ID   MT1_TETPI               Reviewed;         107 AA.
AC   P80394; Q8MZN1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Metallothionein-1;
DE            Short=MT-1;
DE   Contains:
DE     RecName: Full=Metallothionein-2;
DE              Short=MT-2;
DE   Flags: Precursor;
OS   Tetrahymena pigmentosa.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Boldrin F., Santovito G., Irato P., Piccinni E.;
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 3-107, AND MASS SPECTROMETRY.
RX   PubMed=7813475; DOI=10.1111/j.1432-1033.1994.t01-1-00853.x;
RA   Piccinni E., Staudenmann W., Albergoni V., de Gabrieli R., James P.;
RT   "Purification and primary structure of metallothioneins induced by cadmium
RT   in the protists Tetrahymena pigmentosa and Tetrahymena pyriformis.";
RL   Eur. J. Biochem. 226:853-859(1994).
CC   -!- FUNCTION: The metallothioneins are involved in the cellular
CC       sequestration of toxic metal ions. Binds 12 cadmium ions per molecule.
CC   -!- INDUCTION: By cadmium.
CC   -!- MASS SPECTROMETRY: [Metallothionein-1]: Mass=10850; Mass_error=1;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:7813475};
CC   -!- MASS SPECTROMETRY: [Metallothionein-2]: Mass=10722; Mass_error=1;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:7813475};
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 7 family.
CC       {ECO:0000305}.
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DR   EMBL; AF509328; AAM34287.1; -; Genomic_DNA.
DR   PIR; S50911; S50911.
DR   AlphaFoldDB; P80394; -.
DR   GO; GO:0046870; F:cadmium ion binding; IEA:InterPro.
DR   InterPro; IPR012484; Metalthion_7.
DR   Pfam; PF07846; Metallothio_Cad; 2.
PE   1: Evidence at protein level;
KW   Cadmium; Direct protein sequencing; Metal-binding; Metal-thiolate cluster.
FT   PROPEP          1..2
FT                   /evidence="ECO:0000269|PubMed:7813475"
FT                   /id="PRO_0000018667"
FT   CHAIN           3..107
FT                   /note="Metallothionein-1"
FT                   /id="PRO_0000018668"
FT   CHAIN           4..107
FT                   /note="Metallothionein-2"
FT                   /id="PRO_0000018669"
SQ   SEQUENCE   107 AA;  11096 MW;  41C85CCB1A8E465C CRC64;
     MDKVNNNCCC GENAKPCCTD PNSGCCCVSE TNNCCKSDKK ECCTGTGEGC KCTGCKCCQP
     AKSGCCCGDK AKACCTDPNS GCCCSSKTNK CCDSTNKTEC KTCECCK