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Protein

Metallothionein-1

Gene

Mt1

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

  • copper ion binding Source: MGI
  • metal ion binding Source: MGI
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cellular metal ion homeostasis Source: MGI
  • cellular response to chromate Source: MGI
  • cellular response to zinc ion Source: MGI
  • cellular zinc ion homeostasis Source: MGI
  • detoxification of copper ion Source: MGI
  • negative regulation of growth Source: UniProtKB
  • negative regulation of neuron apoptotic process Source: UniProtKB
  • nitric oxide mediated signal transduction Source: MGI
  • response to metal ion Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Metal-thiolate cluster

Enzyme and pathway databases

ReactomeiR-MMU-5661231. Metallothioneins bind metals.

Names & Taxonomyi

Protein namesi
Recommended name:
Metallothionein-1
Short name:
MT-1
Alternative name(s):
Metallothionein-I
Short name:
MT-I
Gene namesi
Name:Mt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:97171. Mt1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • lysosome Source: MGI
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6161Metallothionein-1PRO_0000197206Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP02802.
MaxQBiP02802.
PaxDbiP02802.
PeptideAtlasiP02802.
PRIDEiP02802.
TopDownProteomicsiP02802.

PTM databases

iPTMnetiP02802.
PhosphoSiteiP02802.

Expressioni

Gene expression databases

BgeeiP02802.
CleanExiMM_MT1.
GenevisibleiP02802. MM.

Interactioni

Protein-protein interaction databases

BioGridi201578. 1 interaction.
STRINGi10090.ENSMUSP00000034215.

Structurei

Secondary structure

1
61
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Beta strandi20 – 234Combined sources
Beta strandi25 – 284Combined sources
Beta strandi35 – 373Combined sources
Beta strandi42 – 476Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DFSNMR-A31-61[»]
1DFTNMR-A1-30[»]
ProteinModelPortaliP02802.
SMRiP02802. Positions 1-61.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02802.

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

eggNOGiENOG410JFS1. Eukaryota.
ENOG41113QR. LUCA.
GeneTreeiENSGT00840000131018.
HOGENOMiHOG000236262.
HOVERGENiHBG009063.
InParanoidiP02802.
KOiK14739.
OMAiSCACKNC.
TreeFamiTF336054.

Family and domain databases

Gene3Di4.10.10.10. 1 hit.
InterProiIPR003019. Metalthion.
IPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
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.

P02802-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPNCSCSTG GSCTCTSSCA CKNCKCTSCK KSCCSCCPVG CSKCAQGCVC
60
KGAADKCTCC A
Length:61
Mass (Da):6,018
Last modified:July 21, 1986 - v1
Checksum:i4B3754EC759C0ADB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231N → D AA sequence (PubMed:914867).Curated
Sequence conflicti32 – 321S → G (PubMed:6277322).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S62785 mRNA. Translation: AAB26768.1.
J00605 Genomic DNA. Translation: AAA39527.2.
AK018727 mRNA. Translation: BAC25563.1.
BC036990 mRNA. Translation: AAH36990.1.
CCDSiCCDS40438.1.
PIRiA93261. SMMSI.
RefSeqiNP_038630.1. NM_013602.3.
UniGeneiMm.192991.
Mm.388249.

Genome annotation databases

EnsembliENSMUST00000034215; ENSMUSP00000034215; ENSMUSG00000031765.
GeneIDi17748.
KEGGimmu:17748.
UCSCiuc009mvw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S62785 mRNA. Translation: AAB26768.1.
J00605 Genomic DNA. Translation: AAA39527.2.
AK018727 mRNA. Translation: BAC25563.1.
BC036990 mRNA. Translation: AAH36990.1.
CCDSiCCDS40438.1.
PIRiA93261. SMMSI.
RefSeqiNP_038630.1. NM_013602.3.
UniGeneiMm.192991.
Mm.388249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DFSNMR-A31-61[»]
1DFTNMR-A1-30[»]
ProteinModelPortaliP02802.
SMRiP02802. Positions 1-61.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201578. 1 interaction.
STRINGi10090.ENSMUSP00000034215.

PTM databases

iPTMnetiP02802.
PhosphoSiteiP02802.

Proteomic databases

EPDiP02802.
MaxQBiP02802.
PaxDbiP02802.
PeptideAtlasiP02802.
PRIDEiP02802.
TopDownProteomicsiP02802.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034215; ENSMUSP00000034215; ENSMUSG00000031765.
GeneIDi17748.
KEGGimmu:17748.
UCSCiuc009mvw.2. mouse.

Organism-specific databases

CTDi17748.
MGIiMGI:97171. Mt1.

Phylogenomic databases

eggNOGiENOG410JFS1. Eukaryota.
ENOG41113QR. LUCA.
GeneTreeiENSGT00840000131018.
HOGENOMiHOG000236262.
HOVERGENiHBG009063.
InParanoidiP02802.
KOiK14739.
OMAiSCACKNC.
TreeFamiTF336054.

Enzyme and pathway databases

ReactomeiR-MMU-5661231. Metallothioneins bind metals.

Miscellaneous databases

EvolutionaryTraceiP02802.
PROiP02802.
SOURCEiSearch...

Gene expression databases

BgeeiP02802.
CleanExiMM_MT1.
GenevisibleiP02802. MM.

Family and domain databases

Gene3Di4.10.10.10. 1 hit.
InterProiIPR003019. Metalthion.
IPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
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. "Mouse liver metallothioneins. Complete amino acid sequence of metallothionein-I."
    Huang I.-Y., Yoshida A., Tsunoo H., Nakajima H.
    J. Biol. Chem. 252:8217-8221(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ACETYLATION AT MET-1.
    Tissue: Liver.
  2. "Structure of mouse metallothionein-I gene and its mRNA."
    Glanville N., Durnam D.M., Palmiter R.D.
    Nature 292:267-269(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Isolation and characterization of the mouse metallothionein-I gene."
    Durnam D.M., Perrin F., Gannon F., Palmiter R.D.
    Proc. Natl. Acad. Sci. U.S.A. 77:6511-6515(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  4. "Cloning and sequencing of cDNA for mouse liver metallothionein-I."
    Mbikay M., Maiti I.B., Thirion J.-P.
    Biochem. Biophys. Res. Commun. 103:825-832(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Production of a bifunctional hybrid molecule B72.3/metallothionein-1 by protein engineering."
    Xiang J., Koropatnick J., Qi Y., Luo X., Moyana T., Li K., Chen Y.
    Immunology 78:574-581(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  6. "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.
  7. "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: FVB/N.
    Tissue: Colon.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.
  9. "Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy."
    Zangger K., Oez G., Otvos J.D., Armitage I.M.
    Protein Sci. 8:2630-2638(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiMT1_MOUSE
AccessioniPrimary (citable) accession number: P02802
Secondary accession number(s): Q64485
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.