ID   MT1_MOUSE               Reviewed;          61 AA.
AC   P02802; Q64485;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-SEP-2026, entry version 190.
DE   RecName: Full=Metallothionein-1;
DE            Short=MT-1;
DE   AltName: Full=Metallothionein-I;
DE            Short=MT-I;
GN   Name=Mt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC   TISSUE=Liver;
RX   PubMed=914867; DOI=10.1016/s0021-9258(17)40958-6;
RA   Huang I.-Y., Yoshida A., Tsunoo H., Nakajima H.;
RT   "Mouse liver metallothioneins. Complete amino acid sequence of
RT   metallothionein-I.";
RL   J. Biol. Chem. 252:8217-8221(1977).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7254320; DOI=10.1038/292267a0;
RA   Glanville N., Durnam D.M., Palmiter R.D.;
RT   "Structure of mouse metallothionein-I gene and its mRNA.";
RL   Nature 292:267-269(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=6935664; DOI=10.1073/pnas.77.11.6511;
RA   Durnam D.M., Perrin F., Gannon F., Palmiter R.D.;
RT   "Isolation and characterization of the mouse metallothionein-I gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:6511-6515(1980).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6277322; DOI=10.1016/0006-291x(81)90885-8;
RA   Mbikay M., Maiti I.B., Thirion J.-P.;
RT   "Cloning and sequencing of cDNA for mouse liver metallothionein-I.";
RL   Biochem. Biophys. Res. Commun. 103:825-832(1981).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8495976;
RA   Xiang J., Koropatnick J., Qi Y., Luo X., Moyana T., Li K., Chen Y.;
RT   "Production of a bifunctional hybrid molecule B72.3/metallothionein-1 by
RT   protein engineering.";
RL   Immunology 78:574-581(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9] {ECO:0007744|PDB:1DFS, ECO:0007744|PDB:1DFT}
RP   STRUCTURE BY NMR IN COMPLEX WITH CADMIUM IONS.
RX   PubMed=10631978; DOI=10.1110/ps.8.12.2630;
RA   Zangger K., Oez G., Otvos J.D., Armitage I.M.;
RT   "Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by
RT   homonuclear and heteronuclear NMR spectroscopy.";
RL   Protein Sci. 8:2630-2638(1999).
CC   -!- FUNCTION: Metallothioneins have a high content of cysteine residues
CC       that bind various heavy metals; these proteins are transcriptionally
CC       regulated by both heavy metals and glucocorticoids.
CC   -!- DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four
CC       divalent ions are chelated within cluster A of the alpha domain and are
CC       coordinated via cysteinyl thiolate bridges to 11 cysteine ligands.
CC       Cluster B, the corresponding region within the beta domain, can ligate
CC       three divalent ions to 9 cysteines.
CC   -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; S62785; AAB26768.1; -; mRNA.
DR   EMBL; J00605; AAA39527.2; -; Genomic_DNA.
DR   EMBL; AK018727; BAC25563.1; -; mRNA.
DR   EMBL; BC036990; AAH36990.1; -; mRNA.
DR   CCDS; CCDS40438.1; -.
DR   PIR; A93261; SMMSI.
DR   RefSeq; NP_038630.1; NM_013602.3.
DR   PDB; 1DFS; NMR; -; A=31-61.
DR   PDB; 1DFT; NMR; -; A=1-30.
DR   AlphaFoldDB; P02802; -.
DR   BMRB; P02802; -.
DR   MDposit; P02802; -.
DR   SMR; P02802; -.
DR   BioGRID; 201578; 2.
DR   FunCoup; P02802; 142.
DR   STRING; 10090.ENSMUSP00000034215; -.
DR   iPTMnet; P02802; -.
DR   PhosphoSitePlus; P02802; -.
DR   SwissPalm; P02802; -.
DR   jPOST; P02802; -.
DR   PaxDb; 10090-ENSMUSP00000034215; -.
DR   PeptideAtlas; P02802; -.
DR   ProteomicsDB; 290103; -.
DR   TopDownProteomics; P02802; -.
DR   Ensembl; ENSMUST00000034215.8; ENSMUSP00000034215.7; ENSMUSG00000031765.9.
DR   GeneID; 17748; -.
DR   KEGG; mmu:17748; -.
DR   UCSC; uc009mvw.2; mouse.
DR   AGR; MGI:97171; -.
DR   CTD; 17748; -.
DR   MGI; MGI:97171; Mt1.
DR   VEuPathDB; HostDB:ENSMUSG00000031765; -.
DR   eggNOG; KOG4738; Eukaryota.
DR   GeneTree; ENSGT00950000182967; -.
DR   HOGENOM; CLU_171204_2_0_1; -.
DR   InParanoid; P02802; -.
DR   OrthoDB; 9635099at2759; -.
DR   BioGRID-ORCS; 17748; 4 hits in 77 CRISPR screens.
DR   EvolutionaryTrace; P02802; -.
DR   PRO; PR:P02802; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P02802; protein.
DR   Bgee; ENSMUSG00000031765; Expressed in gastrula and 296 other cell types or tissues.
DR   ExpressionAtlas; P02802; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IBA:GO_Central.
DR   GO; GO:0071247; P:cellular response to chromate; IDA:MGI.
DR   GO; GO:0071280; P:cellular response to copper ion; IBA:GO_Central.
DR   GO; GO:0071294; P:cellular response to zinc ion; IDA:MGI.
DR   GO; GO:0010273; P:detoxification of copper ion; IGI:MGI.
DR   GO; GO:0030003; P:intracellular monoatomic cation homeostasis; IDA:MGI.
DR   GO; GO:0006882; P:intracellular zinc ion homeostasis; IMP:MGI.
DR   GO; GO:0045926; P:negative regulation of growth; ISS:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
DR   GO; GO:1900407; P:regulation of cellular response to oxidative stress; IMP:MGI.
DR   FunFam; 4.10.10.10:FF:000001; Metallothionein; 1.
DR   Gene3D; 4.10.10.10; Metallothionein Isoform II; 1.
DR   InterPro; IPR017854; Metalthion_dom_sf.
DR   InterPro; IPR023587; Metalthion_dom_sf_vert.
DR   InterPro; IPR000006; Metalthion_vert.
DR   InterPro; IPR018064; Metalthion_vert_metal_BS.
DR   PANTHER; PTHR23299; METALLOTHIONEIN; 1.
DR   PANTHER; PTHR23299:SF55; METALLOTHIONEIN-1F; 1.
DR   Pfam; PF00131; Metallothio; 1.
DR   PRINTS; PR00860; MTVERTEBRATE.
DR   SUPFAM; SSF57868; Metallothionein; 1.
DR   PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
DR   PDBsum; 1DFS; -.
DR   PDBsum; 1DFT; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Metal-binding;
KW   Metal-thiolate cluster; Reference proteome.
FT   CHAIN           1..61
FT                   /note="Metallothionein-1"
FT                   /id="PRO_0000197206"
FT   REGION          1..29
FT                   /note="Beta"
FT   REGION          30..61
FT                   /note="Alpha"
FT   BINDING         5
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         7
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         7
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         13
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         15
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         15
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="3"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         19
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="3"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         21
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         24
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         24
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="3"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         26
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         29
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="3"
FT                   /ligand_note="in cluster B"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFT"
FT   BINDING         33
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="4"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         34
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="4"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         34
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="5"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         36
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="5"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         37
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="5"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         37
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="6"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         41
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="6"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         44
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="4"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         44
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="6"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         48
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="4"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         50
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="5"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         50
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="7"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         57
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="7"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         59
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="7"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         60
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="6"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   BINDING         60
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="7"
FT                   /ligand_note="in cluster A"
FT                   /evidence="ECO:0000269|PubMed:10631978,
FT                   ECO:0007744|PDB:1DFS"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:914867"
FT   CONFLICT        23
FT                   /note="N -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="S -> G (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:1DFT"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:1DFT"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:1DFT"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1DFS"
FT   STRAND          42..47
FT                   /evidence="ECO:0007829|PDB:1DFS"
SQ   SEQUENCE   61 AA;  6018 MW;  4B3754EC759C0ADB CRC64;
     MDPNCSCSTG GSCTCTSSCA CKNCKCTSCK KSCCSCCPVG CSKCAQGCVC KGAADKCTCC
     A
//