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Sequence of the cDNA encoding the Ca(2+)-activated photoprotein obelin from the hydroid polyp Obelia longissima.

Abstract
A cDNA clone encoding the Ca(2+)-activated photoprotein, obelin (Obl), from Obelia longissima was sequenced. The nucleotide (nt) sequence contained two long overlapping open reading frames (ORFs), one of which encoded apoobelin (apoObl). The deduced amino acid (aa) sequence of apoObl revealed that this 195-aa protein has three EF-hand structures that are characteristic for Ca(2+)-binding domains. Strong aa homology was shown among apoObl, apoaequorin and apoclytin. The second ORF present in the obl cDNA consists of 139 codons and encodes a very basic protein with a calculated pI of 10.56 and a molecular mass of 16,153 Da.
AuthorsB A Illarionov, V S Bondar, V A Illarionova, E S Vysotski
JournalGene (Gene) Vol. 153 Issue 2 Pg. 273-4 (Feb 14 1995) ISSN: 0378-1119 [Print] Netherlands
PMID7875600 (Publication Type: Journal Article)
Chemical References
  • Apoproteins
  • Calcium-Binding Proteins
  • DNA, Complementary
  • Luminescent Proteins
  • Recombinant Proteins
  • apoaequorin
  • obelin
  • phialidin
  • Aequorin
Topics
  • Aequorin (genetics)
  • Animals
  • Apoproteins (chemistry, genetics)
  • Calcium-Binding Proteins (chemistry, genetics)
  • Cloning, Molecular
  • DNA, Complementary (genetics)
  • Hydra (genetics)
  • Luminescent Proteins (chemistry, genetics)
  • Molecular Sequence Data
  • Open Reading Frames (genetics)
  • Recombinant Proteins (genetics)
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid

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