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P02798 (MT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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_0000197207

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

Experimental info

Sequence conflict521E → Q AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P02798 [UniParc].

Last modified August 1, 1991. Version 2.
Checksum: A20D1311166672EC

FASTA616,115
        10         20         30         40         50         60 
MDPNCSCASD GSCSCAGACK CKQCKCTSCK KSCCSCCPVG CAKCSQGCIC KEASDKCSCC 


A 

« Hide

References

« Hide 'large scale' references
[1]"Complete amino acid sequence of mouse liver metallothionein-II."
Huang I.-Y., Kimura M., Hata A., Tsunoo H., Yoshida A.
J. Biochem. 89:1839-1845(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Regulation, linkage, and sequence of mouse metallothionein I and II genes."
Searle P.F., Davison B.L., Stuart G.W., Wilkie T.M., Norstedt G., Palmiter R.D.
Mol. Cell. Biol. 4:1221-1230(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02236 Genomic DNA. Translation: AAA39528.1.
AK002567 mRNA. Translation: BAB22192.1.
BC031758 mRNA. Translation: AAH31758.1.
PIRSMMS2. A03275.
I57572.
RefSeqNP_032656.1. NM_008630.2.
UniGeneMm.147226.

3D structure databases

ProteinModelPortalP02798.
SMRP02798. Positions 1-61.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000034214.

PTM databases

PhosphoSiteP02798.

Proteomic databases

PaxDbP02798.
PRIDEP02798.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034214; ENSMUSP00000034214; ENSMUSG00000031762.
GeneID17750.
KEGGmmu:17750.
UCSCuc009mvv.1. mouse.

Organism-specific databases

CTD17750.
MGIMGI:97172. Mt2.

Phylogenomic databases

eggNOGNOG138665.
GeneTreeENSGT00730000110883.
HOGENOMHOG000236262.
InParanoidP02798.
KOK14739.
OMACKCASCK.
TreeFamTF336054.

Gene expression databases

BgeeP02798.
CleanExMM_MT2.
GenevestigatorP02798.

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

ChiTaRSMT2A. mouse.
NextBio292411.
PROP02798.
SOURCESearch...

Entry information

Entry nameMT2_MOUSE
AccessionPrimary (citable) accession number: P02798
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: April 16, 2014
This is version 110 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Metallothioneins

Classification of metallothioneins and list of entries