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    FEBS Lett. 1992 Dec 21;314(3):220-3.

    The amino acid sequence of a type I copper protein with an unusual serine- and hydroxyproline-rich C-terminal domain isolated from cucumber peelings.

    Mann K, Schäfer W, Thoenes U, Messerschmidt A, Mehrabian Z, Nalbandyan R.

    Max-Planck-Institut für Biochemie, Martinsried, Germany.

    We have determined the amino acid sequence of a small copper protein isolated from cucumber peelings. This cupredoxin contains 137 amino acids including a pyroglutamate as the first residue. The N-terminal 110 amino acid-long domain shows 30-37% identity to 2 other cupredoxins, stellacyanin and cucumber basic blue protein. A unique feature of this protein is a 27 amino acid-long C-terminal domain rich in 4-hydroxyproline and serine and resembling certain plant cell wall proteins. The prolines in this domain are hydroxylated to a different extent depending on the surrounding sequence.

    PMID: 1468551 [PubMed - indexed for MEDLINE]

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