P25127 · MT_ESOLU
- ProteinMetallothionein
- Genemt
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceInferred from homology
- Annotation score3/5
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 | 4 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 6 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 6 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 12 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 14 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 14 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 18 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 20 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 23 | a divalent metal cation 1 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 23 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 25 | a divalent metal cation 2 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 28 | a divalent metal cation 3 (UniProtKB | ChEBI); in cluster B | ||||
Sequence: C | ||||||
Binding site | 32 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 33 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 33 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 35 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 36 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 36 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 40 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 43 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 43 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 47 | a divalent metal cation 4 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 49 | a divalent metal cation 5 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 49 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 54 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 58 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 59 | a divalent metal cation 6 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C | ||||||
Binding site | 59 | a divalent metal cation 7 (UniProtKB | ChEBI); in cluster A | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Biological Process | angiogenesis | |
Biological Process | positive regulation of cell migration involved in sprouting angiogenesis | |
Biological Process | positive regulation of vascular endothelial growth factor production | |
Biological Process | response to cadmium ion | |
Biological Process | response to copper ion | |
Biological Process | response to methylmercury | |
Biological Process | response to zinc ion |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMetallothionein
- Short namesMT
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Protacanthopterygii > Esociformes > Esocidae > Esox
Accessions
- Primary accessionP25127
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000197283 | 1-60 | Metallothionein | |||
Sequence: MDPCECSKTGSCNCGGSCKCSNCACTSCKKSCCSCCPSGCSKCASGCICKGKTCDTSCCQ |
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-28 | Beta | ||||
Sequence: MDPCECSKTGSCNCGGSCKCSNCACTSC | ||||||
Region | 29-60 | Alpha | ||||
Sequence: KKSCCSCCPSGCSKCASGCICKGKTCDTSCCQ |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length60
- Mass (Da)5,979
- Last updated1992-05-01 v1
- Checksum9EA1E43F95F8D97E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X59392 EMBL· GenBank· DDBJ | CAA42035.1 EMBL· GenBank· DDBJ | mRNA | ||
X70042 EMBL· GenBank· DDBJ | CAA49636.1 EMBL· GenBank· DDBJ | Genomic DNA |