Human copper transporter 1 (CTR1)

**Human copper transporter 1 (CTR1)** is a plasma membrane protein that serves as the main high-affinity copper(I) influx transporter in mammalian cells[1][2][3]. Structurally, it forms a symmetrical trimer that creates a central pore allowing for selective copper(I) transport[1][3][4][5]. Each monomer consists of an extracellular N-terminal domain rich in methionine and histidine residues, three transmembrane domains, an intracellular loop, and a short C-terminal tail[1][2][4]. CTR1 is essential for cellular copper homeostasis and is involved in embryonic development, nutrition, and tissue-specific functions, especially in the heart and liver[5]. In addition to copper transport, CTR1 mediates the cellular uptake of the platinum-based anticancer drug cisplatin, which enters cells partly via this transporter[1][3][5]. The transporter’s function is energy-independent, and passage of copper involves specific coordination with methionine motifs in the transmembrane region[1][4][5]. Abnormalities in CTR1 are linked to diseases involving copper deficiency or overload (e.g., Wilson’s and Menkes disease), various cancers (through effects on cisplatin uptake/resistance), and other metabolic or neurodegenerative disorders[2][5].

Other names

COPT1SLC31A1hCTR1

Facilitates high-affinity uptake of copper(I) ions; mediates uptake of cisplatin likely via a channel-like or endocytic pathway; action is energy-independent and involves methionine-rich motifs for metal binding[1][2][3][5]