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Copper metallothionein 1-2 (Cu-MT) (Cu-metallothionein) (Copper chelatin) (Copper thionein)

 MTCU2_YEAST             Reviewed;          61 AA.
P0CX81; D3DL02; P07215;
28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
22-NOV-2017, entry version 39.
RecName: Full=Copper metallothionein 1-2;
Short=Cu-MT;
Short=Cu-metallothionein;
AltName: Full=Copper chelatin;
AltName: Full=Copper thionein;
Flags: Precursor;
Name=CUP1-2; Synonyms=MTH1; OrderedLocusNames=YHR055C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6364141; DOI=10.1073/pnas.81.2.337;
Karin M., Najarian R.C., Haslinger A., Valenzuela P., Welch J.,
Fogel S.;
"Primary structure and transcription of an amplified genetic locus:
the CUP1 locus of yeast.";
Proc. Natl. Acad. Sci. U.S.A. 81:337-341(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6374656; DOI=10.1073/pnas.81.11.3332;
Butt T.R., Sternberg E.J., Gorman J.A., Clark P., Hamer D.,
Rosenberg M., Crooke S.T.;
"Copper metallothionein of yeast, structure of the gene, and
regulation of expression.";
Proc. Natl. Acad. Sci. U.S.A. 81:3332-3336(1984).
[3]
PROTEIN SEQUENCE.
PubMed=3902832;
Winge D.R., Nielson K.B., Gray W.R., Hamer D.H.;
"Yeast metallothionein. Sequence and metal-binding properties.";
J. Biol. Chem. 260:14464-14470(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2017134; DOI=10.1007/BF00261675;
Jeyaprakash A., Welch J.W., Fogel S.;
"Multicopy CUP1 plasmids enhance cadmium and copper resistance levels
in yeast.";
Mol. Gen. Genet. 225:363-368(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091229; DOI=10.1126/science.8091229;
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
VIII.";
Science 265:2077-2082(1994).
[6]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[8]
ABSORPTION SPECTROSCOPY.
PubMed=3286647;
George G.N., Byrd J., Winge D.R.;
"X-ray absorption studies of yeast copper metallothionein.";
J. Biol. Chem. 263:8199-8203(1988).
[9]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-30, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: Protects the cell against copper toxicity by tightly
chelating copper ions. May also act as a depository for copper
designated for the effective transfer into the apo forms of copper
proteins.
-!- DOMAIN: Contains 1 metal-binding domain: 6 to 8 copper ions are
chelated within a single copper-thiolate cluster and are
coordinated via cysteinyl thiolate bridges to 10 cysteine ligands.
6 copper ions are trigonally coordinated, whereas the other 2 are
only digonally coordinated.
-!- MISCELLANEOUS: There are 2 copies for copper thionein in yeast.
The 2 identical copies CUP1-1 and CUP1-2 are arranged in tandem.
-!- SIMILARITY: Belongs to the metallothionein superfamily. Type 12
family. {ECO:0000305}.
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EMBL; U00061; AAB68384.1; -; Genomic_DNA.
EMBL; AY693077; AAT93096.1; -; Genomic_DNA.
EMBL; BK006934; DAA06746.1; -; Genomic_DNA.
PIR; S14049; S14049.
RefSeq; NP_011920.1; NM_001179183.1.
RefSeq; NP_011922.1; NM_001179185.1.
ProteinModelPortal; P0CX81; -.
SMR; P0CX81; -.
BioGrid; 36485; 6.
BioGrid; 36487; 54.
iPTMnet; P0CX81; -.
EnsemblFungi; YHR053C; YHR053C; YHR053C.
EnsemblFungi; YHR055C; YHR055C; YHR055C.
GeneID; 856450; -.
GeneID; 856452; -.
KEGG; sce:YHR053C; -.
KEGG; sce:YHR055C; -.
SGD; S000001097; CUP1-2.
GeneTree; ENSGT00390000004371; -.
OrthoDB; EOG092C5V5Y; -.
BioCyc; YEAST:G3O-31109-MONOMER; -.
PRO; PR:P0CX81; -.
Proteomes; UP000002311; Chromosome VIII.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0016209; F:antioxidant activity; IDA:SGD.
GO; GO:0046870; F:cadmium ion binding; IDA:SGD.
GO; GO:0005507; F:copper ion binding; IDA:SGD.
GO; GO:0004784; F:superoxide dismutase activity; IMP:SGD.
GO; GO:0071585; P:detoxification of cadmium ion; IMP:SGD.
GO; GO:0010273; P:detoxification of copper ion; IMP:SGD.
GO; GO:0019430; P:removal of superoxide radicals; IDA:SGD.
GO; GO:0046688; P:response to copper ion; IMP:SGD.
Gene3D; 4.10.650.10; -; 1.
InterPro; IPR037130; Cup1_sf.
InterPro; IPR017854; Metalthion_dom_sf.
InterPro; IPR022710; Metalthion_dom_yeast.
Pfam; PF11403; Yeast_MT; 1.
SUPFAM; SSF57868; SSF57868; 1.
1: Evidence at protein level;
Complete proteome; Copper; Direct protein sequencing; Isopeptide bond;
Metal-binding; Metal-thiolate cluster; Reference proteome;
Ubl conjugation.
PROPEP 1 8
/FTId=PRO_0000410444.
CHAIN 9 61 Copper metallothionein 1-2.
/FTId=PRO_0000410445.
METAL 15 15 Copper 1.
METAL 15 15 Copper 2.
METAL 17 17 Copper 1.
METAL 17 17 Copper 3.
METAL 19 19 Copper 4.
METAL 19 19 Copper 5.
METAL 22 22 Copper 3.
METAL 22 22 Copper 4.
METAL 22 22 Copper 6.
METAL 28 28 Copper 2.
METAL 28 28 Copper 6.
METAL 32 32 Copper 1.
METAL 32 32 Copper 7.
METAL 34 34 Copper 3.
METAL 34 34 Copper 7.
METAL 34 34 Copper 8.
METAL 38 38 Copper 5.
METAL 38 38 Copper 8.
METAL 44 44 Copper 4.
METAL 44 44 Copper 8.
METAL 46 46 Copper 6.
METAL 46 46 Copper 7.
CROSSLNK 30 30 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
SEQUENCE 61 AA; 6650 MW; 688B0FF1DB986C6E CRC64;
MFSELINFQN EGHECQCQCG SCKNNEQCQK SCSCPTGCNS DDKCPCGNKS EETKKSCCSG
K


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