P29499 (MT1_HOMAM) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 63.
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-1 Alternative name(s): CuMT-1 |
| Organism | Homarus americanus (American lobster) |
| Taxonomic identifier | 6706 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Pleocyemata › Astacidea › Nephropoidea › Nephropidae › Homarus![]() |
Protein attributes
| Sequence length | 58 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. The different forms of lobster metallothioneins may have different biological functions. Class I MTS in marine crustacea are involved in the sequestration of elevated levels of heavy-metal ions. Binds 6 metal ions. Known to bind cadmium. |
| Sequence similarities | Belongs to the metallothionein superfamily. Type 3 family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Cadmium Copper Metal-binding Metal-thiolate cluster |
| Technical term | 3D-structure 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 – 58 | 58 | Metallothionein-1 | PRO_0000197342 | |||||||||||||
Regions | |||||||||||||||||
| Region | 1 – 28 | 28 | Beta | ||||||||||||||
| Region | 29 – 58 | 30 | Alpha | ||||||||||||||
Sites | |||||||||||||||||
| Metal binding | 4 | 1 | Divalent metal cation; cluster B | ||||||||||||||
| Metal binding | 5 | 1 | Divalent metal cation; cluster B | ||||||||||||||
| Metal binding | 9 | 1 | Divalent metal cation; cluster B | ||||||||||||||
| Metal binding | 11 | 1 | Divalent metal cation; cluster B | ||||||||||||||
| Metal binding | 16 | 1 | Divalent metal cation; cluster B | ||||||||||||||
| Metal binding | 20 | 1 | Divalent metal cation; cluster B | ||||||||||||||
| Metal binding | 22 | 1 | Divalent metal cation; cluster B | ||||||||||||||
| Metal binding | 25 | 1 | Divalent metal cation; cluster B | ||||||||||||||
| Metal binding | 27 | 1 | Divalent metal cation; cluster B | ||||||||||||||
| Metal binding | 30 | 1 | Divalent metal cation; cluster A | ||||||||||||||
| Metal binding | 33 | 1 | Divalent metal cation; cluster A | ||||||||||||||
| Metal binding | 37 | 1 | Divalent metal cation; cluster A | ||||||||||||||
| Metal binding | 39 | 1 | Divalent metal cation; cluster A | ||||||||||||||
| Metal binding | 45 | 1 | Divalent metal cation; cluster A | ||||||||||||||
| Metal binding | 49 | 1 | Divalent metal cation; cluster A | ||||||||||||||
| Metal binding | 53 | 1 | Divalent metal cation; cluster A | ||||||||||||||
| Metal binding | 55 | 1 | Divalent metal cation; cluster A | ||||||||||||||
| Metal binding | 56 | 1 | Divalent metal cation; cluster A | ||||||||||||||
Secondary structure | |||||||||||||||||
Helix Strand Turn | |||||||||||||||||
| Beta strand | 6 – 8 | 3 | |||||||||||||||
| Beta strand | 11 – 14 | 4 | |||||||||||||||
| Helix | 31 – 33 | 3 | |||||||||||||||
| Helix | 45 – 48 | 4 | |||||||||||||||
Sequences
References
| [1] | "Structural and functional diversity of copper-metallothioneins from the American lobster Homarus americanus." Brouwer M., Winge D.R., Gray W.R. J. Inorg. Biochem. 35:289-303(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Hepatopancreas. |
| [2] | "Sequential proton resonance assignments and metal cluster topology of lobster metallothionein-1." Zhu Z., Derose E.F., Mullen G.P., Petering D.H., Shaw C.F. III Biochemistry 33:8858-8865(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PIR | A37039. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ProteinModelPortal | P29499. | ||||||||||||||||||
| SMR | P29499. Positions 1-28. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR002045. Metalthion_3_crustacean. IPR017854. Metalthion_dom. IPR003019. Metalthion_sfam_euk. [Graphical view] | ||||||||||||||||||
| Pfam | PF00131. Metallothio. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00858. MTCRUSTACEAN. | ||||||||||||||||||
| SUPFAM | SSF57868. Metallothionein_sfam. 2 hits. | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P29499. | ||||||||||||||||||
Entry information
| Entry name | MT1_HOMAM | ||||||||
| Accession | Primary (citable) accession number: P29499 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Metallothioneins Classification of metallothioneins and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
