Innate immune receptors induce activation of conventional dendritic cells (cDCs) and enhance antigen (cross-)presentation, favoring immune responses. DNGR-1 (CLEC9A), a receptor expressed by type 1 cDCs (cDC1s) and implicated in immunity to viruses and cancers, recognizes F-actin exposed on dead cell remnants and promotes cross-presentation of associated antigens. Here, we show that DNGR-1 does not trigger cDC1 activation, in part by recruiting phosphatase SHIP1, a process governed by a single amino acid adjacent to the signaling motif of the receptor. Substituting this residue converts DNGR-1 into an activating receptor but decreases its induction of cross-presentation of dead cell-associated antigens. Interestingly, introducing the reverse mutation into related receptor Dectin-1 impairs its activation capacity while enhancing its ability to promote cross-presentation. These findings reveal an unexpected functional trade-off in receptor signaling and suggest that DNGR-1 has evolved to prioritize antigen cross-presentation over cellular activation, possibly to minimize inflammatory responses to dead cells.