):301-5. doi: 10.1016/0014-5793(93)80675-k.

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

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aequorin / chemistry
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Calcium-Binding Proteins / biosynthesis*
  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / genetics
  • Cloning, Molecular / methods
  • Consensus Sequence
  • DNA, Complementary / chemistry*
  • DNA, Complementary / genetics
  • Luminescence
  • Luminescent Proteins / biosynthesis*
  • Luminescent Proteins / chemistry
  • Luminescent Proteins / genetics
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Restriction Mapping
  • Scyphozoa / genetics
  • Scyphozoa / metabolism*
  • Sequence Homology, Amino Acid

Substances

  • Calcium-Binding Proteins
  • DNA, Complementary
  • Luminescent Proteins
  • Recombinant Proteins
  • mitrocomin protein, Mitrocoma celluria
  • phialidin
  • Aequorin