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Reviewed, UniProtKB/Swiss-Prot Q9XST5 (MT2_CANFA)

Last modified September 2, 2008. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Metallothionein-2
      Short name=MT-2
Alternative name(s):
    Metallothionein-II
      Short name=MT-II
Gene names
Name: MT2A
Synonyms: MT2
ORF Names: B28
OrganismCanis familiaris (Dog)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length61 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

   LigandMetal-binding
Metal-thiolate cluster
   PTMAcetylation
   Technical termDirect protein sequencing

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 6161Metallothionein-2

Regions

Region1 – 2929Beta
Region30 – 6132Alpha

Sites

Metal binding51Cluster B By similarity
Metal binding71Cluster B By similarity
Metal binding131Cluster B By similarity
Metal binding151Cluster B By similarity
Metal binding191Cluster B By similarity
Metal binding211Cluster B By similarity
Metal binding241Cluster B By similarity
Metal binding261Cluster B By similarity
Metal binding291Cluster B By similarity
Metal binding331Cluster A By similarity
Metal binding341Cluster A By similarity
Metal binding361Cluster A By similarity
Metal binding371Cluster A By similarity
Metal binding411Cluster A By similarity
Metal binding441Cluster A By similarity
Metal binding481Cluster A By similarity
Metal binding501Cluster A By similarity
Metal binding571Cluster A By similarity
Metal binding591Cluster A By similarity
Metal binding601Cluster A By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue511N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9XST5-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 7B0A7C54E272C448

FASTA616,012
        10         20         30         40         50         60 
MDPNCSCAAG GSCTCAGSCK CKECRCTSCK KSCCSCCPVG CAKCAQGCIC KGASDKCSCC 


A 

« Hide

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.

Cross-references

Sequence databases

AB028042 mRNA. Translation: BAA87327.1.
AJ388530 mRNA. Translation: CAB46832.1.
RefSeqNP_001003149.1.
UniGeneCfa.3542

3D structure databases

HSSPHSSP built from PDB template 1MHU based on UniProtKB P02795.
SMRQ9XST5. Positions 1-61.
ModBaseSearch...

Genome annotation databases

EnsemblENSCAFG00000023759. Canis familiaris. [Contig view]
GeneID403768.
KEGGcfa:403768.

Phylogenomic databases

HOVERGENQ9XST5.

Family and domain databases

InterProIPR002400. GF_cysknot.
IPR003019. Metallothionein_sfam_euk.
IPR000006. Metallothionein_vert.
[Graphical view]
Gene3DG3DSA:4.10.10.10. Metallothionein_vert. 1 hit.
PANTHERPTHR23299. Metallothionein_vert. 1 hit.
PfamPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSPR00438. GFCYSKNOT.
PR00860. MTVERTEBRATE.
PROSITEPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]
ProDomQ9XST5.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameMT2_CANFA
AccessionPrimary (citable) accession number: Q9XST5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 1, 1999
Last modified: September 2, 2008
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Metallothioneins

Classification of metallothioneins and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents