Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P18055 (MT2A_RABIT)

Last modified November 24, 2009. Version 71. 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-2A
      Short name=MT-2A
Alternative name(s):
    Metallothionein-IIA
      Short name=MT-IIA
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length62 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.

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 binding51Cluster B
Metal binding71Cluster B
Metal binding141Cluster B
Metal binding161Cluster B
Metal binding201Cluster B
Metal binding221Cluster B
Metal binding251Cluster B
Metal binding271Cluster B
Metal binding301Cluster B
Metal binding341Cluster A
Metal binding351Cluster A
Metal binding371Cluster A
Metal binding381Cluster A
Metal binding421Cluster A
Metal binding451Cluster A
Metal binding491Cluster A
Metal binding511Cluster A
Metal binding581Cluster A
Metal binding601Cluster A
Metal binding611Cluster A

Amino acid modifications

Modified residue11N-acetylmethionine

Secondary structure

....... 62
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18055-1 [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: 1779803] [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: 7864820] [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: 3709538] [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: 3959079] [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: 3418714] [Abstract]
Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

PIRA37425.
S54336.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1MRBNMR-A32-62[»]
2MRBNMR-A1-31[»]
ModBaseSearch...

Phylogenomic databases

HOVERGENP18055.

Family and domain databases

InterProIPR017854. Metallothionein_sfam.
IPR003019. Metallothionein_sfam_euk.
IPR000006. Metallothionein_vert.
IPR018064. Metallothionein_vert_metal_BS.
[Graphical view]
Gene3DG3DSA:4.10.10.10. Metallothionein_vert. 1 hit.
PANTHERPTHR23299. Metallothionein_vert. 1 hit.
PfamPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSPR00860. MTVERTEBRATE.
PROSITEPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]
ProtoNetSearch...

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: November 24, 2009
This is version 71 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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