O18842 (MT_BALMY) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 60.
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 Short name=MT |
| Organism | Balaena mysticetus (Bowhead whale) |
| Taxonomic identifier | 27602 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Cetacea › Mysticeti › Balaenidae › Balaena |
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 By similarity. |
| Subunit structure | Monomer By similarity. |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Metal-thiolate cluster |
| PTM | Acetylation |
| Gene Ontology (GO) | |
| Biological_process | cellular response to zinc ion Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of growthInferred 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 | PRO_0000197257 | |||||
Regions | |||||||||
| Region | 1 – 29 | 29 | Beta | ||||||
| Region | 30 – 61 | 32 | Alpha | ||||||
Sites | |||||||||
| Metal binding | 5 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 7 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 13 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 15 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 19 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 21 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 24 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 26 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 29 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 33 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 34 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 36 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 37 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 41 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 44 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 48 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 50 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 57 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 59 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 60 | 1 | Divalent metal cation; cluster A By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
Sequences
References
| [1] | Kaysen J., O'Hara T., Goodwin T., Linnehan R., Hammond T. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF022117 mRNA. Translation: AAB72006.1. |
3D structure databases | |
| ProteinModelPortal | O18842. |
| SMR | O18842. Positions 1-61. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG009063. |
Family and domain databases | |
| Gene3D | 4.10.10.10. 1 hit. |
| InterPro | IPR017854. Metalthion_dom. IPR023587. Metalthion_dom_vert. IPR003019. Metalthion_sfam_euk. IPR000006. Metalthion_vert. IPR018064. Metalthion_vert_metal_BS. [Graphical view] |
| PANTHER | PTHR23299. PTHR23299. 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 | MT_BALMY | ||||||||
| Accession | Primary (citable) accession number: O18842 | ||||||||
| 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 |