Identification of the human PMR1 mRNA endonuclease as an alternatively processed product of the gene for peroxidasin-like protein

Relationship of PXDNL to xPMR1. (A) The full-length PXDNL protein is shown schematically with relative positioning of the functional domains of the full-length protein. Beneath this, the peroxidase domain is expanded to show the relative positioning of sequence elements that are conserved between the 57-kDa form of PXDNL and xPMR1. (B) The sequence of the 57-kDa form of PXDNL is aligned with that of the 60-kDa form of xPMR1 (xPMR60), with matching residues based on similarities with xPMR1. The sequence of xPMR1 does not start with methionine because it is generated by proteolytic cleavage from a larger precursor. In this figure, identical amino acids are shaded, the binding site for c-Src is shown in yellow, the active site histidines are shown in blue, and the tyrosine phosphorylation site is shown in red.