title: Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.
abstract: The complete primary structure (967 amino acids) of an intestinal human aminopeptidase N (EC 3.4.11.2) was deduced from the sequence of a cDNA clone. Aminopeptidase N is anchored to the microvillar membrane via an uncleaved signal for membrane insertion. A domain constituting amino acid 250-555 positioned within the catalytic domain shows very clear homology to E. coli aminopeptidase N and contains Zn2+ ligands. Therefore these residues are part of the active site. However, no homology of the anchor/junctional peptide domain is found suggesting that the juxta- and intra-membraneous parts of the molecule have been added/preserved during development. It is speculated that this part carries the apical address.
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000235:genetics; D000818:Animals; D001483:Base Sequence; D018826:CD13 Antigens; D002384:Catalysis; D003001:Cloning, Molecular; D003062:Codon; D004247:DNA / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006801:Humans; D007422:Intestines / Q000201:enzymology*; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics; D011817:Rabbits; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
chemical_list: D003062:Codon; D012333:RNA, Messenger; D004247:DNA; D000626:Aminopeptidases; D018826:CD13 Antigens