Plays a role in controlling biogenesis of secretory granules at the trans-Golgi network (PubMed:22981988). Mechanisitically, binds ARF-GTP at the neck of a growing secretory granule precursor and forms a protective scaffold (PubMed:9038142, PubMed:22981988). Once the granule precursor has been completely loaded, active PRKD1 phosphorylates ARFIP1 and releases it from ARFs (PubMed:22981988). In turn, ARFs induce fission (PubMed:22981988). Through this mechanism, ensures proper secretory granule formation at the Golgi of pancreatic beta cells (PubMed:22981988). Forms homodimers or heterodimers with ARFIP2 (PubMed:21239483). Interacts with non-myristoylated GTP-bound ARF3, but not to GDP-bound ARF3 (PubMed:10413101). Interacts with ARF1 (PubMed:10413101, PubMed:22981988). Binds with lower affinity to ARF5 and with very little affinity to ARF6 (PubMed:10413101). Interacts with ARL1 (PubMed:22981988, PubMed:21239483). Interacts with ATG9A (PubMed:30917996). Ubiquitously expressed (PubMed:9038142). Higher levels in liver, pancreas, placenta, skeletal muscle and heart (PubMed:9038142). Phosphorylated by PRKD1; phosphorylation delocalizes ARFIP1 from the Golgi and disrupts its ability to inhibit the activity of ADP-ribosylation factor, an important component of the vesicle scission machinery.