Cells of monocytic differentiation can promote proteolytic activation of factor X following binding to the adhesive receptor Mac-1. We now show that the product, factor Xa, binds to a second receptor on these cells in a Ca2+-dependent reaction. Functionally, this results in the capacity to convert prothrombin to thrombin. The factor Xa receptor was identified by monoclonal antibody (7G12) reactive with plasma factor V/Va, but selected for reactivity with THP-1 cells. It reacted with 71.2 +/- 10.1% of monocytes, bound 153,600 +/- 33,500 sites/THP-1 cell, blocked binding of 125I-factor Xa, inhibited formation of thrombin, and immunoprecipitated 125I-factor Xa chemically cross-linked to its receptor on THP-1 cells. Following surface iodination or intrinsic labeling of THP-1 cells, antibody 7G12 immunoprecipitated a 74-kDa molecular species, similar to plasma factor Va light chain. Thus, monocytes and monocyte-like cells synthesize and express a factor V/Va-like receptor for factor Xa and organize a functional prothrombinase complex. The simultaneous membrane coexpression of a factor X receptor (Mac-1) and a factor Xa receptor as demonstrated by two-color flow cytofluorometric analysis of monocytes or THP-1 cells is consistent with a sequential receptor cascade for coordinated molecular assembly of coagulation proteins on specialized cells.