ATX1_YEAST
ID ATX1_YEAST Reviewed; 73 AA.
AC P38636; D6W0T4; E9P8W0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Metal homeostasis factor ATX1;
GN Name=ATX1; OrderedLocusNames=YNL259C; ORFNames=N0840;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7731983; DOI=10.1073/pnas.92.9.3784;
RA Lin S.-J., Culotta V.L.;
RT "The ATX1 gene of Saccharomyces cerevisiae encodes a small metal
RT homeostasis factor that protects cells against reactive oxygen toxicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3784-3788(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS).
RX PubMed=10404590; DOI=10.1016/s0969-2126(99)80082-3;
RA Rosenzweig A.C., Huffman D.L., Hou M.Y., Wernimont A.K., Pufahl R.A.,
RA O'Halloran T.V.;
RT "Crystal structure of the Atx1 metallochaperone protein at 1.02 A
RT resolution.";
RL Structure 7:605-617(1999).
CC -!- FUNCTION: Shuttles copper to the transport ATPase CCC2. Protects
CC against oxygen toxicity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the ATX1 family. {ECO:0000305}.
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DR EMBL; L35270; AAC37428.1; -; Genomic_DNA.
DR EMBL; X96722; CAA65485.1; -; Genomic_DNA.
DR EMBL; Z71535; CAA96166.1; -; Genomic_DNA.
DR EMBL; AY558367; AAS56693.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10300.1; -; Genomic_DNA.
DR PIR; S47930; S47930.
DR RefSeq; NP_014140.1; NM_001183097.1.
DR PDB; 1CC7; X-ray; 1.20 A; A=1-73.
DR PDB; 1CC8; X-ray; 1.02 A; A=1-73.
DR PDB; 1FD8; NMR; -; A=1-73.
DR PDB; 1FES; NMR; -; A=1-73.
DR PDB; 2GGP; NMR; -; A=1-73.
DR PDB; 3K7R; X-ray; 2.28 A; A/B/C/D/E/F/G/H/I/J/K/L=1-73.
DR PDB; 5VDE; X-ray; 1.65 A; A/B/C/D=1-73.
DR PDB; 5VDF; X-ray; 1.93 A; A/B/C/D/E/F/G/H=1-73.
DR PDBsum; 1CC7; -.
DR PDBsum; 1CC8; -.
DR PDBsum; 1FD8; -.
DR PDBsum; 1FES; -.
DR PDBsum; 2GGP; -.
DR PDBsum; 3K7R; -.
DR PDBsum; 5VDE; -.
DR PDBsum; 5VDF; -.
DR AlphaFoldDB; P38636; -.
DR SMR; P38636; -.
DR BioGRID; 35580; 80.
DR DIP; DIP-813N; -.
DR IntAct; P38636; 5.
DR MINT; P38636; -.
DR STRING; 4932.YNL259C; -.
DR MaxQB; P38636; -.
DR PaxDb; P38636; -.
DR PRIDE; P38636; -.
DR EnsemblFungi; YNL259C_mRNA; YNL259C; YNL259C.
DR GeneID; 855462; -.
DR KEGG; sce:YNL259C; -.
DR SGD; S000005203; ATX1.
DR VEuPathDB; FungiDB:YNL259C; -.
DR eggNOG; KOG1603; Eukaryota.
DR HOGENOM; CLU_134973_3_1_1; -.
DR InParanoid; P38636; -.
DR OMA; MAETHTY; -.
DR BioCyc; YEAST:G3O-33255-MON; -.
DR ChiTaRS; ATX1; yeast.
DR EvolutionaryTrace; P38636; -.
DR PRO; PR:P38636; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P38636; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0016531; F:copper chaperone activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006825; P:copper ion transport; IMP:SGD.
DR CDD; cd00371; HMA; 1.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR Pfam; PF00403; HMA; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Copper; Copper transport; Cytoplasm;
KW Ion transport; Metal-binding; Reference proteome; Transport.
FT CHAIN 1..73
FT /note="Metal homeostasis factor ATX1"
FT /id="PRO_0000212535"
FT DOMAIN 4..68
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 15
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 18
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT CONFLICT 8
FT /note="Q -> H (in Ref. 5; AAS56693)"
FT /evidence="ECO:0000305"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1CC8"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:1CC8"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:1CC8"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:1CC8"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1CC8"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:1CC8"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:1CC8"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:5VDE"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1CC8"
SQ SEQUENCE 73 AA; 8221 MW; 9BDF0B542F80EA83 CRC64;
MAEIKHYQFN VVMTCSGCSG AVNKVLTKLE PDVSKIDISL EKQLVDVYTT LPYDFILEKI
KKTGKEVRSG KQL
