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P28184 (MT3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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-3

Short name=MT-3
Alternative name(s):
Growth inhibitory factor
Short name=GIF
Metallothionein-III
Short name=MT-III
Gene names
Name:Mt3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length68 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro By similarity.

Tissue specificity

Brain.

Sequence similarities

Belongs to the metallothionein superfamily. Type 1 family.

Ontologies

Keywords
   LigandCopper
Metal-binding
Metal-thiolate cluster
Zinc
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

activation of protein kinase B activity

Inferred from sequence or structural similarity. Source: UniProtKB

astrocyte development

Inferred from direct assay PubMed 20544854. Source: UniProtKB

cadmium ion homeostasis

Inferred from mutant phenotype PubMed 20371971. Source: UniProtKB

cellular lipid catabolic process

Inferred from mutant phenotype PubMed 20544854. Source: UniProtKB

cellular metal ion homeostasis

Inferred from direct assay PubMed 12130647. Source: MGI

cellular response to cadmium ion

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to nitric oxide

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to oxidative stress

Inferred from direct assay PubMed 20544854. Source: UniProtKB

cellular zinc ion homeostasis

Inferred from direct assay PubMed 20544854PubMed 21359432. Source: UniProtKB

cholesterol catabolic process

Inferred from mutant phenotype PubMed 20544854. Source: UniProtKB

energy reserve metabolic process

Inferred from mutant phenotype PubMed 21726645. Source: UniProtKB

histone modification

Inferred from sequence or structural similarity. Source: UniProtKB

leptin-mediated signaling pathway

Inferred from mutant phenotype PubMed 21726645. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 19635467. Source: UniProtKB

negative regulation of autophagy

Inferred from mutant phenotype PubMed 20544854. Source: UniProtKB

negative regulation of axon extension

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of necrotic cell death

Inferred from mutant phenotype PubMed 20371971. Source: UniProtKB

negative regulation of neurogenesis

Inferred from direct assay PubMed 12130647. Source: MGI

negative regulation of neuron apoptotic process

Inferred from direct assay PubMed 21359432. Source: UniProtKB

negative regulation of oxidoreductase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20544854. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 21726645. Source: UniProtKB

positive regulation of catalytic activity

Inferred from mutant phenotype PubMed 20544854. Source: UniProtKB

positive regulation of cell death

Inferred from mutant phenotype PubMed 20544854. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype PubMed 20544854. Source: UniProtKB

positive regulation of lysosomal membrane permeability

Inferred from mutant phenotype PubMed 20544854. Source: UniProtKB

positive regulation of necrotic cell death

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of oxygen metabolic process

Inferred from mutant phenotype PubMed 21726645. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 21726645. Source: UniProtKB

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

protein import into nucleus, translocation

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

protein stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein glycosylation

Inferred from mutant phenotype PubMed 20544854. Source: UniProtKB

regulation of response to food

Inferred from mutant phenotype PubMed 21726645. Source: UniProtKB

removal of superoxide radicals

Inferred from sequence or structural similarity. Source: UniProtKB

response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

response to oxidative stress

Inferred from mutant phenotype PubMed 19635467. Source: UniProtKB

zinc ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion transport

Inferred from direct assay PubMed 21359432. Source: UniProtKB

   Cellular_componentinclusion body

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle

Inferred from direct assay PubMed 7931547. Source: UniProtKB

   Molecular_functioncadmium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from direct assay PubMed 12130647. Source: MGI

protein kinase activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from direct assay PubMed 7931547. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6868Metallothionein-3
PRO_0000197251

Regions

Region1 – 3030Beta
Region31 – 6838Alpha

Sites

Metal binding61Divalent metal cation; cluster B By similarity
Metal binding81Divalent metal cation; cluster B By similarity
Metal binding141Divalent metal cation; cluster B By similarity
Metal binding161Divalent metal cation; cluster B By similarity
Metal binding201Divalent metal cation; cluster B By similarity
Metal binding221Divalent metal cation; cluster B By similarity
Metal binding251Divalent metal cation; cluster B By similarity
Metal binding271Divalent metal cation; cluster B By similarity
Metal binding301Divalent metal cation; cluster B By similarity
Metal binding341Divalent metal cation; cluster A By similarity
Metal binding351Divalent metal cation; cluster A By similarity
Metal binding371Divalent metal cation; cluster A By similarity
Metal binding381Divalent metal cation; cluster A By similarity
Metal binding421Divalent metal cation; cluster A By similarity
Metal binding451Divalent metal cation; cluster A By similarity
Metal binding491Divalent metal cation; cluster A By similarity
Metal binding511Divalent metal cation; cluster A By similarity
Metal binding641Divalent metal cation; cluster A By similarity
Metal binding661Divalent metal cation; cluster A By similarity
Metal binding671Divalent metal cation; cluster A By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Secondary structure

..... 68
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28184 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 791AF60E38FED3CA

FASTA687,009
        10         20         30         40         50         60 
MDPETCPCPT GGSCTCSDKC KCKGCKCTNC KKSCCSCCPA GCEKCAKDCV CKGEEGAKAE 


AEKCSCCQ 

« Hide

References

« Hide 'large scale' references
[1]"MT-III, a brain-specific member of the metallothionein gene family."
Palmiter R.D., Findley S.D., Whitmore T.E., Durnam D.M.
Proc. Natl. Acad. Sci. U.S.A. 89:6333-6337(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain.
[2]"Structures of the human and mouse growth inhibitory factor-encoding genes."
Naruse S., Igarashi S., Furuya T., Kobayashi H., Miyatake T., Tsuji S.
Gene 144:283-287(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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].
Tissue: Brain.
[4]"Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: metallothionein-3."
Oz G., Zangger K., Armitage I.M.
Biochemistry 40:11433-11441(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 32-68.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93310 Genomic DNA. Translation: AAA39529.1.
S72046 Genomic DNA. Translation: AAB31397.1.
BC059725 mRNA. Translation: AAH59725.1.
PIRA46034.
RefSeqNP_038631.1. NM_013603.2.
UniGeneMm.2064.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JI9NMR-A32-68[»]
ProteinModelPortalP28184.
SMRP28184. Positions 32-68.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP28184.

Proteomic databases

PRIDEP28184.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034211; ENSMUSP00000034211; ENSMUSG00000031760.
GeneID17751.
KEGGmmu:17751.
UCSCuc009mvu.2. mouse.

Organism-specific databases

CTD4504.
MGIMGI:97173. Mt3.

Phylogenomic databases

HOGENOMHOG000236262.
HOVERGENHBG094960.
InParanoidP28184.
KOK14740.
OMAVCKGGEG.

Gene expression databases

BgeeP28184.
CleanExMM_MT3.
GenevestigatorP28184.

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

EvolutionaryTraceP28184.
NextBio292415.
PROP28184.
SOURCESearch...

Entry information

Entry nameMT3_MOUSE
AccessionPrimary (citable) accession number: P28184
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 119 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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

Metallothioneins

Classification of metallothioneins and list of entries