P23038 · MT_CRAVI
- ProteinMetallothionein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
The metallothioneins are involved in the cellular sequestration of toxic metal ions.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 15 | Cd2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 19 | Cd2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 19 | Cd2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 24 | Cd2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 26 | Cd2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 30 | Cd2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 32 | Cd2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 32 | Cd2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 36 | Cd2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 38 | Cd2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 41 | Cd2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 41 | Cd2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 45 | Cd2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 47 | Cd2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 53 | Cd2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 55 | Cd2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 55 | Cd2+ 6 (UniProtKB | ChEBI) | |||
Binding site | 59 | Cd2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 59 | Cd2+ 5 (UniProtKB | ChEBI) | |||
Binding site | 65 | Cd2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 67 | Cd2+ 6 (UniProtKB | ChEBI) | |||
Binding site | 71 | Cd2+ 6 (UniProtKB | ChEBI) | |||
Binding site | 73 | Cd2+ 4 (UniProtKB | ChEBI) | |||
Binding site | 73 | Cd2+ 6 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMetallothionein
- Short namesMT
Organism names
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Mollusca > Bivalvia > Autobranchia > Pteriomorphia > Ostreida > Ostreoidea > Ostreidae > Crassostrea
Accessions
- Primary accessionP23038
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Initiator methionine | 1 | Removed | |||
Modified residue | 2 | N-acetylserine | |||
Chain | PRO_0000197322 | 2-75 | Metallothionein | ||
Keywords
- PTM
PTM databases
Expression
Induction
By cadmium.
Structure
Family & Domains
Sequence similarities
Belongs to the metallothionein superfamily. Type 2 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length75
- Mass (Da)7,345
- Last updated2007-01-23 v3
- Checksum636480D23D314667
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X59862 EMBL· GenBank· DDBJ | CAA42522.1 EMBL· GenBank· DDBJ | mRNA |