CD10 (Common Acute Lymphocytic Leukemia Antigen, CALLA), is a cell surface enzyme with neutral metalloendopeptidase activity which inactivates a variety of biologically active peptides. CD10 is expressed on the cells of lymphoblastic, Burkitt's, and follicular germinal center lymphomas, immature B cells with in adult bone marrow and on cells from patients with chronic myelocytic leukemia (CML). CD10 is also present on breast myoepithelial cells, bile canaliculi, fibroblasts, with especially high expression on the brush border of kidney and gut epithelial cells. CD10 is a neutral endopeptidase that cleaves peptides at the amino side of hydrophobic residues and inactivates several peptide hormones including glucagon, enkephalins, substance P, neurotensin, oxytocin, and bradykinin. Further, CD10 is a 100 kDa type II transmembrane glycoprotein that exists in a single copy of greater than 45 kb. The 5' untranslated region of the CD10 gene is alternatively spliced, resulting in four separate mRNA transcripts and the coding region is not affected by alternative splicing. Diseases associated with CD10 dysfunction include spinocerebellar ataxia 43 and Charcot-Marie tooth Disease.
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Protein Aliases: Atriopeptidase; CALLA; CD10; Common acute lymphocytic leukemia antigen; Enkephalinase; membrane metallo-endopeptidase (neutral endopeptidase, enkephalinase, CALLA, CD10); membrane metallo-endopeptidase variant 1; membrane metallo-endopeptidase variant 2; NEP; Neprilysin; neprilysin-390; neprilysin-411; Neutral endopeptidase 24.11; SFE; Skin fibroblast elastase
Gene Aliases: CALLA; CD10; CMT2T; EPN; MME; NEP; SFE
UniProt ID: (Human) P08473
Entrez Gene ID: (Human) 4311
Molecular Function: metalloprotease