High affinity copper uptake protein 1 (CTR1 (also commonly abbreviated as hCTR1))

High affinity copper uptake protein 1 (CTR1) is a plasma membrane transporter encoded by the human SLC31A1 gene and is the primary high-affinity copper influx transporter in mammalian cells[1][2][7][8]. Structurally, CTR1 is a homotrimer, where each monomer is ~190 amino acids with three transmembrane domains forming a central channel for selective copper(I) (Cu^+) ions to cross the membrane[1][2][3][4]. The N-terminal extracellular domain is rich in histidine and methionine motifs involved in copper binding, while the short C-terminal tail relays copper to intracellular chaperones[1][4][6][8]. CTR1 also mediates cellular uptake of platinum-based chemotherapeutic agents such as cisplatin, making it relevant to cancer therapy and resistance phenotypes[1][2][5]. Its functional presence is essential for copper homeostasis, and its alteration can result in copper metabolism disorders in the central nervous system, contributing to neurodegenerative disease in rare cases[7]. CTR1 is thus an established therapeutic and diagnostic target in oncology and inherited metabolic diseases.

Other names

Human copper transporter 1Copper transporter 1SLC31A1hCtr1COPT1

Drug uptake: High affinity copper uptake protein 1 mediates transport of copper and also the cellular entry of platinum-based drugs such as cisplatin, facilitating their cytotoxic effects inside tumor cells[1][2][5][7].