P55945 (MT_PSEAM) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 59.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Metallothionein Short name=MT | ||
| Gene names |
| ||
| Organism | Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus) | ||
| Taxonomic identifier | 8265 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Pleuronectiformes › Pleuronectoidei › Pleuronectidae › Pleuronectinae › Pseudopleuronectes![]() |
Protein attributes
| Sequence length | 60 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Metallothioneins have a high content of cysteine residues that bind various heavy metals 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 | Copper Metal-binding Metal-thiolate cluster |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 60 | 60 | Metallothionein | PRO_0000197310 | |||||
Regions | |||||||||
| Region | 1 – 28 | 28 | Beta | ||||||
| Region | 29 – 60 | 32 | Alpha | ||||||
Sites | |||||||||
| Metal binding | 4 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 6 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 12 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 14 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 18 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 20 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 23 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 25 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 28 | 1 | Divalent metal cation; cluster B By similarity | ||||||
| Metal binding | 32 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 33 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 35 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 36 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 40 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 43 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 47 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 49 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 54 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 58 | 1 | Divalent metal cation; cluster A By similarity | ||||||
| Metal binding | 59 | 1 | Divalent metal cation; cluster A By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine | ||||||
Sequences
References
| [1] | "Molecular cloning of metallothionein cDNA and analysis of metallothionein gene expression in winter flounder tissues." Chan K.-M., Davidson W.S., Hew C.-L., Fletcher G.L. Can. J. Zool. 67:2520-2527(1989) Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-25. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X13594 mRNA. Translation: CAA31930.1. |
3D structure databases | |
| ProteinModelPortal | P55945. |
| SMR | P55945. Positions 2-28, 31-60. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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_PSEAM | ||||||||
| Accession | Primary (citable) accession number: P55945 Secondary accession number(s): Q6LBT7 | ||||||||
| 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 |

Clusters with
