P68304 (MT2_CHLAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 35.
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 |
| ||
| Organism | Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops) | ||
| Taxonomic identifier | 9534 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Chlorocebus |
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_0000197233 | |||||
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] | "Cloning and sequence analysis of two monkey metallothionein cDNAs." Schmidt C.J., Hamer D.H. Gene 24:137-146(1983) [PubMed: 6414888] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Kidney. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | V01532 Genomic DNA. Translation: CAA24771.1. |
| PIR | SMMK2. A03272. |
3D structure databases | |
| ProteinModelPortal | P68304. |
| SMR | P68304. Positions 1-61. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P68304. |
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_CHLAE | ||||||||
| Accession | Primary (citable) accession number: P68304 Secondary accession number(s): P02796 | ||||||||
| 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 |