The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF24 (ring finger protein 24), also known as Goliath-like protein (C3CH4 type) or G1L, is a single-pass membrane protein found in the Golgi apparatus, consisting of 148 amino acids. RNF24 causes intracellular retention of TRPCs, regulates insertion of TRPCs into the plasma membrane and interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and TRPC7. The RNF24 protein shares similarity with Drosophila Goliath protein and thus, may function as a transcription factor. Multiple transcript variants encoding different isoforms have been found for the RNF24 gene, which maps to human chromosome 20p13.