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P18055 (MT2A_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Metallothionein-2A
Short name=MT-2A
Alternative name(s):
Metallothionein-IIA
Short name=MT-IIA
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length62 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.

Subunit structure

Monomer.

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 – 6262Metallothionein-2A
PRO_0000197216

Regions

Region1 – 3030Beta
Region31 – 6232Alpha

Sites

Metal binding51Divalent metal cation; cluster B
Metal binding71Divalent metal cation; cluster B
Metal binding141Divalent metal cation; cluster B
Metal binding161Divalent metal cation; cluster B
Metal binding201Divalent metal cation; cluster B
Metal binding221Divalent metal cation; cluster B
Metal binding251Divalent metal cation; cluster B
Metal binding271Divalent metal cation; cluster B
Metal binding301Divalent metal cation; cluster B
Metal binding341Divalent metal cation; cluster A
Metal binding351Divalent metal cation; cluster A
Metal binding371Divalent metal cation; cluster A
Metal binding381Divalent metal cation; cluster A
Metal binding421Divalent metal cation; cluster A
Metal binding451Divalent metal cation; cluster A
Metal binding491Divalent metal cation; cluster A
Metal binding511Divalent metal cation; cluster A
Metal binding581Divalent metal cation; cluster A
Metal binding601Divalent metal cation; cluster A
Metal binding611Divalent metal cation; cluster A

Amino acid modifications

Modified residue11N-acetylmethionine

Secondary structure

1 ....... 62
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18055 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: C3FEA7B701081B3E

FASTA626,083
        10         20         30         40         50         60 
MDPNCSCAAA GDSCTCANSC TCKACKCTSC KKSCCSCCPP GCAKCAQGCI CKGASDKCSC 


CA

« Hide

References

[1]"Amino acid sequence determination."
Hunziker P.E.
Methods Enzymol. 205:421-426(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: New Zealand white.
Tissue: Kidney and Liver.
[2]"Primary structures of seven metallothioneins from rabbit tissue."
Hunziker P.E., Kaur P., Wan M., Kaenzig A.
Biochem. J. 306:265-270(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: New Zealand white.
Tissue: Kidney and Liver.
[3]"Sequence-specific 1H-NMR assignments in rabbit-liver metallothionein-2."
Wagner G., Neuhaus D., Worgotter E., Vasak M., Kaegi J.H.R., Wuethrich K.
Eur. J. Biochem. 157:275-289(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, PROTEIN SEQUENCE.
[4]"Nuclear magnetic resonance identification of 'half-turn' and 3(10)-helix secondary structure in rabbit liver metallothionein-2."
Wagner G., Neuhaus D., Worgotter E., Vasak M., Kaegi J.H.R., Wuethrich K.
J. Mol. Biol. 187:131-135(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[5]"Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance."
Arseniev A., Schultze P., Worgotter E., Braun W., Wagner G., Vasak M., Kaegi J.H.R., Wuethrich K.
J. Mol. Biol. 201:637-657(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

PIRA37425.
S54336.
RefSeqXP_002711575.1. XM_002711529.1.
UniGeneOcu.3423.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MRBNMR-A32-62[»]
2MRBNMR-A1-31[»]
ProteinModelPortalP18055.
SMRP18055. Positions 1-62.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000018875.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000023383; ENSOCUP00000018875; ENSOCUG00000021126.
GeneID100343299.

Phylogenomic databases

eggNOGNOG138665.
GeneTreeENSGT00390000010461.
HOGENOMHOG000236262.
OMASCACKNC.
OrthoDBEOG48KRD3.

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. Metallothionein_sfam. 1 hit.
PROSITEPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP18055.

Entry information

Entry nameMT2A_RABIT
AccessionPrimary (citable) accession number: P18055
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents