Determination of the mRNA sequence of cathepsin Y, a cysteine endopeptidase from rat spleen, 1 and confirmation of its ubiquitous expression.
A cysteine endopeptidase from rat spleen was purified, characterized and its gene cloned. This enzyme was originally recognized by its action of producing kinin-potentiating peptide from a plasma protein. We named it cathepsin Y due to its localization, acidic pH optimum and the presence of the same set of active site amino acids as in other thiol cathepsins. Here we show the total sequence of the mRNA obtained by means of TaKaRa 5' Full RACE Core Set and complete the previously reported sequence. This completion of the mRNA sequence resulted in the omission of the strangely attached C-terminal peptide from cathepsin Y.
Nakazono
Eri
E
Division of Food and Nutrition, Nakamura Gakuen University, Befu 5-7-1, Jonan-ku, Fukuoka 814-0198, Japan.
Kamata
Yoriko
Y
Yamafuji
Keiko
K
D000595:Amino Acid Sequence; D000818:Animals; D002403:Cathepsins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D003546:Cysteine Endopeptidases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D018076:DNA, Complementary / Q000096:biosynthesis / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic / Q000235:genetics*; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000737:chemistry*; D051381:Rats; D013154:Spleen / Q000737:chemistry*; D014018:Tissue Distribution
D018076:DNA, Complementary; D012333:RNA, Messenger; D002403:Cathepsins; D003546:Cysteine Endopeptidases; C404516:cathepsin Y