UniProt functional annotation for O00244



	UniProt functional annotation for O00244

UniProt code: O00244.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.

Subunit: Interacts with ATP7B (PubMed:10966647). Interacts with ATP7A (PubMed:21667063, PubMed:19453293). {ECO:0000269|PubMed:10966647, ECO:0000269|PubMed:19453293, ECO:0000269|PubMed:21667063}.

Tissue specificity: Ubiquitous.

Domain: The heavy-metal-associated domain (HMA) coordinates a Cu(+) ion via the cysteine residues within the CXXC motif. The transfer of Cu(+) ion from ATOX1 to ATP7A involves the formation of a three-coordinate Cu(+)-bridged heterodimer where the metal is shared between the two metal binding sites of ATOX1 and ATP7A. The Cu(+) ion appears to switch between two coordination modes, forming two links with one protein and one with the other. Cisplatin, a chemotherapeutic drug, can bind the CXXC motif and hinder the release of Cu(+) ion. {ECO:0000269|PubMed:19453293, ECO:0000269|PubMed:31283225}.

Similarity: Belongs to the ATX1 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.


Subunit:		Interacts with ATP7B (PubMed:10966647). Interacts with ATP7A (PubMed:21667063, PubMed:19453293). {ECO:0000269\|PubMed:10966647, ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:21667063}.
Tissue specificity:		Ubiquitous.
Domain:		The heavy-metal-associated domain (HMA) coordinates a Cu(+) ion via the cysteine residues within the CXXC motif. The transfer of Cu(+) ion from ATOX1 to ATP7A involves the formation of a three-coordinate Cu(+)-bridged heterodimer where the metal is shared between the two metal binding sites of ATOX1 and ATP7A. The Cu(+) ion appears to switch between two coordination modes, forming two links with one protein and one with the other. Cisplatin, a chemotherapeutic drug, can bind the CXXC motif and hinder the release of Cu(+) ion. {ECO:0000269\|PubMed:19453293, ECO:0000269\|PubMed:31283225}.
Similarity:		Belongs to the ATX1 family. {ECO:0000305}.