Substrate-recognition component of the GID complex, a multisubunit ubiquitin ligase that targets enzymes involved in gluconeogenesis for proteasomal degradation when cells are shifted to glucose-containing medium (PubMed:12686616, PubMed:18508925, PubMed:28126757). Specific for substrates with an N-terminal Pro (Pro/N-degron), including FBP1, ICL1 and MDH2 (PubMed:28126757). Has high affinity for the N-terminal sequence Pro-Thr-Leu-Val, and can bind peptides with an N-terminal sequence of the type Pro-[Gly,Ala,Ser,Thr,Asp,Asn,Tyr,His]-[Ala,Val,Leu,Ile,Lys,Arg]-[Val,Cys,Pro,Leu,Ile,Trp] (PubMed:28126757). Required for vacuolar degradation of FBP1 when cells are shifted to glucose-containing medium, probably by targeting FBP1-containing vesicles to the vacuole, but is not required for FBP1 sequestration in cytoplasmic vesicles (PubMed:9508768). Substrate-recognition component of the GID ubiquitin ligase complex; interacts with proteins that have an N-terminal Pro/N-degron, including FBP1, ICL1 and MDH2 (PubMed:28126757). Identified in the GID complex, but only when cells are shifted to glucose-containing medium. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is recruited to the complex via interaction with VID28/GID5 (PubMed:22645139). Colocalizes with FBPase-containing vesicles. Rapidly induced by a shift to glucose-containing medium. Ubiquitinated by the GID complex, leading to subsequent proteasomal degradation. Present with 6650 molecules/cell in log phase SD medium. Belongs to the GID4/VID24 family. To yeast YGR066c and S.pombe SpAC3H1.14.