ATOX1_RAT
ID ATOX1_RAT Reviewed; 68 AA.
AC Q9WUC4; Q549B3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Copper transport protein ATOX1;
DE AltName: Full=ATX1 homolog protein Rah1;
DE AltName: Full=Metal transport protein ATX1;
GN Name=Atox1; Synonyms=Rah1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10558899; DOI=10.1006/bbrc.1999.1678;
RA Hiromura M., Sakurai H.;
RT "Molecular cloning of rat ATX1 homologue protein.";
RL Biochem. Biophys. Res. Commun. 265:509-512(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10473283; DOI=10.1016/s0306-4522(99)00175-x;
RA Naeve G.S., Vana A.M., Eggold J.R., Kelner G.S., Maki R., Desouza E.B.,
RA Foster A.C.;
RT "Expression profile of the copper homeostasis gene, rAtox1, in the rat
RT brain.";
RL Neuroscience 93:1179-1187(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 26-57, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
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; AF177671; AAD53914.1; -; mRNA.
DR EMBL; AF127137; AAD27844.1; -; mRNA.
DR EMBL; BC058458; AAH58458.1; -; mRNA.
DR PIR; JC7133; JC7133.
DR RefSeq; NP_445811.1; NM_053359.2.
DR AlphaFoldDB; Q9WUC4; -.
DR SMR; Q9WUC4; -.
DR STRING; 10116.ENSRNOP00000017588; -.
DR iPTMnet; Q9WUC4; -.
DR PhosphoSitePlus; Q9WUC4; -.
DR SwissPalm; Q9WUC4; -.
DR jPOST; Q9WUC4; -.
DR PaxDb; Q9WUC4; -.
DR PRIDE; Q9WUC4; -.
DR GeneID; 84355; -.
DR KEGG; rno:84355; -.
DR UCSC; RGD:621684; rat.
DR CTD; 475; -.
DR RGD; 621684; Atox1.
DR VEuPathDB; HostDB:ENSRNOG00000013118; -.
DR eggNOG; KOG1603; Eukaryota.
DR HOGENOM; CLU_134973_3_1_1; -.
DR InParanoid; Q9WUC4; -.
DR OMA; MTHTYKF; -.
DR OrthoDB; 1564517at2759; -.
DR PhylomeDB; Q9WUC4; -.
DR TreeFam; TF352589; -.
DR Reactome; R-RNO-6803544; Ion influx/efflux at host-pathogen interface.
DR PRO; PR:Q9WUC4; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000013118; Expressed in duodenum and 20 other tissues.
DR Genevisible; Q9WUC4; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IPI:RGD.
DR GO; GO:0016531; F:copper chaperone activity; ISO:RGD.
DR GO; GO:0005507; F:copper ion binding; ISO:RGD.
DR GO; GO:0032767; F:copper-dependent protein binding; ISO:RGD.
DR GO; GO:1903136; F:cuprous ion binding; ISO:RGD.
DR GO; GO:0006878; P:cellular copper ion homeostasis; ISO:RGD.
DR GO; GO:0060003; P:copper ion export; IMP:RGD.
DR GO; GO:0006825; P:copper ion transport; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
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 1: Evidence at protein level;
KW Acetylation; Chaperone; Copper; Copper transport;
KW Direct protein sequencing; Ion transport; Metal-binding; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..68
FT /note="Copper transport protein ATOX1"
FT /id="PRO_0000212539"
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; 7292 MW; 57D01EC1FCDC6371 CRC64;
MPKHEFSVDM TCGGCAEAVS RVLNKLGGVE FNIDLPNKKV CIESEHSSDI LLATLNKTGK
AVSYLGPK
