YIPF3 (Yip1 domain family member 3) is a five-pass transmembrane protein that primarily localizes to the cis-Golgi apparatus and plays crucial roles in Golgi maintenance and selective autophagy 12. The protein functions as part of a heterodimeric complex with YIPF4, which serves as a novel Golgiphagy receptor that facilitates the selective degradation of Golgi compartments through autophagy 34. YIPF3 contains an LC3-interacting region (LIR) motif that enables direct binding to mammalian Atg8-family proteins (LC3B, GABARAP, and GABARAPL1), with this interaction regulated by phosphorylation sites upstream of the LIR motif 3. The protein undergoes complex post-translational modifications, being N-glycosylated in the ER, then O-glycosylated in the Golgi, and finally cleaved at its C-terminal luminal domain 2. YIPF3 is essential for maintaining normal Golgi morphology, as its depletion causes Golgi fragmentation and elongated morphology 23. Beyond its structural role, YIPF3 has been identified as a hematopoietic marker expressed from embryonic stem cells to mature blood cell lineages, particularly NK cells 5. Clinically, YIPF3 has emerged as a potential biomarker in acute myocardial infarction and shows associations with anti-VEGF treatment response in neovascular age-related macular degeneration 67.