P58280 (MT1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 56.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·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 | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
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. |
| Subunit structure | Monomer. |
| 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
| Keywords | |
|---|---|
| Ligand | Cadmium Copper Metal-binding Metal-thiolate cluster Zinc |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | negative regulation of growth Inferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | nucleus Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasmInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 61 | 61 | Metallothionein-1 | PRO_0000197197 | |||||
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 By similarity | ||||||
Sequences
References
| [1] | "(Cu,Zn)-metallothioneins from fetal bovine liver. Chemical and spectroscopic properties." Muenger K., Germann U.A., Beltramini M., Niedermann D., Baitella-Eberle G., Kaegi J.H.R., Lerch K. J. Biol. Chem. 260:10032-10038(1985) [PubMed: 4019500] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| IPI | IPI00702893. |
| PIR | A23889. |
3D structure databases | |
| ProteinModelPortal | P58280. |
| SMR | P58280. Positions 1-61. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P58280. |
Proteomic databases | |
| PRIDE | P58280. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG009063. |
| InParanoid | P58280. |
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. |
| 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... |
Entry information
| Entry name | MT1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P58280 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Metallothioneins Classification of metallothioneins and list of entries |
| SIMILARITY comments Index of protein domains and families |