[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1074/jbc.272.14.9221; PubMed=9083055 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1186/1471-2156-4-4; PubMed=12594858 [NCBI, ExPASy, EBI, Israel, Japan] 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 [GENOMIC DNA]. NIEHS SNPs program; Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[7]	X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). DOI=10.1038/78999; PubMed=10966647 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Could bind and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.
TISSUE SPECIFICITY: Ubiquitous.
SIMILARITY: Belongs to the ATX1 family.
SIMILARITY: Contains 1 HMA domain.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/atox1/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U70660; AAC51227.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY165037; AAN84554.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT009786; AAP88788.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY986502; AAX81411.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112248; AAI12249.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112250; AAI12251.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00010863; -.

NP_004036.1; -.

3D structure databases

PDB

1FE0; X-ray; 1.75 A; A/B=1-68.	[ExPASy / RCSB / EBI]
1FE4; X-ray; 1.75 A; A/B=1-68.	[ExPASy / RCSB / EBI]
1FEE; X-ray; 1.80 A; A/B=1-68.	[ExPASy / RCSB / EBI]
1TL4; NMR; -; A=1-68.	[ExPASy / RCSB / EBI]
1TL5; NMR; -; A=1-68.	[ExPASy / RCSB / EBI]
2K1R; NMR; -; B=1-68.	[ExPASy / RCSB / EBI]
3CJK; X-ray; 1.80 A; A=2-68.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FE0; -.
1FE4; -.
1FEE; -.
1TL4; -.
1TL5; -.
2K1R; -.
3CJK; -.

ModBase

O00244.

Organism-specific databases

GC05M151102; -.

HIX0020331; -.

HGNC:798; ATOX1.

602270; gene. [NCBI / EBI]

PharmGKB

PA25096; -.

Gene expression databases

O00244; -.

O00244; -.

HS_ATOX1; -.

ENSG00000177556; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (traceable author statement from UniProtKB).
GO:0016531;	Molecular function: copper chaperone activity (inferred from direct assay from UniProtKB).
GO:0032767;	Molecular function: copper-dependent protein binding (inferred from physical interaction from UniProtKB).
GO:0006878;	Biological process: cellular copper ion homeostasis (traceable author statement from ProtInc).
GO:0006825;	Biological process: copper ion transport (traceable author statement from UniProtKB).
GO:0006979;	Biological process: response to oxidative stress (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR017969; Heavy-metal-associated_CS.
IPR006121; HeavyMe_transpt.
Graphical view of domain structure.

Pfam

PF00403; HMA; 1.
Pfam graphical view of domain structure.

PROSITE

PS01047; HMA_1; 1.
PS50846; HMA_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

O00244; -.

PRIDE

O00244; -.

Genome annotation databases

Ensembl

ENSG00000177556; Homo sapiens. [Contig view]

GeneID

475; -.

KEGG

hsa:475; -.

Phylogenomic databases

HOGENOM

O00244; -.

HOVERGEN

O00244; -.

Other

1967; -.

ATOX1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Chaperone; Copper; Copper transport; Ion transport; Metal-binding; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 68`	`68`	`Copper transport protein ATOX1.`	`PRO_0000212537`
`DOMAIN`	`2 68`	`67`	`HMA.`
`METAL`	`12 12`		`Copper.`
`METAL`	`15 15`		`Copper.`
`STRAND`	`3 8`	`6`
`HELIX`	`13 26`	`14`
`STRAND`	`28 34`	`7`
`TURN`	`35 38`	`4`
`STRAND`	`39 46`	`8`
`HELIX`	`48 56`	`9`
`TURN`	`57 59`	`3`
`STRAND`	`62 66`	`5`

Sequence information

Length: 68 AA [This is the length of the unprocessed precursor]

Molecular weight: 7402 Da [This is the MW of the unprocessed precursor]

CRC64: 0B364B1BD1279314 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPKHEFSVDM TCGGCAEAVS RVLNKLGGVK YDIDLPNKKV CIESEHSMDT LLATLKKTGK 


TVSYLGLE

O00244 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools