Q6J1T3 · MT_SCYTO
- ProteinMetallothionein
- Genemt
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Metallothioneins have a high content of cysteine residues that bind various heavy metals.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 7 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 9 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 9 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 14 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 16 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 16 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 20 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 22 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 25 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 25 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 27 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 35 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | |||
Binding site | 39 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 40 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 40 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 42 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 43 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 43 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 47 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 50 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 50 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 54 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 56 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 56 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 64 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 66 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 67 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | |||
Binding site | 67 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Biological Process | cellular response to cadmium ion | |
Biological Process | cellular response to copper ion | |
Biological Process | cellular response to zinc ion | |
Biological Process | detoxification of copper ion | |
Biological Process | intracellular zinc ion homeostasis |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMetallothionein
- Short namesMT
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Chondrichthyes > Elasmobranchii > Galeomorphii > Galeoidea > Carcharhiniformes > Scyliorhinidae > Scyliorhinus
Accessions
- Primary accessionQ6J1T3
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000197319 | 1-68 | Metallothionein | ||
Structure
Family & Domains
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.