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Protein

Metallothionein-2

Gene

Mt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi5 – 51Divalent metal cation; cluster B
Metal bindingi7 – 71Divalent metal cation; cluster B
Metal bindingi13 – 131Divalent metal cation; cluster B
Metal bindingi15 – 151Divalent metal cation; cluster B
Metal bindingi19 – 191Divalent metal cation; cluster B
Metal bindingi21 – 211Divalent metal cation; cluster B
Metal bindingi24 – 241Divalent metal cation; cluster B
Metal bindingi26 – 261Divalent metal cation; cluster B
Metal bindingi29 – 291Divalent metal cation; cluster B
Metal bindingi33 – 331Divalent metal cation; cluster A
Metal bindingi34 – 341Divalent metal cation; cluster A
Metal bindingi36 – 361Divalent metal cation; cluster A
Metal bindingi37 – 371Divalent metal cation; cluster A
Metal bindingi41 – 411Divalent metal cation; cluster A
Metal bindingi44 – 441Divalent metal cation; cluster A
Metal bindingi48 – 481Divalent metal cation; cluster A
Metal bindingi50 – 501Divalent metal cation; cluster A
Metal bindingi57 – 571Divalent metal cation; cluster A
Metal bindingi59 – 591Divalent metal cation; cluster A
Metal bindingi60 – 601Divalent metal cation; cluster A

GO - Molecular functioni

  1. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to cadmium ion Source: Ensembl
  2. cellular response to erythropoietin Source: Ensembl
  3. cellular response to zinc ion Source: UniProtKB
  4. cellular zinc ion homeostasis Source: MGI
  5. detoxification of copper ion Source: MGI
  6. negative regulation of growth Source: UniProtKB
  7. nitric oxide mediated signal transduction Source: MGI
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Metal-thiolate cluster

Enzyme and pathway databases

ReactomeiREACT_349056. Interferon gamma signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Metallothionein-2
Short name:
MT-2
Alternative name(s):
Metallothionein-II
Short name:
MT-II
Gene namesi
Name:Mt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:97172. Mt2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6161Metallothionein-2PRO_0000197207Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei58 – 581PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP02798.
PaxDbiP02798.
PRIDEiP02798.

PTM databases

PhosphoSiteiP02798.

Expressioni

Gene expression databases

BgeeiP02798.
CleanExiMM_MT2.
GenevestigatoriP02798.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034214.

Structurei

3D structure databases

ProteinModelPortaliP02798.
SMRiP02798. Positions 1-61.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2929BetaAdd
BLAST
Regioni30 – 6132AlphaAdd
BLAST

Domaini

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 similaritiesi

Phylogenomic databases

eggNOGiNOG138665.
GeneTreeiENSGT00730000110883.
HOGENOMiHOG000236262.
InParanoidiP02798.
KOiK14739.
OMAiCKKSCCT.
TreeFamiTF336054.

Family and domain databases

Gene3Di4.10.10.10. 1 hit.
InterProiIPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR003019. Metalthion_sfam_euk.
IPR000006. Metalthion_vert.
IPR018064. Metalthion_vert_metal_BS.
[Graphical view]
PANTHERiPTHR23299. PTHR23299. 1 hit.
PfamiPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSiPR00860. MTVERTEBRATE.
SUPFAMiSSF57868. SSF57868. 1 hit.
PROSITEiPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPNCSCASD GSCSCAGACK CKQCKCTSCK KSCCSCCPVG CAKCSQGCIC
60
KEASDKCSCC A
Length:61
Mass (Da):6,115
Last modified:August 1, 1991 - v2
Checksum:iA20D1311166672EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521E → Q AA sequence (PubMed:7287658).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02236 Genomic DNA. Translation: AAA39528.1.
AK002567 mRNA. Translation: BAB22192.1.
BC031758 mRNA. Translation: AAH31758.1.
CCDSiCCDS40437.1.
PIRiA03275. SMMS2.
I57572.
RefSeqiNP_032656.1. NM_008630.2.
UniGeneiMm.147226.

Genome annotation databases

EnsembliENSMUST00000034214; ENSMUSP00000034214; ENSMUSG00000031762.
GeneIDi17750.
KEGGimmu:17750.
UCSCiuc009mvv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02236 Genomic DNA. Translation: AAA39528.1.
AK002567 mRNA. Translation: BAB22192.1.
BC031758 mRNA. Translation: AAH31758.1.
CCDSiCCDS40437.1.
PIRiA03275. SMMS2.
I57572.
RefSeqiNP_032656.1. NM_008630.2.
UniGeneiMm.147226.

3D structure databases

ProteinModelPortaliP02798.
SMRiP02798. Positions 1-61.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034214.

PTM databases

PhosphoSiteiP02798.

Proteomic databases

MaxQBiP02798.
PaxDbiP02798.
PRIDEiP02798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034214; ENSMUSP00000034214; ENSMUSG00000031762.
GeneIDi17750.
KEGGimmu:17750.
UCSCiuc009mvv.1. mouse.

Organism-specific databases

CTDi17750.
MGIiMGI:97172. Mt2.

Phylogenomic databases

eggNOGiNOG138665.
GeneTreeiENSGT00730000110883.
HOGENOMiHOG000236262.
InParanoidiP02798.
KOiK14739.
OMAiCKKSCCT.
TreeFamiTF336054.

Enzyme and pathway databases

ReactomeiREACT_349056. Interferon gamma signaling.

Miscellaneous databases

NextBioi292411.
PROiP02798.
SOURCEiSearch...

Gene expression databases

BgeeiP02798.
CleanExiMM_MT2.
GenevestigatoriP02798.

Family and domain databases

Gene3Di4.10.10.10. 1 hit.
InterProiIPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR003019. Metalthion_sfam_euk.
IPR000006. Metalthion_vert.
IPR018064. Metalthion_vert_metal_BS.
[Graphical view]
PANTHERiPTHR23299. PTHR23299. 1 hit.
PfamiPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSiPR00860. MTVERTEBRATE.
SUPFAMiSSF57868. SSF57868. 1 hit.
PROSITEiPS00203. METALLOTHIONEIN_VRT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, ACETYLATION AT MET-1.
  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.
    , 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.

Entry informationi

Entry nameiMT2_MOUSE
AccessioniPrimary (citable) accession number: P02798
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: April 1, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Metallothioneins
    Classification of metallothioneins and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.