@article{e2bffe9099fa11dd86a6000ea68e967b,
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.",
author = "Cowell, {G M} and E K{\o}nigsh{\o}fer and Danielsen, {E M} and Hansen, {O C} and J Engberg and W Hunziker and J{\o}rgen Olsen and Jette M{\o}ller and Lotte Laustsen and Welinder, {K G}",
note = "Keywords: Amino Acid Sequence; Aminopeptidases; Animals; Antigens, CD13; Base Sequence; Catalysis; Cloning, Molecular; Codon; DNA; Escherichia coli; Humans; Intestines; Molecular Sequence Data; Nucleic Acid Hybridization; Protein Biosynthesis; RNA, Messenger; Rabbits; Sequence Homology, Nucleic Acid; Swine",
year = "1988",
language = "English",
volume = "238",
pages = "307--14",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "2",
}