MTCU1_YEAST
ID MTCU1_YEAST Reviewed; 61 AA.
AC P0CX80; D3DL02; P07215;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Copper metallothionein 1-1;
DE Short=Cu-MT;
DE Short=Cu-metallothionein;
DE AltName: Full=Copper chelatin;
DE AltName: Full=Copper thionein;
DE Flags: Precursor;
GN Name=CUP1-1; Synonyms=MTH1; OrderedLocusNames=YHR053C;
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=6364141; DOI=10.1073/pnas.81.2.337;
RA Karin M., Najarian R.C., Haslinger A., Valenzuela P., Welch J., Fogel S.;
RT "Primary structure and transcription of an amplified genetic locus: the
RT CUP1 locus of yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:337-341(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6374656; DOI=10.1073/pnas.81.11.3332;
RA Butt T.R., Sternberg E.J., Gorman J.A., Clark P., Hamer D., Rosenberg M.,
RA Crooke S.T.;
RT "Copper metallothionein of yeast, structure of the gene, and regulation of
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:3332-3336(1984).
RN [3]
RP PROTEIN SEQUENCE.
RX PubMed=3902832; DOI=10.1016/s0021-9258(17)38592-7;
RA Winge D.R., Nielson K.B., Gray W.R., Hamer D.H.;
RT "Yeast metallothionein. Sequence and metal-binding properties.";
RL J. Biol. Chem. 260:14464-14470(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2017134; DOI=10.1007/bf00261675;
RA Jeyaprakash A., Welch J.W., Fogel S.;
RT "Multicopy CUP1 plasmids enhance cadmium and copper resistance levels in
RT yeast.";
RL Mol. Gen. Genet. 225:363-368(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [6]
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 [7]
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 [8]
RP ABSORPTION SPECTROSCOPY.
RX PubMed=3286647; DOI=10.1016/s0021-9258(18)68462-5;
RA George G.N., Byrd J., Winge D.R.;
RT "X-ray absorption studies of yeast copper metallothionein.";
RL J. Biol. Chem. 263:8199-8203(1988).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-30, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [10]
RP STRUCTURE BY NMR OF 9-48.
RX PubMed=8566237; DOI=10.1016/0014-5793(95)01492-6;
RA Peterson C.W., Narula S.S., Armitage I.M.;
RT "3D solution structure of copper and silver-substituted yeast
RT metallothioneins.";
RL FEBS Lett. 379:85-93(1996).
RN [11]
RP STRUCTURE BY NMR OF 9-48.
RX PubMed=10672009; DOI=10.1046/j.1432-1327.2000.01093.x;
RA Bertini I., Hartmann H.J., Klein T., Liu G., Luchinat C., Weser U.;
RT "High resolution solution structure of the protein part of Cu7
RT metallothionein.";
RL Eur. J. Biochem. 267:1008-1018(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 13-48.
RX PubMed=15613489; DOI=10.1073/pnas.0408254101;
RA Calderone V., Dolderer B., Hartmann H.J., Echner H., Luchinat C.,
RA Del Bianco C., Mangani S., Weser U.;
RT "The crystal structure of yeast copper thionein: the solution of a long-
RT lasting enigma.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:51-56(2005).
CC -!- FUNCTION: Protects the cell against copper toxicity by tightly
CC chelating copper ions. May also act as a depository for copper
CC designated for the effective transfer into the apo forms of copper
CC proteins.
CC -!- DOMAIN: Contains 1 metal-binding domain: 6 to 8 copper ions are
CC chelated within a single copper-thiolate cluster and are coordinated
CC via cysteinyl thiolate bridges to 10 cysteine ligands. 6 copper ions
CC are trigonally coordinated, whereas the other 2 are only digonally
CC coordinated.
CC -!- MISCELLANEOUS: There are 2 copies for copper thionein in yeast. The 2
CC identical copies CUP1-1 and CUP1-2 are arranged in tandem.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 12 family.
CC {ECO:0000305}.
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DR EMBL; K02204; AAA34541.1; -; Genomic_DNA.
DR EMBL; U00061; AAB68382.1; -; Genomic_DNA.
DR EMBL; AY558517; AAS56843.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06748.1; -; Genomic_DNA.
DR PIR; S14049; S14049.
DR RefSeq; NP_011920.1; NM_001179183.1.
DR RefSeq; NP_011922.1; NM_001179185.1.
DR PDB; 1AOO; NMR; -; A=9-48.
DR PDB; 1AQQ; NMR; -; A=9-48.
DR PDB; 1AQR; NMR; -; A=9-48.
DR PDB; 1AQS; NMR; -; A=9-61.
DR PDB; 1FMY; NMR; -; A=9-48.
DR PDB; 1RJU; X-ray; 1.44 A; V=13-48.
DR PDBsum; 1AOO; -.
DR PDBsum; 1AQQ; -.
DR PDBsum; 1AQR; -.
DR PDBsum; 1AQS; -.
DR PDBsum; 1FMY; -.
DR PDBsum; 1RJU; -.
DR AlphaFoldDB; P0CX80; -.
DR BMRB; P0CX80; -.
DR SMR; P0CX80; -.
DR BioGRID; 36485; 13.
DR BioGRID; 36487; 54.
DR STRING; 4932.YHR053C; -.
DR iPTMnet; P0CX80; -.
DR MaxQB; P0CX80; -.
DR PaxDb; P0CX80; -.
DR PRIDE; P0CX80; -.
DR EnsemblFungi; YHR053C_mRNA; YHR053C; YHR053C.
DR EnsemblFungi; YHR055C_mRNA; YHR055C; YHR055C.
DR GeneID; 856450; -.
DR GeneID; 856452; -.
DR KEGG; sce:YHR053C; -.
DR KEGG; sce:YHR055C; -.
DR SGD; S000001095; CUP1-1.
DR VEuPathDB; FungiDB:YHR053C; -.
DR VEuPathDB; FungiDB:YHR055C; -.
DR eggNOG; KOG4738; Eukaryota.
DR HOGENOM; CLU_2943095_0_0_1; -.
DR BioCyc; YEAST:G3O-31107-MON; -.
DR EvolutionaryTrace; P0CX80; -.
DR PRO; PR:P0CX80; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P0CX80; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0016209; F:antioxidant activity; IDA:SGD.
DR GO; GO:0046870; F:cadmium ion binding; IDA:SGD.
DR GO; GO:0005507; F:copper ion binding; IDA:SGD.
DR GO; GO:0004784; F:superoxide dismutase activity; IMP:SGD.
DR GO; GO:0071585; P:detoxification of cadmium ion; IMP:SGD.
DR GO; GO:0010273; P:detoxification of copper ion; IMP:SGD.
DR GO; GO:0019430; P:removal of superoxide radicals; IDA:SGD.
DR GO; GO:0046688; P:response to copper ion; IMP:SGD.
DR Gene3D; 4.10.650.10; -; 1.
DR InterPro; IPR037130; Cup1_sf.
DR InterPro; IPR017854; Metalthion_dom_sf.
DR InterPro; IPR022710; Metalthion_dom_yeast.
DR Pfam; PF11403; Yeast_MT; 1.
DR SUPFAM; SSF57868; SSF57868; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Isopeptide bond;
KW Metal-binding; Metal-thiolate cluster; Reference proteome; Ubl conjugation.
FT PROPEP 1..8
FT /id="PRO_0000018675"
FT CHAIN 9..61
FT /note="Copper metallothionein 1-1"
FT /id="PRO_0000018676"
FT REGION 37..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 15
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT BINDING 15
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT BINDING 17
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT BINDING 17
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT BINDING 19
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT BINDING 19
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT BINDING 22
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT BINDING 22
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT BINDING 22
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT BINDING 28
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT BINDING 28
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT BINDING 32
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT BINDING 32
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="7"
FT BINDING 34
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT BINDING 34
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="7"
FT BINDING 34
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="8"
FT BINDING 38
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT BINDING 38
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="8"
FT BINDING 44
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT BINDING 44
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="8"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT BINDING 46
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="7"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT TURN 20..24
FT /evidence="ECO:0007829|PDB:1RJU"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1RJU"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1AQR"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1RJU"
SQ SEQUENCE 61 AA; 6650 MW; 688B0FF1DB986C6E CRC64;
MFSELINFQN EGHECQCQCG SCKNNEQCQK SCSCPTGCNS DDKCPCGNKS EETKKSCCSG
K
