Lipid-binding protein required for SHH long-range signaling by binding to the dually lipid-modified SHH (ShhNp) and by promoting ShhNp mobilization, solubilization and release from the cell membrane (PubMed:22902404, PubMed:22677548). Acts by enhancing the proteolytic processing (shedding) of the lipid-modified N- and C- terminal of ShhNp at the cell surface (PubMed:24522195). Synergizes with DISP1 to increase SHH secretion (PubMed:22902404). Probable cell surface coreceptor for VEGFR2 involved in VEGFR2-mediated angiogenesis (PubMed:27834687). Forms homooligomers. Forms heterooligomers with SCUBE1. Forms heterooligomers with SCUBE3 (PubMed:33308444). Interacts with SHH via the cholesterol anchor of the dually lipid-modified SHH (ShhNp) (PubMed:19480626, PubMed:22902404). Interacts with PTCH1 (PubMed:19480626, PubMed:22902404). Interacts with VEGFR2 (PubMed:27834687). Secreted and tethered at the cell surface (PubMed:19480626). Expressed in a broad spectrum of adult tissues (PubMed:12270931). The CUB domain is important for the interaction with the cholesterol-anchor of SHH. The CUB domain regulates protease recruitment and activation during SHH shedding. N-glycosylated. It is unclear how SCUBE2 binds the dilipidated SHH. According to a report, the SHH cholesterol-anchor, but not palmitate, seems to be both necessary and sufficient for SCUBE2-mediated SHH release from the cell membrane (PubMed:22902404). According to a second paper, palmitoylation accelerates the rate of SCUBE2-mediated release (PubMed:22677548). Cholesterol modification is sufficient for a heterologous protein to bind to SCUBE2 and to be secreted in a SCUBE2-dependent manner (PubMed:22902404).