ATOX1_MOUSE
ID ATOX1_MOUSE Reviewed; 68 AA.
AC O08997; Q5NCU2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Copper transport protein ATOX1;
DE AltName: Full=Metal transport protein ATX1;
GN Name=Atox1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=10673341; DOI=10.1006/geno.1999.6046;
RA Hamza I., Klomp L.W.J., Gaedigk R., White R.A., Gitlin J.D.;
RT "Structure, expression, and chromosomal localization of the mouse Atox1
RT gene.";
RL Genomics 63:294-297(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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; AF004591; AAB61465.1; -; mRNA.
DR EMBL; AK002432; BAB22098.1; -; mRNA.
DR EMBL; AL596207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027632; AAH27632.1; -; mRNA.
DR CCDS; CCDS36158.1; -.
DR RefSeq; NP_033850.1; NM_009720.2.
DR AlphaFoldDB; O08997; -.
DR SMR; O08997; -.
DR BioGRID; 198242; 1.
DR STRING; 10090.ENSMUSP00000104485; -.
DR iPTMnet; O08997; -.
DR PhosphoSitePlus; O08997; -.
DR SwissPalm; O08997; -.
DR CPTAC; non-CPTAC-3768; -.
DR EPD; O08997; -.
DR jPOST; O08997; -.
DR MaxQB; O08997; -.
DR PaxDb; O08997; -.
DR PeptideAtlas; O08997; -.
DR PRIDE; O08997; -.
DR ProteomicsDB; 265155; -.
DR TopDownProteomics; O08997; -.
DR Antibodypedia; 28244; 231 antibodies from 24 providers.
DR DNASU; 11927; -.
DR Ensembl; ENSMUST00000108857; ENSMUSP00000104485; ENSMUSG00000018585.
DR GeneID; 11927; -.
DR KEGG; mmu:11927; -.
DR UCSC; uc007izj.1; mouse.
DR CTD; 475; -.
DR MGI; MGI:1333855; Atox1.
DR VEuPathDB; HostDB:ENSMUSG00000018585; -.
DR eggNOG; KOG1603; Eukaryota.
DR GeneTree; ENSGT00940000162517; -.
DR HOGENOM; CLU_134973_3_1_1; -.
DR InParanoid; O08997; -.
DR OMA; MTHTYKF; -.
DR OrthoDB; 1564517at2759; -.
DR PhylomeDB; O08997; -.
DR TreeFam; TF352589; -.
DR Reactome; R-MMU-6803544; Ion influx/efflux at host-pathogen interface.
DR BioGRID-ORCS; 11927; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Atox1; mouse.
DR PRO; PR:O08997; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O08997; protein.
DR Bgee; ENSMUSG00000018585; Expressed in yolk sac and 265 other tissues.
DR Genevisible; O08997; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0016531; F:copper chaperone activity; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; ISO:MGI.
DR GO; GO:0032767; F:copper-dependent protein binding; ISO:MGI.
DR GO; GO:1903136; F:cuprous ion binding; ISO:MGI.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IMP:MGI.
DR GO; GO:0060003; P:copper ion export; ISO:MGI.
DR GO; GO:0006825; P:copper ion transport; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
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; Ion transport;
KW Metal-binding; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..68
FT /note="Copper transport protein ATOX1"
FT /id="PRO_0000212538"
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:0007744|PubMed:23806337"
SQ SEQUENCE 68 AA; 7338 MW; 85D11908CCDC6372 CRC64;
MPKHEFSVDM TCEGCAEAVS RVLNKLGGVE FNIDLPNKKV CIDSEHSSDT LLATLNKTGK
AVSYLGPK
