ATOX1_SHEEP
ID ATOX1_SHEEP Reviewed; 68 AA.
AC Q9XT28;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Copper transport protein ATOX1;
DE AltName: Full=Copper chaperone SAH;
DE AltName: Full=Metal transport protein ATX1;
GN Name=ATOX1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10786613; DOI=10.1016/s0167-4781(99)00230-4;
RA Lockhart P.J., Mercer J.F.B.;
RT "Identification of the copper chaperone SAH in Ovis aries: expression
RT analysis and in vitro interaction of SAH with ATP7B.";
RL Biochim. Biophys. Acta 1490:11-20(2000).
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; AF134813; AAD38514.1; -; mRNA.
DR RefSeq; NP_001009429.1; NM_001009429.1.
DR AlphaFoldDB; Q9XT28; -.
DR SMR; Q9XT28; -.
DR STRING; 9940.ENSOARP00000009704; -.
DR Ensembl; ENSOART00020026584; ENSOARP00020022066; ENSOARG00020017245.
DR GeneID; 443451; -.
DR KEGG; oas:443451; -.
DR CTD; 475; -.
DR eggNOG; KOG1603; Eukaryota.
DR OrthoDB; 1564517at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
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_0000212540"
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
