ID   CTR86_YEAST             Reviewed;         563 AA.
AC   P25355; D6VR62;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Copper transport protein 86;
GN   Name=CTR86; OrderedLocusNames=YCR054C; ORFNames=YCR54C;
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=2204248; DOI=10.1002/yea.320060408;
RA   Mannhaupt G., van der Linden C.G., Vetter I., Maurer K., Pilz U.,
RA   Planta R.J., Feldmann H.;
RT   "Analysis of the THR4 region on chromosome III of the yeast Saccharomyces
RT   cerevisiae.";
RL   Yeast 6:353-361(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [3]
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   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433 AND SER-559, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Essential protein which may be involved in threonine
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CTR86 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X59720; CAA42285.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07531.1; -; Genomic_DNA.
DR   PIR; S22837; S22837.
DR   RefSeq; NP_009983.1; NM_001178768.1.
DR   AlphaFoldDB; P25355; -.
DR   BioGRID; 31034; 89.
DR   DIP; DIP-2728N; -.
DR   IntAct; P25355; 8.
DR   MINT; P25355; -.
DR   STRING; 4932.YCR054C; -.
DR   iPTMnet; P25355; -.
DR   MaxQB; P25355; -.
DR   PaxDb; 4932-YCR054C; -.
DR   PeptideAtlas; P25355; -.
DR   EnsemblFungi; YCR054C_mRNA; YCR054C; YCR054C.
DR   GeneID; 850421; -.
DR   KEGG; sce:YCR054C; -.
DR   AGR; SGD:S000000650; -.
DR   SGD; S000000650; CTR86.
DR   VEuPathDB; FungiDB:YCR054C; -.
DR   eggNOG; KOG2676; Eukaryota.
DR   GeneTree; ENSGT00390000010377; -.
DR   HOGENOM; CLU_043683_0_0_1; -.
DR   InParanoid; P25355; -.
DR   OMA; TNFPECK; -.
DR   OrthoDB; 1438872at2759; -.
DR   BioCyc; YEAST:G3O-29362-MONOMER; -.
DR   BioGRID-ORCS; 850421; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P25355; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25355; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR019156; Ataxin-10_domain.
DR   PANTHER; PTHR13255; ATAXIN-10; 1.
DR   PANTHER; PTHR13255:SF0; ATAXIN-10; 1.
DR   Pfam; PF09759; Atx10homo_assoc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cytoplasm; Phosphoprotein; Reference proteome;
KW   Threonine biosynthesis.
FT   CHAIN           1..563
FT                   /note="Copper transport protein 86"
FT                   /id="PRO_0000202572"
FT   REGION          544..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         433
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         559
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   563 AA;  65206 MW;  38DE4EBFA781D629 CRC64;
     MPMNNFLDEF NLFDSIITMM KNDPCCVEDY EPIVENLNRI FQRTFNDEEH RKSMANSQLF
     WERLRDTLEA MLLPASLNEN SSIPYTRTVR GLILMMRNLA AENQEIPQKL LLQNLVIRGF
     LHATSEYVVD TPLIKHLYIA CLTCLFNIQQ NYSTVDMTTF PALLQFLQYP YGIKLEDGEE
     EEHFWLPYLF LFKTYLNNDE FSNEFFRDND TPQKDYYCVR DRIFFDIVTA KFIQDQENSF
     LIEKGRNYLD DSKLEITSID LSVLECISKS LTTASFGKYL NGLEERQPGK FTTLLQILQL
     VVTSKEDWNT YELTAIMSWC YPILQRLACK DIPAFFNKSC NDYAPSVAIQ LHSTLLSCLD
     IISDLCKFNH VRKFLISYDS VKILVSLLDT FQKNLLRINF LKGNGDTVNE IKITDHEGNK
     IEDRLLIFNR VNTNESFIRA DNFPHCKLVI IEILASLVYA HPEIQDQIRE LGGLALILSN
     CVIDDNDPFI KERSIVCLKF LLKNNAKNQE YVKKMEAQDV VQDDALSKAG FEISVEKGGK
     VRLVSKEEDP GNENSEIISI DED
//