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9.B.462.  The Atx1 Copper Ion Chaparone or Transport Protein (Atx1) Family

The proteins of this family are annotated in UniProt as being copper chaparone proteins, but Deng and Wang 2023 have considered them to be copper efflux transporters. They are small proteins of about 70 - 80 aas in length with an N-terminal region that is moderately hydrophobic (may be an N-terminal TMS) and a C-terminal region that is more hydrophilic.  The Atx1 proteins are homologous to the N-terminal regulatory regions of copper P-type ATPases (TC# 3.A.3.5) which are thought to play a copper binding function, but not to be the actual transporter region of the ATPases. This same region seems to be homologous to mercuric ion binding proteins/transporters (see TC#s 1.A.72.3.1 and 1.A.72.3.4).

This family belongs to the: Heavy Metal Binding Domain.

References associated with 9.B.462 family:

Deng, S. and W.X. Wang. (2023). A surge of copper accumulation in cell division revealed its cyclical kinetics in synchronized green alga Chlamydomonas reinhardtii. Sci Total Environ 899: 165566. 37474058
Qin, X., P. Wang, H. Liang, and W. Si. (2024). Curcumin suppresses copper accumulation in non-small cell lung cancer by binding ATOX1. BMC Pharmacol Toxicol 25: 54. 39169392