Selected article for: "cooh terminal and cytoplasmic tail"
Title: Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans
  • Document date: 1991_12_2
    • ID: qrg1rtzi_1
    Snippet: Abstract. Golgi a-mannosidase II (G1cNAc transferase 1-dependent a1,3[a1,6] mannosidase, EC 3.2.1.114) catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures . We have isolated overlapping clones from a murine cDNA library encoding the full length a-mannosidase II open reading frame and most of the 5' and 3' untranslated region . The coding s.....
    Document: Abstract. Golgi a-mannosidase II (G1cNAc transferase 1-dependent a1,3[a1,6] mannosidase, EC 3.2.1.114) catalyzes the final hydrolytic step in the N-glycan maturation pathway acting as the committed step in the conversion of high mannose to complex type structures . We have isolated overlapping clones from a murine cDNA library encoding the full length a-mannosidase II open reading frame and most of the 5' and 3' untranslated region . The coding sequence predicts a type II transmembrane protein with a short cytoplasmic tail (five amino acids), a single transmembrane domain (21 amino acids), and a large COOH-terminal catalytic domain (1,124 amino acids) . This domain organization which is shared with the Golgi glycosyltransferases suggests that the common structural motifs may have a functional role in Golgi enzyme function or localization .

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