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Copper transport protein ATOX1 (Metal transport protein ATX1)

 ATOX1_HUMAN             Reviewed;          68 AA.
O00244; A8KAJ8; D3DQI2; Q2M1R6; Q56AP3;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
20-JUN-2018, entry version 159.
RecName: Full=Copper transport protein ATOX1;
AltName: Full=Metal transport protein ATX1;
Name=ATOX1; Synonyms=HAH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=9083055; DOI=10.1074/jbc.272.14.9221;
Klomp L.W.J., Lin S.-J., Yuan D.S., Klausner R.D., Culotta V.C.,
Gitlin J.D.;
"Identification and functional expression of HAH1, a novel human gene
involved in copper homeostasis.";
J. Biol. Chem. 272:9221-9226(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12594858; DOI=10.1186/1471-2156-4-4;
Liu P.-C., Koeller D.M., Kaler S.G.;
"Genomic organization of ATOX1, a human copper chaperone.";
BMC Genet. 4:4-4(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
INTERACTION WITH ATP7A.
PubMed=21667063; DOI=10.1007/s00018-011-0743-1;
Vonk W.I., de Bie P., Wichers C.G., van den Berghe P.V.,
van der Plaats R., Berger R., Wijmenga C., Klomp L.W.,
van de Sluis B.;
"The copper-transporting capacity of ATP7A mutants associated with
Menkes disease is ameliorated by COMMD1 as a result of improved
protein expression.";
Cell. Mol. Life Sci. 69:149-163(2012).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), COPPER-BINDING SITES, AND
INTERACTION WITH ATP7B.
PubMed=10966647; DOI=10.1038/78999;
Wernimont A.K., Huffman D.L., Lamb A.L., O'Halloran T.V.,
Rosenzweig A.C.;
"Structural basis for copper transfer by the metallochaperone for the
Menkes/Wilson disease proteins.";
Nat. Struct. Biol. 7:766-771(2000).
-!- FUNCTION: Binds and deliver cytosolic copper to the copper ATPase
proteins. May be important in cellular antioxidant defense.
-!- SUBUNIT: Interacts with ATP7B (PubMed:10966647). Interacts with
ATP7A (PubMed:21667063). {ECO:0000269|PubMed:10966647,
ECO:0000269|PubMed:21667063}.
-!- INTERACTION:
P35670:ATP7B; NbExp=3; IntAct=EBI-10179267, EBI-11668501;
O43822:C21orf2; NbExp=3; IntAct=EBI-10179267, EBI-2835332;
Q9NWS6:FAM118A; NbExp=5; IntAct=EBI-10179267, EBI-8638992;
O95749:GGPS1; NbExp=3; IntAct=EBI-10179267, EBI-10179283;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the ATX1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/atox1/";
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EMBL; U70660; AAC51227.1; -; mRNA.
EMBL; AY165037; AAN84554.1; -; Genomic_DNA.
EMBL; BT009786; AAP88788.1; -; mRNA.
EMBL; AK293063; BAF85752.1; -; mRNA.
EMBL; AY986502; AAX81411.1; -; Genomic_DNA.
EMBL; CH471062; EAW61663.1; -; Genomic_DNA.
EMBL; CH471062; EAW61664.1; -; Genomic_DNA.
EMBL; BC112248; AAI12249.1; -; mRNA.
EMBL; BC112250; AAI12251.1; -; mRNA.
CCDS; CCDS47317.1; -.
RefSeq; NP_004036.1; NM_004045.3.
UniGene; Hs.125213; -.
PDB; 1FE0; X-ray; 1.75 A; A/B=1-68.
PDB; 1FE4; X-ray; 1.75 A; A/B=1-68.
PDB; 1FEE; X-ray; 1.80 A; A/B=1-68.
PDB; 1TL4; NMR; -; A=1-68.
PDB; 1TL5; NMR; -; A=1-68.
PDB; 2K1R; NMR; -; B=1-68.
PDB; 2LQ9; NMR; -; A=1-68.
PDB; 3CJK; X-ray; 1.80 A; A=2-68.
PDB; 3IWL; X-ray; 1.60 A; A=1-68.
PDB; 3IWX; X-ray; 2.14 A; A/B=1-68.
PDB; 4QOT; X-ray; 2.20 A; A/B=1-68.
PDB; 4YDX; X-ray; 1.60 A; A=2-68.
PDB; 4YEA; X-ray; 2.14 A; A/B=2-68.
PDB; 5F0W; X-ray; 2.70 A; A/B/C/D=1-68.
PDB; 5T7L; X-ray; 2.83 A; A=2-68.
PDBsum; 1FE0; -.
PDBsum; 1FE4; -.
PDBsum; 1FEE; -.
PDBsum; 1TL4; -.
PDBsum; 1TL5; -.
PDBsum; 2K1R; -.
PDBsum; 2LQ9; -.
PDBsum; 3CJK; -.
PDBsum; 3IWL; -.
PDBsum; 3IWX; -.
PDBsum; 4QOT; -.
PDBsum; 4YDX; -.
PDBsum; 4YEA; -.
PDBsum; 5F0W; -.
PDBsum; 5T7L; -.
ProteinModelPortal; O00244; -.
SMR; O00244; -.
BioGrid; 106965; 14.
IntAct; O00244; 6.
STRING; 9606.ENSP00000316854; -.
DrugBank; DB03127; Benzamidine.
DrugBank; DB02772; Sucrose.
iPTMnet; O00244; -.
PhosphoSitePlus; O00244; -.
BioMuta; ATOX1; -.
EPD; O00244; -.
MaxQB; O00244; -.
PaxDb; O00244; -.
PeptideAtlas; O00244; -.
PRIDE; O00244; -.
ProteomicsDB; 47805; -.
TopDownProteomics; O00244; -.
DNASU; 475; -.
Ensembl; ENST00000313115; ENSP00000316854; ENSG00000177556.
Ensembl; ENST00000522710; ENSP00000429814; ENSG00000177556.
Ensembl; ENST00000524142; ENSP00000430598; ENSG00000177556.
GeneID; 475; -.
KEGG; hsa:475; -.
UCSC; uc003luk.4; human.
CTD; 475; -.
DisGeNET; 475; -.
EuPathDB; HostDB:ENSG00000177556.11; -.
GeneCards; ATOX1; -.
HGNC; HGNC:798; ATOX1.
HPA; HPA055036; -.
MIM; 602270; gene.
neXtProt; NX_O00244; -.
OpenTargets; ENSG00000177556; -.
PharmGKB; PA25096; -.
eggNOG; KOG1603; Eukaryota.
eggNOG; COG2608; LUCA.
GeneTree; ENSGT00390000005805; -.
HOGENOM; HOG000038877; -.
HOVERGEN; HBG050610; -.
InParanoid; O00244; -.
KO; K07213; -.
PhylomeDB; O00244; -.
TreeFam; TF352589; -.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-6803544; Ion influx/efflux at host-pathogen interface.
ChiTaRS; ATOX1; human.
EvolutionaryTrace; O00244; -.
GeneWiki; ATOX1; -.
GenomeRNAi; 475; -.
PRO; PR:O00244; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000177556; -.
CleanEx; HS_ATOX1; -.
ExpressionAtlas; O00244; baseline and differential.
Genevisible; O00244; HS.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0016531; F:copper chaperone activity; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0005375; F:copper ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0032767; F:copper-dependent protein binding; IPI:UniProtKB.
GO; GO:0016530; F:metallochaperone activity; TAS:UniProtKB.
GO; GO:0006878; P:cellular copper ion homeostasis; IBA:GO_Central.
GO; GO:0006825; P:copper ion transport; TAS:UniProtKB.
GO; GO:0015680; P:intracellular copper ion transport; IBA:GO_Central.
GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
CDD; cd00371; HMA; 1.
InterPro; IPR017969; Heavy-metal-associated_CS.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
Pfam; PF00403; HMA; 1.
SUPFAM; SSF55008; SSF55008; 1.
PROSITE; PS01047; HMA_1; 1.
PROSITE; PS50846; HMA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chaperone; Complete proteome; Copper;
Copper transport; Ion transport; Metal-binding; Phosphoprotein;
Reference proteome; Transport.
CHAIN 1 68 Copper transport protein ATOX1.
/FTId=PRO_0000212537.
DOMAIN 2 68 HMA. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 12 12 Copper.
METAL 15 15 Copper.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08997}.
STRAND 3 8 {ECO:0000244|PDB:3IWL}.
HELIX 13 26 {ECO:0000244|PDB:3IWL}.
STRAND 28 34 {ECO:0000244|PDB:3IWL}.
TURN 35 38 {ECO:0000244|PDB:3IWL}.
STRAND 39 46 {ECO:0000244|PDB:3IWL}.
HELIX 48 56 {ECO:0000244|PDB:3IWL}.
TURN 57 59 {ECO:0000244|PDB:1FE0}.
STRAND 62 66 {ECO:0000244|PDB:3IWL}.
SEQUENCE 68 AA; 7402 MW; 0B364B1BD1279314 CRC64;
MPKHEFSVDM TCGGCAEAVS RVLNKLGGVK YDIDLPNKKV CIESEHSMDT LLATLKKTGK
TVSYLGLE


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