ID   ATOX1_CANLF             Reviewed;          68 AA.
AC   Q9TT99;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Copper transport protein ATOX1;
DE   AltName: Full=Metal transport protein ATX1;
GN   Name=ATOX1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10585777; DOI=10.1006/geno.1999.5983;
RA   Nanji M.S., Cox D.W.;
RT   "The copper chaperone Atox1 in canine copper toxicosis in Bedlington
RT   terriers.";
RL   Genomics 62:108-112(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11474190; DOI=10.1159/000056959;
RA   van de Sluis B., Nanji M.S., Breen M., Pearson P.L., van Oost B.A.,
RA   Cox D.W., Wijmenga C.;
RT   "Characterization and chromosomal localization of five canine ATOX1
RT   pseudogenes.";
RL   Cytogenet. Cell Genet. 93:105-108(2001).
CC   -!- FUNCTION: Binds and deliver cytosolic copper to the copper ATPase
CC       proteins. May be important in cellular antioxidant defense (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ATP7B (By similarity). Interacts with ATP7A (By
CC       similarity). {ECO:0000250|UniProtKB:O00244}.
CC   -!- DOMAIN: The heavy-metal-associated domain (HMA) coordinates a Cu(+) ion
CC       via the cysteine residues within the CXXC motif. The transfer of Cu(+)
CC       ion from ATOX1 to ATP7A involves the formation of a three-coordinate
CC       Cu(+)-bridged heterodimer where the metal is shared between the two
CC       metal binding sites of ATOX1 and ATP7A. The Cu(+) ion appears to switch
CC       between two coordination modes, forming two links with one protein and
CC       one with the other. Cisplatin, a chemotherapeutic drug, can bind the
CC       CXXC motif and hinder the release of Cu(+) ion.
CC       {ECO:0000250|UniProtKB:O00244}.
CC   -!- SIMILARITY: Belongs to the ATX1 family. {ECO:0000305}.
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DR   EMBL; AF179715; AAF01286.1; -; mRNA.
DR   EMBL; AF286878; AAL03945.1; -; Genomic_DNA.
DR   EMBL; AF286877; AAL03945.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001003119.1; NM_001003119.1.
DR   RefSeq; XP_005618921.1; XM_005618864.2.
DR   AlphaFoldDB; Q9TT99; -.
DR   SMR; Q9TT99; -.
DR   STRING; 9612.ENSCAFP00000041904; -.
DR   PaxDb; Q9TT99; -.
DR   Ensembl; ENSCAFT00030007267; ENSCAFP00030006371; ENSCAFG00030003936.
DR   Ensembl; ENSCAFT00040013498; ENSCAFP00040011699; ENSCAFG00040007251.
DR   Ensembl; ENSCAFT00845009205; ENSCAFP00845007240; ENSCAFG00845005141.
DR   GeneID; 403713; -.
DR   KEGG; cfa:403713; -.
DR   CTD; 475; -.
DR   VEuPathDB; HostDB:ENSCAFG00845005141; -.
DR   eggNOG; KOG1603; Eukaryota.
DR   GeneTree; ENSGT00940000162517; -.
DR   InParanoid; Q9TT99; -.
DR   OMA; MTHTYKF; -.
DR   OrthoDB; 1564517at2759; -.
DR   TreeFam; TF352589; -.
DR   Reactome; R-CFA-6803544; Ion influx/efflux at host-pathogen interface.
DR   Proteomes; UP000002254; Chromosome 4.
DR   Bgee; ENSCAFG00000017846; Expressed in placenta and 48 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016531; F:copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006825; P:copper ion transport; IBA:GO_Central.
DR   CDD; cd00371; HMA; 1.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   Pfam; PF00403; HMA; 1.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chaperone; Copper; Copper transport; Ion transport;
KW   Metal-binding; Phosphoprotein; Reference proteome; Transport.
FT   CHAIN           1..68
FT                   /note="Copper transport protein ATOX1"
FT                   /id="PRO_0000212536"
FT   DOMAIN          1..63
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         12
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:O00244,
FT                   ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         15
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:O00244,
FT                   ECO:0000255|PROSITE-ProRule:PRU00280"
FT   MOD_RES         47
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00244"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O08997"
SQ   SEQUENCE   68 AA;  7437 MW;  1A1BAC749FD5E498 CRC64;
     MPKHEFSVDM TCEGCSNAVS RVLNKLGGVE FDIDLPNKKV CINSEHSVDI LLETLEKTGK
     AVSYLGPK