MT2_CANGA
ID MT2_CANGA Reviewed; 52 AA.
AC P15114;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Metallothionein-2;
DE Short=MT-2;
DE AltName: Full=Metallothionein-II;
DE Short=MT-II;
DE Contains:
DE RecName: Full=Metallothionein-2';
DE Short=MT-2';
DE AltName: Full=Metallothionein-II';
DE Short=MT-II';
GN Name=MT-II; OrderedLocusNames=CAGL0H04257g;
GN and
GN Name=MT-IIB; OrderedLocusNames=CAGL0H04279g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-39.
RX PubMed=2584191; DOI=10.1016/s0021-9258(19)47175-5;
RA Mehra R.K., Garey J.R., Butt T.R., Gray W.R., Winge D.R.;
RT "Candida glabrata metallothioneins. Cloning and sequence of the genes and
RT characterization of proteins.";
RL J. Biol. Chem. 264:19747-19753(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2318858; DOI=10.1016/s0021-9258(19)39335-4;
RA Mehra R.K., Garey J.R., Winge D.R.;
RT "Selective and tandem amplification of a member of the metallothionein gene
RT family in Candida glabrata.";
RL J. Biol. Chem. 265:6369-6375(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1339367; DOI=10.1016/0378-1119(92)90709-x;
RA Mehra R.K., Thorvaldsen J.L., Macreadie I.G., Winge D.R.;
RT "Disruption analysis of metallothionein-encoding genes in Candida
RT glabrata.";
RL Gene 114:75-80(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-20 AND 35-52.
RX PubMed=3194392; DOI=10.1073/pnas.85.23.8815;
RA Mehra R.K., Tarbet B.E., Gray W.R., Winge D.R.;
RT "Metal-specific synthesis of two metallothioneins and gamma-glutamyl
RT peptides in Candida glabrata.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8815-8819(1988).
CC -!- FUNCTION: The metallothioneins are involved in the cellular
CC sequestration of toxic metal ions.
CC -!- INDUCTION: Both MT-I and MT-II genes are regulated by copper ion in a
CC concentration-dependent fashion, and both are inducible by silver but
CC not by cadmium salts.
CC -!- MISCELLANEOUS: MT-II might bind nearly 10 mol eq of Cu(+).
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 10 family.
CC {ECO:0000305}.
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DR EMBL; J05134; AAA35273.1; -; Genomic_DNA.
DR EMBL; J05398; AAA35274.1; -; Genomic_DNA.
DR EMBL; M86727; AAA35275.1; -; Genomic_DNA.
DR EMBL; CR380954; CAG59913.1; -; Genomic_DNA.
DR EMBL; CR380954; CAG59914.1; -; Genomic_DNA.
DR PIR; B31252; B31252.
DR PIR; JC1197; JC1197.
DR RefSeq; XP_002999586.1; XM_002999540.1.
DR RefSeq; XP_446980.1; XM_446980.1.
DR RefSeq; XP_446981.1; XM_446981.1.
DR AlphaFoldDB; P15114; -.
DR EnsemblFungi; CAG59913; CAG59913; CAGL0H04257g.
DR EnsemblFungi; CAG59914; CAG59914; CAGL0H04279g.
DR GeneID; 2888780; -.
DR GeneID; 2888781; -.
DR GeneID; 9488054; -.
DR KEGG; cgr:CAGL0H04257g; -.
DR KEGG; cgr:CAGL0H04279g; -.
DR KEGG; cgr:CAGL0L01831g; -.
DR CGD; CAL0135114; CAGL0L01831g.
DR CGD; CAL0131544; MT-II.
DR CGD; CAL0129811; MT-IIB.
DR VEuPathDB; FungiDB:CAGL0H04257g; -.
DR VEuPathDB; FungiDB:CAGL0H04279g; -.
DR VEuPathDB; FungiDB:CAGL0L01831g; -.
DR HOGENOM; CLU_3087043_0_0_1; -.
DR OMA; CACENTC; -.
DR Proteomes; UP000002428; Chromosome H.
DR GO; GO:0005507; F:copper ion binding; IDA:CGD.
DR GO; GO:0071280; P:cellular response to copper ion; IDA:CGD.
DR GO; GO:0071292; P:cellular response to silver ion; IDA:CGD.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Metal-binding; Metal-thiolate cluster;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3194392"
FT CHAIN 2..52
FT /note="Metallothionein-2"
FT /id="PRO_0000045887"
FT CHAIN 8..52
FT /note="Metallothionein-2'"
FT /id="PRO_0000045888"
FT REPEAT 43..47
FT REPEAT 48..52
SQ SEQUENCE 52 AA; 5585 MW; ABD19E284CC34D22 CRC64;
MPEQVNCQYD CHCSNCACEN TCNCCAKPAC ACTNSASNEC SCQTCKCQTC KC
