P02802 (MT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 106.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Metallothionein-1 Short name=MT-1 Alternative name(s): Metallothionein-I Short name=MT-I | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 61 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. |
| Domain | Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines. |
| Sequence similarities | Belongs to the metallothionein superfamily. Type 1 family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||
Molecule processing | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 61 | 61 | Metallothionein-1 | PRO_0000197206 | |||||||||||||||
Regions | |||||||||||||||||||
| Region | 1 – 29 | 29 | Beta | ||||||||||||||||
| Region | 30 – 61 | 32 | Alpha | ||||||||||||||||
Sites | |||||||||||||||||||
| Metal binding | 5 | 1 | Divalent metal cation; cluster B | ||||||||||||||||
| Metal binding | 7 | 1 | Divalent metal cation; cluster B | ||||||||||||||||
| Metal binding | 13 | 1 | Divalent metal cation; cluster B | ||||||||||||||||
| Metal binding | 15 | 1 | Divalent metal cation; cluster B | ||||||||||||||||
| Metal binding | 19 | 1 | Divalent metal cation; cluster B | ||||||||||||||||
| Metal binding | 21 | 1 | Divalent metal cation; cluster B | ||||||||||||||||
| Metal binding | 24 | 1 | Divalent metal cation; cluster B | ||||||||||||||||
| Metal binding | 26 | 1 | Divalent metal cation; cluster B | ||||||||||||||||
| Metal binding | 29 | 1 | Divalent metal cation; cluster B | ||||||||||||||||
| Metal binding | 33 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 34 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 36 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 37 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 41 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 44 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 48 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 50 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 57 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 59 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
| Metal binding | 60 | 1 | Divalent metal cation; cluster A | ||||||||||||||||
Amino acid modifications | |||||||||||||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.1 | ||||||||||||||||
Experimental info | |||||||||||||||||||
| Sequence conflict | 23 | 1 | N → D AA sequence Ref.1 | ||||||||||||||||
| Sequence conflict | 32 | 1 | S → G Ref.4 | ||||||||||||||||
Secondary structure | |||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||
| Beta strand | 9 – 11 | 3 | |||||||||||||||||
| Beta strand | 20 – 23 | 4 | |||||||||||||||||
| Beta strand | 25 – 28 | 4 | |||||||||||||||||
| Beta strand | 35 – 37 | 3 | |||||||||||||||||
| Beta strand | 42 – 47 | 6 | |||||||||||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "Mouse liver metallothioneins. Complete amino acid sequence of metallothionein-I." Huang I.-Y., Yoshida A., Tsunoo H., Nakajima H. J. Biol. Chem. 252:8217-8221(1977) [PubMed: 914867] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver. |
| [2] | "Structure of mouse metallothionein-I gene and its mRNA." Glanville N., Durnam D.M., Palmiter R.D. Nature 292:267-269(1981) [PubMed: 7254320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Isolation and characterization of the mouse metallothionein-I gene." Durnam D.M., Perrin F., Gannon F., Palmiter R.D. Proc. Natl. Acad. Sci. U.S.A. 77:6511-6515(1980) [PubMed: 6935664] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver. |
| [4] | "Cloning and sequencing of cDNA for mouse liver metallothionein-I." Mbikay M., Maiti I.B., Thirion J.-P. Biochem. Biophys. Res. Commun. 103:825-832(1981) [PubMed: 6277322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [5] | "Production of a bifunctional hybrid molecule B72.3/metallothionein-1 by protein engineering." Xiang J., Koropatnick J., Qi Y., Luo X., Moyana T., Li K., Chen Y. Immunology 78:574-581(1993) [PubMed: 8495976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. |
| [6] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney. |
| [7] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon. |
| [8] | "Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy." Zangger K., Oez G., Otvos J.D., Armitage I.M. Protein Sci. 8:2630-2638(1999) [PubMed: 10631978] [Abstract] Cited for: STRUCTURE BY NMR. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | S62785 mRNA. Translation: AAB26768.1. J00605 Genomic DNA. Translation: AAA39527.2. AK018727 mRNA. Translation: BAC25563.1. BC036990 mRNA. Translation: AAH36990.1. | ||||||||||||||||||
| IPI | IPI00113696. | ||||||||||||||||||
| PIR | SMMSI. A93261. | ||||||||||||||||||
| RefSeq | NP_038630.1. NM_013602.3. | ||||||||||||||||||
| UniGene | Mm.192991. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | P02802. | ||||||||||||||||||
| SMR | P02802. Positions 1-61. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | P02802. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P02802. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | P02802. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSMUST00000034215; ENSMUSP00000034215; ENSMUSG00000031765. | ||||||||||||||||||
| GeneID | 17748. | ||||||||||||||||||
| KEGG | mmu:17748. | ||||||||||||||||||
| UCSC | uc009mvw.2. mouse. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 17748. | ||||||||||||||||||
| MGI | MGI:97171. Mt1. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | maNOG21730. | ||||||||||||||||||
| GeneTree | ENSGT00390000010461. | ||||||||||||||||||
| HOVERGEN | HBG009063. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P02802. | ||||||||||||||||||
| Bgee | P02802. | ||||||||||||||||||
| CleanEx | MM_MT1. | ||||||||||||||||||
| Genevestigator | P02802. | ||||||||||||||||||
| GermOnline | ENSMUSG00000031765. Mus musculus. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR017854. Metalthion_dom. IPR023587. Metalthion_dom_vert. IPR003019. Metalthion_sfam_euk. IPR000006. Metalthion_vert. IPR018064. Metalthion_vert_metal_BS. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:4.10.10.10. Metallothionein_vert. 1 hit. | ||||||||||||||||||
| KO | K14739. | ||||||||||||||||||
| PANTHER | PTHR23299. Metallothionein_vert. 1 hit. | ||||||||||||||||||
| Pfam | PF00131. Metallothio. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00860. MTVERTEBRATE. | ||||||||||||||||||
| SUPFAM | SSF57868. Metallothionein_sfam. 1 hit. | ||||||||||||||||||
| PROSITE | PS00203. METALLOTHIONEIN_VRT. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| NextBio | 292401. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | MT1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P02802 Secondary accession number(s): Q64485 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Metallothioneins Classification of metallothioneins and list of entries |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with