Q9XST5 (MT2_CANFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 73.
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-2 Short name=MT-2 Alternative name(s): Metallothionein-II Short name=MT-II | ||||||
| Gene names |
| ||||||
| Organism | Canis familiaris (Dog) (Canis lupus familiaris) | ||||||
| Taxonomic identifier | 9615 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis |
Protein attributes
| Sequence length | 61 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; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. |
| 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 |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | negative regulation of growth Inferred 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-2 | PRO_0000197199 | |||||
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 | ||||||
| Modified residue | 51 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "Canine hepatic lysosomal copper protein: identification as metallothionein." Lerch K., Johnson G.F., Grushoff P.S., Sternlieb I. Arch. Biochem. Biophys. 243:108-114(1985) [PubMed: 4062298] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Liver. |
| [2] | "Molecular cloning and expression of canine metallothionein-II." Kobayashi K., Morita T., Shimada A. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Beagle. Tissue: Kidney. |
| [3] | "A method for the large-scale cloning of nuclear proteins and nuclear targeting sequences on a functional basis." Pichon B., Mercan D., Pouillon V., Christophe-Hobertus C., Christophe D. Anal. Biochem. 284:231-239(2000) [PubMed: 10964405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thyroid. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB028042 mRNA. Translation: BAA87327.1. AJ388530 mRNA. Translation: CAB46832.1. |
| RefSeq | NP_001003149.1. NM_001003149.1. |
| UniGene | Cfa.3542. |
3D structure databases | |
| ProteinModelPortal | Q9XST5. |
| SMR | Q9XST5. Positions 1-61. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSCAFT00000014487; ENSCAFP00000013399; ENSCAFG00000023759. |
| GeneID | 403768. |
| KEGG | cfa:403768. |
Organism-specific databases | |
| CTD | 4502. |
Phylogenomic databases | |
| eggNOG | maNOG21730. |
| GeneTree | ENSGT00390000010461. |
| InParanoid | Q9XST5. |
| OMA | NCAGSCK. |
Family and domain databases | |
| InterPro | IPR017854. Metalthion_dom. IPR023587. Metalthion_dom_vert. IPR003019. Metalthion_sfam_euk. IPR000006. Metalthion_vert. IPR018064. Metalthion_vert_metal_BS. [Graphical view] |
| Gene3D | G3DSA:4.10.10.10. Metallothionein_vert. 1 hit. |
| KO | K14739. |
| PANTHER | PTHR23299. Metallothionein_vert. 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 | MT2_CANFA | ||||||||
| Accession | Primary (citable) accession number: Q9XST5 | ||||||||
| 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