Zinc-regulated GTPase metalloprotein activator 1C (ZNG1C)

Zinc-regulated GTPase metalloprotein activator 1C (ZNG1C) is a protein-coding gene product that functions as a zinc chaperone, specifically facilitating the direct transfer of zinc as a cofactor to target metalloproteins, thereby activating them[1][4]. ZNG1C performs this role by catalyzing zinc insertion into the active site of methionine aminopeptidase METAP1, a critical enzyme that removes the initiator methionine from polypeptides during or after translation. Mechanistically, ZNG1C uses motifs in its N-terminal and GTPase domain to dock with inactive METAP1, undergoes GTP hydrolysis-dependent zinc transfer, and releases the now-active METAP1 after GTP/GDP exchange. While ZNG1C is predicted to be present in the cytoplasm and nucleus, detailed information on tissue-specific roles, disease correlations, or therapeutic targeting is currently lacking[1][4][5].

Other names

CBWD3COBW domain-containing protein 3bA561O23.1Cobalamin synthase W domain-containing protein 3zinc-regulated GTPase metalloprotein activator 1CCOBW domain containing 3cobalamin synthetase W domain-containing protein 3