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\nCategory:American prison officersMolecular cloning and expression of a human endopeptidase-24.11, a novel member of the CD10 family.
\nHuman endopeptidase-24.11 (EP24.11) has been previously identified as a cell surface protein (termed MFI1) with adhesive and antiproliferative functions for adult T-cell leukemia cells. The cDNA for EP24.11 was cloned from the cDNA library of peripheral blood mononuclear cells (PBMC) of an adult T-cell leukemia patient. The gene is a single copy gene, and encodes a 2,217 amino acid protein with a predicted molecular mass of 250.26 kDa. The deduced amino acid sequence contains a glycosylation site and seven potential sites for N-linked glycosylation, thus the calculated molecular mass is approximately 246.5 kDa. The homology in amino acid sequence and domain organization to the CD10 family is most striking with about 15% and 20% identity at the amino acid and protein levels, respectively. The active site of EP24.11 is almost identical to that of CD10 as well as with the active site of the matrix metalloproteases and the protease furin. However, unlike other CD10 family members and matrix metalloproteases, EP24.11 cleaves Lys-Arg and other basic amino acid residues at a neutral pH. The 5′-flanking region of the gene contains typical elements for regulation by a variety of cytokines and growth factors including AP-1, NF-kappaB and serum response elements. Southern blot analysis suggests that the gene is a member of a multigene family.\/*
\n * Licensed under the Apache License, Version 2.0 (the “License”); you may not use this file except in compliance with
\n * the License. You may obtain a copy of the License at
\n *
\n *
\n *
\n * Unless required by applicable law or agreed
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