ATX1/YNL259C Summary Help

Standard Name ATX1 1
Systematic Name YNL259C
Feature Type ORF, Verified
Description Cytosolic copper metallochaperone; transports copper to the secretory vesicle copper transporter Ccc2p for eventual insertion into Fet3p, which is a multicopper oxidase required for high-affinity iron uptake (1, 2 and see Summary Paragraph)
Name Description AnTioXidant 1
Chromosomal Location
ChrXIV:157865 to 157644 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All ATX1 GO evidence and references
  View Computational GO annotations for ATX1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 6 genes
Classical genetics
Large-scale survey
50 total interaction(s) for 45 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 2
  • PCA: 4
  • Reconstituted Complex: 3
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 34
  • Synthetic Growth Defect: 1
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 2

Expression Summary
Length (a.a.) 73
Molecular Weight (Da) 8,221
Isoelectric Point (pI) 8.64
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIV:157865 to 157644 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..222 157865..157644 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005203

Atx1p is an 8 kDa cytosolic mettallochaperone required for copper-dependent iron absorption (2). Atx1p transports copper(I) ions (3) from Ctr1p on the plasma membrane to Ccc2p on a post-Golgi vesicle for eventual targeting to the cell-surface high-affinity iron uptake protein Fet3p (2). atx1 deletion mutants are deficient in iron absorption, but this deficiency is suppressed by adding copper. A second, endocytosis-dependent pathway is capable of delivering copper to Ccc2p (2). ATX1 was identified as a multicopy suppressor of the superoxide (O2-) sensitivity phenotype of superoxide dismutase (SOD) deficient cells (1). A weak intrinsic antioxidant activity of Atx1p stoichiometrically compensates for SOD deficiency when ATX1 is overexpressed (4). ATX1 expression is induced by oxygen (1), but not by copper (2). It is also induced by iron through the action of Aft1p, but is not strictly dependent on Aft1p (2).

The human homolog, called Atox1 or HAH1 (OMIM), complements deletion of ATX1 (5, 6), as do Arabidopsis thaliana CCH (7) and C. elegans CUC-1 (8). Atox1 is a candidate gene for the 5q deletion syndrome (OMIM).

Last updated: 2005-07-18 Contact SGD

References cited on this page View Complete Literature Guide for ATX1
1) Lin SJ and Culotta VC  (1995) The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc Natl Acad Sci U S A 92(9):3784-8
2) Lin SJ, et al.  (1997) A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J Biol Chem 272(14):9215-20
3) Pufahl RA, et al.  (1997) Metal ion chaperone function of the soluble Cu(I) receptor Atx1. Science 278(5339):853-6
4) Portnoy ME, et al.  (1999) Structure-function analyses of the ATX1 metallochaperone. J Biol Chem 274(21):15041-5
5) Klomp LW, et al.  (1997) Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis. J Biol Chem 272(14):9221-6
6) Hung IH, et al.  (1998) HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense. J Biol Chem 273(3):1749-54
7) Himelblau E, et al.  (1998) Identification of a functional homolog of the yeast copper homeostasis gene ATX1 from Arabidopsis. Plant Physiol 117(4):1227-34
8) Wakabayashi T, et al.  (1998) Identification of the copper chaperone, CUC-1, in Caenorhabditis elegans: tissue specific co-expression with the copper transporting ATPase, CUA-1. FEBS Lett 440(1-2):141-6