MT1_MOUSE
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 03-AUG-2022, entry version 175.
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 PDBsum; 1DFS; -.
DR PDBsum; 1DFT; -.
DR AlphaFoldDB; P02802; -.
DR BMRB; P02802; -.
DR SMR; P02802; -.
DR BioGRID; 201578; 2.
DR STRING; 10090.ENSMUSP00000034215; -.
DR iPTMnet; P02802; -.
DR PhosphoSitePlus; P02802; -.
DR SwissPalm; P02802; -.
DR EPD; P02802; -.
DR jPOST; P02802; -.
DR MaxQB; P02802; -.
DR PaxDb; P02802; -.
DR PeptideAtlas; P02802; -.
DR PRIDE; P02802; -.
DR ProteomicsDB; 290103; -.
DR TopDownProteomics; P02802; -.
DR Ensembl; ENSMUST00000034215; ENSMUSP00000034215; ENSMUSG00000031765.
DR GeneID; 17748; -.
DR KEGG; mmu:17748; -.
DR UCSC; uc009mvw.2; mouse.
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 TreeFam; TF336054; -.
DR Reactome; R-MMU-5661231; Metallothioneins bind metals.
DR BioGRID-ORCS; 17748; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Mt1; mouse.
DR EvolutionaryTrace; P02802; -.
DR PRO; PR:P02802; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P02802; protein.
DR Bgee; ENSMUSG00000031765; Expressed in gastrula and 293 other tissues.
DR ExpressionAtlas; P02802; baseline and differential.
DR Genevisible; P02802; MM.
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:0006875; P:cellular metal ion homeostasis; IDA:MGI.
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:0006882; P:cellular zinc ion homeostasis; IMP:MGI.
DR GO; GO:0010273; P:detoxification of copper ion; IGI: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:0007263; P:nitric oxide mediated signal transduction; IMP:MGI.
DR Gene3D; 4.10.10.10; -; 1.
DR InterPro; IPR003019; Metalthion.
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; PTHR23299; 1.
DR Pfam; PF00131; Metallothio; 1.
DR PRINTS; PR00860; MTVERTEBRATE.
DR SUPFAM; SSF57868; SSF57868; 1.
DR PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
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
