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Reviewed, UniProtKB/Swiss-Prot P67981 (MT2_CRIGR)

Last modified July 22, 2008. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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(s)=MT-2
Alternative name(s):
    Metallothionein-II
      Short name(s)=MT-II
Gene names
Name: MT2
OrganismCricetulus griseus (Chinese hamster)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length61 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

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

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

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
P67981-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 600D4243AD4E14F4

FASTA616,146
        10         20         30         40         50         60 
MDPNCSCATD GSCSCAGSCK CKECKCTTCK KSCCSCCPVG CAKCSQGCVC KEASDKCSCC 


A 

« Hide

References

[1]"cDNA cloning and nucleotide sequence comparison of Chinese hamster metallothionein I and II mRNAs."
Griffith B.B., Walters R.A., Enger M.D., Hildebrand C.E., Griffith J.K.
Nucleic Acids Res. 11:901-910(1983) [PubMed: 6687636] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of Chinese hamster metallothionein II gene and its 5' flanking region."
Hung S.H., Yu C.W., Chou T.M., Huang P.C., Lin L.Y.
Biochim. Biophys. Acta 1090:255-258(1991) [PubMed: 1932120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Sequence homology of Chinese hamster metallothionein genes I and II to those of the mouse and rat, and their amplification in Cd-resistant cells."
Yamada K., Kato H., Kanda N., Fujii-Kuriyama Y., Utakoji T., Itoh R.
Biochim. Biophys. Acta 1219:581-591(1994) [PubMed: 7948015] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lung.
[4]"Splicing patterns of the Chinese hamster metallothionein II gene transcript."
Grady D.L., Hildebrand C.E., Jackson P.J., Walters R.A., Moyzis R.K.
Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

J00062 mRNA. Translation: AAA36997.1.
M81319 Genomic DNA. Translation: AAA73166.1.
D10552 Genomic DNA. Translation: BAA01409.1.
X55065 Genomic DNA. Translation: CAA38898.1.
PIRSMHY2C. A03276.

3D structure databases

HSSPHSSP built from PDB template 1MRT based on UniProtKB P04355.
SMRP67981. Positions 1-61.
ModBaseSearch...

Phylogenomic databases

HOVERGENP67981.

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]
ProDomP67981.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameMT2_CRIGR
AccessionPrimary (citable) accession number: P67981
Secondary accession number(s): P02799
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2008
This is version 22 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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

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