Adhesion G protein-coupled receptor E1 (CD97) (CD97)

Adhesion G protein-coupled receptor E1, commonly known as CD97, is a member of the adhesion GPCR family characterized by an extended extracellular region containing a GPCR autoproteolysis-inducing (GAIN) domain (UniProt P48960). The GAIN domain is critical for the receptor's maturation, as it facilitates self-cleavage at the GPCR proteolysis site (GPS) into an extracellular alpha-subunit and a seven-transmembrane beta-subunit (Araç et al., 2012). This cleavage exposes a tethered agonist sequence, known as the Stachel sequence, which triggers intracellular signaling upon mechanical or ligand-induced activation (Hamann et al., 2015). CD97 is widely expressed on leukocytes and is significantly upregulated in various solid tumors, where it promotes cell migration, invasion, and metastasis (Aust et al., 2016). Its primary ligands include CD55 (decay-accelerating factor) and chondroitin sulfate, which mediate cell-cell and cell-matrix interactions. Due to its role in tumor progression and inflammatory cell recruitment, CD97 and its GAIN domain are being investigated as therapeutic targets for cancer and chronic inflammatory diseases.

Other names

ADGRE1TM7LN1CD97 antigenGPCR autoproteolysis-inducing domain-containing protein

Inhibition of autoproteolysis, blockade of ligand binding (e.g., CD55), or antagonism of the tethered agonist (Stachel sequence).