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Protein

Metal homeostasis factor ATX1

Gene

ATX1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi15 – 151Copper
Metal bindingi18 – 181Copper

GO - Molecular functioni

  • copper chaperone activity Source: SGD

GO - Biological processi

  • cellular iron ion homeostasis Source: SGD
  • cellular response to oxidative stress Source: SGD
  • copper ion transport Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33255-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Metal homeostasis factor ATX1
Gene namesi
Name:ATX1
Ordered Locus Names:YNL259C
ORF Names:N0840
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL259c.
EuPathDBiFungiDB:YNL259C.
SGDiS000005203. ATX1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7373Metal homeostasis factor ATX1PRO_0000212535Add
BLAST

Proteomic databases

MaxQBiP38636.
PaxDbiP38636.

Interactioni

Protein-protein interaction databases

BioGridi35580. 45 interactions.
DIPiDIP-813N.
IntActiP38636. 2 interactions.
MINTiMINT-367601.
STRINGi4932.YNL259C.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Helixi16 – 2712Combined sources
Turni28 – 314Combined sources
Beta strandi32 – 398Combined sources
Turni40 – 434Combined sources
Beta strandi44 – 518Combined sources
Helixi53 – 619Combined sources
Turni62 – 643Combined sources
Beta strandi67 – 737Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CC7X-ray1.20A1-73[»]
1CC8X-ray1.02A1-73[»]
1FD8NMR-A1-73[»]
1FESNMR-A1-73[»]
1UV1model-A1-73[»]
1UV2model-A1-73[»]
2GGPNMR-A1-73[»]
3K7RX-ray2.28A/B/C/D/E/F/G/H/I/J/K/L1-73[»]
ProteinModelPortaliP38636.
SMRiP38636. Positions 2-73.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38636.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 6965HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ATX1 family.Curated
Contains 1 HMA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2608.
HOGENOMiHOG000038877.
InParanoidiP38636.
KOiK07213.
OMAiMADTHTY.
OrthoDBiEOG7G4QR6.

Family and domain databases

InterProiIPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38636-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEIKHYQFN VVMTCSGCSG AVNKVLTKLE PDVSKIDISL EKQLVDVYTT
60 70
LPYDFILEKI KKTGKEVRSG KQL
Length:73
Mass (Da):8,221
Last modified:October 1, 1994 - v1
Checksum:i9BDF0B542F80EA83
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81Q → H in AAS56693 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35270 Genomic DNA. Translation: AAC37428.1.
X96722 Genomic DNA. Translation: CAA65485.1.
Z71535 Genomic DNA. Translation: CAA96166.1.
AY558367 Genomic DNA. Translation: AAS56693.1.
BK006947 Genomic DNA. Translation: DAA10300.1.
PIRiS47930.
RefSeqiNP_014140.1. NM_001183097.1.

Genome annotation databases

EnsemblFungiiYNL259C; YNL259C; YNL259C.
GeneIDi855462.
KEGGisce:YNL259C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35270 Genomic DNA. Translation: AAC37428.1.
X96722 Genomic DNA. Translation: CAA65485.1.
Z71535 Genomic DNA. Translation: CAA96166.1.
AY558367 Genomic DNA. Translation: AAS56693.1.
BK006947 Genomic DNA. Translation: DAA10300.1.
PIRiS47930.
RefSeqiNP_014140.1. NM_001183097.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CC7X-ray1.20A1-73[»]
1CC8X-ray1.02A1-73[»]
1FD8NMR-A1-73[»]
1FESNMR-A1-73[»]
1UV1model-A1-73[»]
1UV2model-A1-73[»]
2GGPNMR-A1-73[»]
3K7RX-ray2.28A/B/C/D/E/F/G/H/I/J/K/L1-73[»]
ProteinModelPortaliP38636.
SMRiP38636. Positions 2-73.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35580. 45 interactions.
DIPiDIP-813N.
IntActiP38636. 2 interactions.
MINTiMINT-367601.
STRINGi4932.YNL259C.

Proteomic databases

MaxQBiP38636.
PaxDbiP38636.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL259C; YNL259C; YNL259C.
GeneIDi855462.
KEGGisce:YNL259C.

Organism-specific databases

CYGDiYNL259c.
EuPathDBiFungiDB:YNL259C.
SGDiS000005203. ATX1.

Phylogenomic databases

eggNOGiCOG2608.
HOGENOMiHOG000038877.
InParanoidiP38636.
KOiK07213.
OMAiMADTHTY.
OrthoDBiEOG7G4QR6.

Enzyme and pathway databases

BioCyciYEAST:G3O-33255-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP38636.
NextBioi979391.
PROiP38636.

Family and domain databases

InterProiIPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PfamiPF00403. HMA. 1 hit.
[Graphical view]
SUPFAMiSSF55008. SSF55008. 1 hit.
PROSITEiPS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity."
    Lin S.-J., Culotta V.L.
    Proc. Natl. Acad. Sci. U.S.A. 92:3784-3788(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the left arm of chromosome XIV from Saccharomyces cerevisiae."
    Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.
    Yeast 13:849-860(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution."
    Rosenzweig A.C., Huffman D.L., Hou M.Y., Wernimont A.K., Pufahl R.A., O'Halloran T.V.
    Structure 7:605-617(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS).

Entry informationi

Entry nameiATX1_YEAST
AccessioniPrimary (citable) accession number: P38636
Secondary accession number(s): D6W0T4, E9P8W0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 24, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.