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Database: UniProt
Entry: ATX1_SCHPO
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Original site: ATX1_SCHPO 
ID   ATX1_SCHPO              Reviewed;          68 AA.
AC   O74735;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Metal homeostasis factor atx1;
GN   Name=atx1; ORFNames=SPBC1709.10c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Shuttles copper to the transport ATPase ccc2. Protects
CC       against oxygen toxicity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the ATX1 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA21249.1; -; Genomic_DNA.
DR   PIR; T39638; T39638.
DR   RefSeq; NP_595443.1; NM_001021352.2.
DR   AlphaFoldDB; O74735; -.
DR   SMR; O74735; -.
DR   BioGRID; 276556; 1.
DR   STRING; 284812.O74735; -.
DR   MaxQB; O74735; -.
DR   PaxDb; 4896-SPBC1709-10c-1; -.
DR   EnsemblFungi; SPBC1709.10c.1; SPBC1709.10c.1:pep; SPBC1709.10c.
DR   GeneID; 2540012; -.
DR   KEGG; spo:SPBC1709.10c; -.
DR   PomBase; SPBC1709.10c; atx1.
DR   VEuPathDB; FungiDB:SPBC1709.10c; -.
DR   eggNOG; KOG1603; Eukaryota.
DR   HOGENOM; CLU_134973_3_1_1; -.
DR   InParanoid; O74735; -.
DR   OMA; MTHTYKF; -.
DR   PhylomeDB; O74735; -.
DR   PRO; PR:O74735; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0016531; F:copper chaperone activity; IDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006825; P:copper ion transport; IBA:GO_Central.
DR   GO; GO:0015680; P:protein maturation by copper ion transfer; EXP:PomBase.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   PANTHER; PTHR46365; COPPER TRANSPORT PROTEIN ATOX1; 1.
DR   PANTHER; PTHR46365:SF1; COPPER TRANSPORT PROTEIN ATOX1; 1.
DR   Pfam; PF00403; HMA; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   Chaperone; Copper; Copper transport; Cytoplasm; Ion transport;
KW   Metal-binding; Nucleus; Reference proteome; Transport.
FT   CHAIN           1..68
FT                   /note="Metal homeostasis factor atx1"
FT                   /id="PRO_0000314752"
FT   DOMAIN          1..62
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         11
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         14
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
SQ   SEQUENCE   68 AA;  7662 MW;  4FDAEC77C6DEA31D CRC64;
     MKYQFNVAMA CDGCKNAIDR VLTRLGVEDK SISVEKQEVI VTTDKPYELV EQTIKKTGKE
     VRSGKVLE
//
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