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Discoidin, CUB and LCCL domain-containing protein 1 (DCBLD1) is a single-pass type I transmembrane scaffolding receptor that contains extracellular discoidin, CUB, and LCCL domains, and a cytoplasmic region with phosphorylation sites and scaffolding motifs[1][2][3]. DCBLD1 is part of a family with DCBLD2, both implicated as putative receptors involved in vertebrate development and cancer. Although DCBLD1 is considered an orphan receptor (no clearly identified ligand), it is predicted to mediate signal transduction through its cytoplasmic domain, engaged by Src homology 2 (SH2) domain-containing adaptors after phosphorylation by the nonreceptor tyrosine kinases FYN and ABL. The protein modulates signaling by and possibly interacts with major receptor tyrosine kinases, influencing multiple biological functions (cell motility, morphogenesis, and response to growth factors)[1][2][3]. DCBLD1 is broadly expressed and localizes to the plasma membrane, and it is evolutionarily conserved with paralogs and orthologs present in vertebrates. Although direct drug interactors and clinical biomarkers have not yet been established, its role in cancer and cell signaling suggests potential as a therapeutic or diagnostic target[1][3].
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