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P04355 (MT2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metallothionein-2

Short name=MT-2
Alternative name(s):
Metallothionein-II
Short name=MT-II
Gene names
Name:Mt2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length61 AA.
Sequence statusComplete.
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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6161Metallothionein-2
PRO_0000197222

Regions

Region1 – 2929Beta
Region30 – 6132Alpha

Sites

Metal binding51Divalent metal cation; cluster B
Metal binding71Divalent metal cation; cluster B
Metal binding131Divalent metal cation; cluster B
Metal binding151Divalent metal cation; cluster B
Metal binding191Divalent metal cation; cluster B
Metal binding211Divalent metal cation; cluster B
Metal binding241Divalent metal cation; cluster B
Metal binding261Divalent metal cation; cluster B
Metal binding291Divalent metal cation; cluster B
Metal binding331Divalent metal cation; cluster A
Metal binding341Divalent metal cation; cluster A
Metal binding361Divalent metal cation; cluster A
Metal binding371Divalent metal cation; cluster A
Metal binding411Divalent metal cation; cluster A
Metal binding441Divalent metal cation; cluster A
Metal binding481Divalent metal cation; cluster A
Metal binding501Divalent metal cation; cluster A
Metal binding571Divalent metal cation; cluster A
Metal binding591Divalent metal cation; cluster A
Metal binding601Divalent metal cation; cluster A

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1

Secondary structure

.......... 61
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04355 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: D50D1306A5ED08E9

FASTA616,145
        10         20         30         40         50         60 
MDPNCSCATD GSCSCAGSCK CKQCKCTSCK KSCCSCCPVG CAKCSQGCIC KEASDKCSCC 


A 

« Hide

References

[1]"Structural characterization of the isoforms of neonatal and adult rat liver metallothionein."
Winge D.R., Nielson K.B., Zeikus R.D., Gray W.R.
J. Biol. Chem. 259:11419-11425(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, ACETYLATION AT MET-1.
Tissue: Liver.
[2]"Rat metallothionein multigene family."
Andersen R.D., Taplitz S.J., Birren B.W., Bristol G., Herschman H.R.
Experientia Suppl. 52:373-384(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Single crystals of cadmium, zinc metallothionein."
Melis K.A., Carter D.C., Stout C.D., Winge D.R.
J. Biol. Chem. 258:6255-6257(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[4]"Crystal structure of Cd,Zn metallothionein."
Furey W.F. Jr., Robbins A.H., Clancy L.L., Winge D.R., Wand B.C., Stout C.D.
Science 231:704-710(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[5]"Refined crystal structure of Cd, Zn metallothionein at 2.0-A resolution."
Robbins A.H., McRee D.E., Williamson M., Collett S.A., Xuong N.H., Furey W.F. Jr., Wang B.C., Stout C.D.
J. Mol. Biol. 221:1269-1293(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[6]"Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy."
Schultze P., Woergotter E., Braun W., Wagner G., Vasak M., Kaegi J.H.R., Wuethrich K.
J. Mol. Biol. 203:251-268(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[7]"Sequence-specific 1H-NMR assignments in rat-liver metallothionein-2."
Woergoetter E., Wagner G., Vasak M., Kaegi J.H.R., Wuethrich K.
Eur. J. Biochem. 167:457-466(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11794 Genomic DNA. Translation: AAA41640.1.
PIRSMRT2. B61561.
RefSeqNP_001131036.1. NM_001137564.1.
UniGeneRn.115549.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MRTNMR-A31-61[»]
2MRTNMR-A1-30[»]
4MT2X-ray2.00A1-61[»]
ProteinModelPortalP04355.
SMRP04355. Positions 1-61.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP04355. 1 interaction.

Proteomic databases

PaxDbP04355.
PRIDEP04355.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000067391; ENSRNOP00000062585; ENSRNOG00000043098.
GeneID689415.
KEGGrno:689415.
UCSCRGD:1592345. rat.

Organism-specific databases

CTD4502.

Phylogenomic databases

eggNOGNOG138665.
GeneTreeENSGT00730000110883.
HOGENOMHOG000236262.
HOVERGENHBG096105.
InParanoidP04355.
KOK14739.
OMANCAGSCK.
OrthoDBEOG79CZ35.
PhylomeDBP04355.
TreeFamTF336054.

Gene expression databases

GenevestigatorP04355.

Family and domain databases

Gene3D4.10.10.10. 1 hit.
InterProIPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR003019. Metalthion_sfam_euk.
IPR000006. Metalthion_vert.
IPR018064. Metalthion_vert_metal_BS.
[Graphical view]
PANTHERPTHR23299. PTHR23299. 1 hit.
PfamPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSPR00860. MTVERTEBRATE.
SUPFAMSSF57868. SSF57868. 1 hit.
PROSITEPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04355.
NextBio738628.

Entry information

Entry nameMT2_RAT
AccessionPrimary (citable) accession number: P04355
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: June 11, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Metallothioneins

Classification of metallothioneins and list of entries