P68303 (MT2_MACFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 33.
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-2 Short name=MT-2 Alternative name(s): Metallothionein-II Short name=MT-II | ||
| Gene names |
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| Organism | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) | ||
| Taxonomic identifier | 9541 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
Protein attributes
| Sequence length | 61 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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. |
| Miscellaneous | This metallothionein binds zinc. |
| Sequence similarities | Belongs to the metallothionein superfamily. Type 1 family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Cadmium Metal-binding Metal-thiolate cluster Zinc |
| PTM | Acetylation |
| 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-2 | PRO_0000197246 | |||||
Regions | |||||||||
| Region | 1 – 29 | 29 | Beta | ||||||
| Region | 20 – 25 | 6 | Antigenic epitope | ||||||
| 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 | ||||||
| Modified residue | 51 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
References
| [1] | "Studies on the mechanism of early onset macular degeneration in cynomolgus monkeys. II. Suppression of metallothionein synthesis in the retina in oxidative stress." Nicolas M.G., Fujiki K., Murayama K., Suzuki M.T., Shindo N., Hotta Y., Iwata F., Fujimura T., Yoshikawa Y., Cho F., Kanai A. Exp. Eye Res. 62:399-408(1996) [PubMed: 8795458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Retina. |
| + | Additional computationally mapped references. |
Cross-references
3D structure databases | |
|---|---|
| ProteinModelPortal | P68303. |
| SMR | P68303. Positions 1-61. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG009063. |
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 | MT2_MACFA | ||||||||
| Accession | Primary (citable) accession number: P68303 Secondary accession number(s): P02796 | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |