P70551 · IOD2_RAT

  • Protein
    Type II iodothyronine deiodinase
  • Gene
    Dio2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Catalyzes the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for providing the brain with appropriate levels of T3 during the critical period of development.

Catalytic activity

Features

Showing features for active site.

126620406080100120140160180200220240260
TypeIDPosition(s)Description
Active site130

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmembrane
Molecular Functionthyroxine 5'-deiodinase activity
Molecular Functionthyroxine 5-deiodinase activity
Molecular Functionubiquitin protein ligase binding
Biological Processbrown fat cell differentiation
Biological Processcellular lipid metabolic process
Biological Processhormone biosynthetic process
Biological Processpositive regulation of cold-induced thermogenesis
Biological Processresponse to lipopolysaccharide
Biological Processthyroid hormone catabolic process
Biological Processthyroid hormone generation
Biological Processthyroid hormone metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Type II iodothyronine deiodinase
  • EC number
  • Alternative names
    • 5DII
    • DIOII
    • Type 2 DI
    • Type-II 5'-deiodinase

Gene names

    • Name
      Dio2
    • Synonyms
      Itdi2, Txdi2

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P70551
  • Secondary accessions
    • O70179

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane10-34Helical

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001543191-266Type II iodothyronine deiodinase

Post-translational modification

Ubiquitinated by MARCHF6, leading to its degradation by the proteasome. Deubiquitinated by USP20 and USP33 (By similarity).

Keywords

Expression

Tissue specificity

Expressed in cerebral cortex, cerebellum, pituitary gland, mostly in anterior pituitary gland, and pineal gland, as well as in brown adipose tissue (BAT).

Induction

In the pineal gland, exhibits night/day variations with a 9-fold increased expression at night. Up-regulation is due to a large degree to the release of norepinephrine from nerve terminals in the pineal gland and cAMP signaling pathway. In BAT, up-regulated in animals exposed to cold.

Interaction

Subunit

Interacts with USP20 and USP33. Interacts with MARCHF6 (By similarity).

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the iodothyronine deiodinase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    266
  • Mass (Da)
    29,871
  • Last updated
    2008-02-26 v4
  • Checksum
    06DE3292FB467578
MGLLSVDLLITLQILPVFFSNCLFLALYDSVILLKHVALLLSRSKSTRGEWRRMLTSEGLRCVWNSFLLDAYKQVKLGEDAPNSSVVHVSNPEAGNNCASEKTADGAECHLLDFASAERPLVVNFGSATUPPFTRQLPAFRQLVEEFSSVADFLLVYIDEAHPSDGWAVPGDSSMSFEVKKHRNQEDRCAAAHQLLERFSLPPQCQVVADRMDNNANVAYGVAFERVCIVQRRKIAYLGGKGPFSYNLQEVRSWLEKNFSKRUILD

Features

Showing features for sequence conflict, non-standard residue.

TypeIDPosition(s)Description
Sequence conflict116in Ref. 2; BAA25186
Non-standard residue130Selenocysteine
Non-standard residue263Selenocysteine

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U53505
EMBL· GenBank· DDBJ
AAC52767.1
EMBL· GenBank· DDBJ
mRNA
AB011068
EMBL· GenBank· DDBJ
BAA25186.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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