ID   ATOX1_BOVIN             Reviewed;          68 AA.
AC   Q3T0E0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Copper transport protein ATOX1;
DE   AltName: Full=Metal transport protein ATX1;
GN   Name=ATOX1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC102437; AAI02438.1; -; mRNA.
DR   RefSeq; NP_001124230.1; NM_001130758.1.
DR   RefSeq; XP_005209705.1; XM_005209648.3.
DR   RefSeq; XP_010805828.1; XM_010807526.2.
DR   RefSeq; XP_015327815.1; XM_015472329.1.
DR   AlphaFoldDB; Q3T0E0; -.
DR   SMR; Q3T0E0; -.
DR   STRING; 9913.ENSBTAP00000010982; -.
DR   PaxDb; Q3T0E0; -.
DR   PeptideAtlas; Q3T0E0; -.
DR   PRIDE; Q3T0E0; -.
DR   Ensembl; ENSBTAT00000010982; ENSBTAP00000010982; ENSBTAG00000008340.
DR   GeneID; 613998; -.
DR   KEGG; bta:613998; -.
DR   CTD; 475; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008340; -.
DR   VGNC; VGNC:26273; ATOX1.
DR   eggNOG; KOG1603; Eukaryota.
DR   GeneTree; ENSGT00940000163780; -.
DR   HOGENOM; CLU_134973_3_1_1; -.
DR   InParanoid; Q3T0E0; -.
DR   OMA; MTHTYKF; -.
DR   OrthoDB; 1564517at2759; -.
DR   TreeFam; TF352589; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000008340; Expressed in caput epididymis and 107 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_0000331118"
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;  7365 MW;  AA4FB9ABFD5FF885 CRC64;
     MPKHEFSVDM TCEGCSNAVT RVLNKLGGVQ FDIDLPNKKV CINSEHSVDT LLETLGKTGK
     AVSYLGPK