ID   ATOX1_HUMAN             Reviewed;          68 AA.
AC   O00244; A8KAJ8; D3DQI2; Q2M1R6; Q56AP3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-JAN-2012, entry version 103.
DE   RecName: Full=Copper transport protein ATOX1;
DE   AltName: Full=Metal transport protein ATX1;
GN   Name=ATOX1; Synonyms=HAH1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=97238857; PubMed=9083055; DOI=10.1074/jbc.272.14.9221;
RA   Klomp L.W.J., Lin S.-J., Yuan D.S., Klausner R.D., Culotta V.C.,
RA   Gitlin J.D.;
RT   "Identification and functional expression of HAH1, a novel human gene
RT   involved in copper homeostasis.";
RL   J. Biol. Chem. 272:9221-9226(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12594858; DOI=10.1186/1471-2156-4-4;
RA   Liu P.-C., Koeller D.M., Kaler S.G.;
RT   "Genomic organization of ATOX1, a human copper chaperone.";
RL   BMC Genet. 4:4-4(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RX   MEDLINE=20423084; PubMed=10966647; DOI=10.1038/78999;
RA   Wernimont A.K., Huffman D.L., Lamb A.L., O'Halloran T.V.,
RA   Rosenzweig A.C.;
RT   "Structural basis for copper transfer by the metallochaperone for the
RT   Menkes/Wilson disease proteins.";
RL   Nat. Struct. Biol. 7:766-771(2000).
CC   -!- FUNCTION: Could bind and deliver cytosolic copper to the copper
CC       ATPase proteins. May be important in cellular antioxidant defense.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the ATX1 family.
CC   -!- SIMILARITY: Contains 1 HMA domain.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/atox1/";
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DR   EMBL; U70660; AAC51227.1; -; mRNA.
DR   EMBL; AY165037; AAN84554.1; -; Genomic_DNA.
DR   EMBL; BT009786; AAP88788.1; -; mRNA.
DR   EMBL; AK293063; BAF85752.1; -; mRNA.
DR   EMBL; AY986502; AAX81411.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61663.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61664.1; -; Genomic_DNA.
DR   EMBL; BC112248; AAI12249.1; -; mRNA.
DR   EMBL; BC112250; AAI12251.1; -; mRNA.
DR   IPI; IPI00010863; -.
DR   RefSeq; NP_004036.1; NM_004045.3.
DR   UniGene; Hs.125213; -.
DR   PDB; 1FE0; X-ray; 1.75 A; A/B=1-68.
DR   PDB; 1FE4; X-ray; 1.75 A; A/B=1-68.
DR   PDB; 1FEE; X-ray; 1.80 A; A/B=1-68.
DR   PDB; 1TL4; NMR; -; A=1-68.
DR   PDB; 1TL5; NMR; -; A=1-68.
DR   PDB; 2K1R; NMR; -; B=1-68.
DR   PDB; 3CJK; X-ray; 1.80 A; A=2-68.
DR   PDB; 3IWL; X-ray; 1.60 A; A=1-68.
DR   PDB; 3IWX; X-ray; 2.14 A; A/B=1-68.
DR   PDBsum; 1FE0; -.
DR   PDBsum; 1FE4; -.
DR   PDBsum; 1FEE; -.
DR   PDBsum; 1TL4; -.
DR   PDBsum; 1TL5; -.
DR   PDBsum; 2K1R; -.
DR   PDBsum; 3CJK; -.
DR   PDBsum; 3IWL; -.
DR   PDBsum; 3IWX; -.
DR   ProteinModelPortal; O00244; -.
DR   SMR; O00244; 2-67.
DR   STRING; O00244; -.
DR   PhosphoSite; O00244; -.
DR   PeptideAtlas; O00244; -.
DR   PRIDE; O00244; -.
DR   Ensembl; ENST00000313115; ENSP00000316854; ENSG00000177556.
DR   GeneID; 475; -.
DR   KEGG; hsa:475; -.
DR   UCSC; uc003luk.1; human.
DR   CTD; 475; -.
DR   GeneCards; GC05M151102; -.
DR   H-InvDB; HIX0020331; -.
DR   HGNC; HGNC:798; ATOX1.
DR   MIM; 602270; gene.
DR   neXtProt; NX_O00244; -.
DR   PharmGKB; PA25096; -.
DR   eggNOG; prNOG21526; -.
DR   HOGENOM; HBG744819; -.
DR   HOVERGEN; HBG050610; -.
DR   InParanoid; O00244; -.
DR   OMA; HEFFVDM; -.
DR   OrthoDB; EOG45TCPV; -.
DR   PhylomeDB; O00244; -.
DR   NextBio; 1967; -.
DR   ArrayExpress; O00244; -.
DR   Bgee; O00244; -.
DR   CleanEx; HS_ATOX1; -.
DR   Genevestigator; O00244; -.
DR   GermOnline; ENSG00000177556; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR   GO; GO:0016531; F:copper chaperone activity; IDA:UniProtKB.
DR   GO; GO:0032767; F:copper-dependent protein binding; IPI:UniProtKB.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; TAS:ProtInc.
DR   GO; GO:0006825; P:copper ion transport; TAS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HeavyMe-assoc_HMA.
DR   KO; K07213; -.
DR   Pfam; PF00403; HMA; 1.
DR   SUPFAM; SSF55008; HeavyMe_transpt; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Complete proteome; Copper; Copper transport;
KW   Ion transport; Metal-binding; Reference proteome; Transport.
FT   CHAIN         1     68       Copper transport protein ATOX1.
FT                                /FTId=PRO_0000212537.
FT   DOMAIN        2     68       HMA.
FT   METAL        12     12       Copper.
FT   METAL        15     15       Copper.
FT   STRAND        3      8
FT   HELIX        13     26
FT   STRAND       28     34
FT   TURN         35     38
FT   STRAND       39     46
FT   HELIX        48     56
FT   TURN         57     59
FT   STRAND       62     66
SQ   SEQUENCE   68 AA;  7402 MW;  0B364B1BD1279314 CRC64;
     MPKHEFSVDM TCGGCAEAVS RVLNKLGGVK YDIDLPNKKV CIESEHSMDT LLATLKKTGK
     TVSYLGLE
//