Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N.

Article Details

Citation

Look AT, Ashmun RA, Shapiro LH, Peiper SC

Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N.

J Clin Invest. 1989 Apr;83(4):1299-307.

PubMed ID
2564851 [ View in PubMed
]
Abstract

To determine the primary structure of CD13, a 150-kD cell surface glycoprotein originally identified on subsets of normal and malignant human myeloid cells, we isolated the complete sequences encoding the polypeptide in overlapping complementary DNA (cDNA) clones. The authenticity of our cDNA clones was demonstrated by the ability of the coding sequences, subcloned in a retroviral expression vector, to mediate expression of bona fide CD13 molecules at the surface of transfected mouse fibroblasts. The nucleotide sequence predicts a 967 amino acid integral membrane protein with a single, 24 amino acid hydrophobic segment near the amino terminus. Amino-terminal protein sequence analysis of CD13 molecules indicated that the hydrophobic segment is not cleaved, but rather serves as both a signal for membrane insertion and as a stable membrane-spanning segment. The remainder of the molecule consists of a large extracellular carboxyterminal domain, which contains a pentapeptide consensus sequence characteristic of members of the zinc-binding metalloprotease superfamily. Sequence comparisons with known enzymes of this class revealed that CD13 is identical to aminopeptidase N, a membrane-bound glycoprotein thought to be involved in the metabolism of regulatory peptides by diverse cell types, including small intestinal and renal tubular epithelial cells, macrophages, granulocytes, and synaptic membranes prepared from cells of the central nervous system.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Aminopeptidase NP15144Details