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ECB-ART-31497
Biochim Biophys Acta 1991 May 30;10781:63-7. doi: 10.1016/0167-4838(91)90093-f.
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Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola.

Mauri F , Omnaas J , Davidson L , Whitfill C , Kitto GB .


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Coelomic cells from the sea cucumber Caudina (Molpadia) arenicola contain four major globins, A, B, C and D. The hemoglobins from this organism show unusual ligand-linked dissociation properties. The complete amino acid sequence of the D globin has been established. It is N-acetylated, consists of 158 residues and has a 10 amino acid N-terminal extension similar to that found in some other invertebrate globins. The C. arenicola D globin has an equal sequence identity (28%) with both alpha and beta human globins and as anticipated, is more closely related to these vertebrate proteins than are molluscan globins. The C. arenicola D globin shows a 59% identity with the globin I from the sea cucumber Paracaudina chilensis. The availability of the C. arenicola D globin sequence will aid the X-ray analysis of this protein and facilitate an understanding of the changes in subunit interactions that occur with cooperative ligand binding.

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Genes referenced: LOC100887844