Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P37359 (MT3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

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

General annotation (Comments)

Function

Binds heavy metals. Contains five zinc and one copper atoms per polypeptide chain and only a negligible amount of cadmium.

Tissue specificity

Brain.

Sequence similarities

Belongs to the metallothionein superfamily. Type 1 family.

Ontologies

Keywords
   LigandCopper
Metal-binding
Metal-thiolate cluster
Zinc
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
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 sequence or structural similarity. Source: UniProtKB

cadmium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular lipid catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

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 sequence or structural similarity. Source: UniProtKB

cellular zinc ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cholesterol catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

energy reserve metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

histone modification

Inferred from sequence or structural similarity. Source: UniProtKB

leptin-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of autophagy

Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell death

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of lysosomal membrane permeability

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of necrotic cell death

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of oxygen metabolic process

Inferred from sequence or structural similarity. 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 sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

regulation of response to food

Inferred from sequence or structural similarity. 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

zinc ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion transport

Inferred from sequence or structural similarity. 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 sequence or structural similarity. 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

protein kinase activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6868Metallothionein-3
PRO_0000197248

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 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

Experimental info

Sequence conflict301S → C AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37359 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: 1DD24B83AA52AE71

FASTA686,937
        10         20         30         40         50         60 
MDPETCPCPT GGSCTCSDPC KCEGCTCASS KKSCCSCCPA ECEKCAKDCV CKGGEGAEAE 


EKKCSCCQ 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, primary structures and metal binding properties of neuronal growth inhibitory factor (GIF) from bovine and equine brain."
Pountney D.L., Fundel S.M., Faller P., Birchler N.E., Hunziker P., Vasak M.
FEBS Lett. 345:193-197(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Brain.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal pons.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC126773 mRNA. Translation: AAI26774.1.
PIRS44391.
RefSeqNP_001106775.1. NM_001113304.2.
UniGeneBt.16213.

3D structure databases

ProteinModelPortalP37359.
SMRP37359. Positions 32-68.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000022460; ENSBTAP00000022460; ENSBTAG00000016886.
GeneID613320.
KEGGbta:613320.

Organism-specific databases

CTD4504.

Phylogenomic databases

GeneTreeENSGT00730000111484.
HOGENOMHOG000236262.
HOVERGENHBG095156.
InParanoidP37359.
KOK14740.
OMAVCKGGEG.

Family and domain databases

Gene3D4.10.10.10. 1 hit.
InterProIPR017854. Metalthion_dom.
IPR023587. Metalthion_dom_vert.
IPR003019. Metalthion_sfam_euk.
IPR000006. Metalthion_vert.
[Graphical view]
PANTHERPTHR23299. PTHR23299. 1 hit.
PfamPF00131. Metallothio. 1 hit.
[Graphical view]
PRINTSPR00860. MTVERTEBRATE.
SUPFAMSSF57868. SSF57868. 1 hit.
ProtoNetSearch...

Other

NextBio20898520.

Entry information

Entry nameMT3_BOVIN
AccessionPrimary (citable) accession number: P37359
Secondary accession number(s): A0JNL9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 17, 2007
Last modified: April 16, 2014
This is version 98 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

Metallothioneins

Classification of metallothioneins and list of entries