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Q9IAX2 (IOD2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Type II iodothyronine deiodinase

EC=1.97.1.10
Alternative name(s):
5DII
DIOII
Type 2 DI
Type-II 5'-deiodinase
Gene names
Name:DIO2
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for 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. Ref.1 UniProtKB Q92813

Catalytic activity

3,5,3'-triiodo-L-thyronine + iodide + A + H+ = L-thyroxine + AH2.

Enzyme regulation

Not inhibited by N(6)-propylthiouracil.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Highly expressed in liver and in various parts of the brain including telencephalon, hippocampus, cerebellum, and brain stem, and weakly expressed in thyroid, lung, and small intestine. Not detected in skeletal muscle, heart atria or ventricle, gizzard or kidney. Ref.1

Sequence similarities

Belongs to the iodothyronine deiodinase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.1 nM for thyroxine Ref.1

Vmax=0.34 pmol/min/mg enzyme

Ontologies

Keywords
   Biological processThyroid hormones biosynthesis
   Cellular componentMembrane
   Coding sequence diversitySelenocysteine
   DomainTransmembrane
Transmembrane helix
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhormone biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

thyroid hormone generation

Inferred from direct assay PubMed 12270789. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionthyroxine 5'-deiodinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 279279Type II iodothyronine deiodinase
PRO_0000154320

Regions

Transmembrane8 – 2821Helical; Potential

Sites

Active site1321

Amino acid modifications

Non-standard residue1321Selenocysteine
Non-standard residue2651Selenocysteine

Sequences

Sequence LengthMass (Da)Tools
Q9IAX2 [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: BC249728E2A8E9C1

FASTA27931,033
        10         20         30         40         50         60 
MGLLSADLLI TLQILPVFFS NCLFLALYDS VILLKHMVLF LSRSKSARGE WRRMLTSEGL 

        70         80         90        100        110        120 
RCVWNSFLLD AYKQVKLGGE APNSSVIHIA KGNDGSNSSW KSVGGKCGTK CHLLDFANSE 

       130        140        150        160        170        180 
RPLVVNFGSA TUPPFTSQLS AFSKLVEEFS GVADFLLVYI DEAHPSDGWA APGISPSSFE 

       190        200        210        220        230        240 
VKKHRNQEDR CAAAHQLLER FSLPPQCQVV ADCMDNNANV AYGVSFERVC IVQRQKIAYL 

       250        260        270 
GGKGPFFYNL QEVRLWLEQN FSKRUNPLST EDLSTDVSL 

« Hide

References

[1]"Cloning and expression of the chicken type 2 iodothyronine 5'-deiodinase."
Gereben B., Bartha T., Tu H.M., Harney J.W., Rudas P., Larsen P.R.
J. Biol. Chem. 274:13768-13776(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Embryo and Pituitary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF125575 mRNA. Translation: AAD33251.1.
UniGeneGga.1819.
Gga.51485.

3D structure databases

ProteinModelPortalQ9IAX2.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9IAX2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000099.
PhylomeDBQ9IAX2.

Family and domain databases

InterProIPR000643. Iodothyronine_deiodinase.
IPR008261. Iodothyronine_deiodinase_AS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR11781. PTHR11781. 1 hit.
PfamPF00837. T4_deiodinase. 1 hit.
[Graphical view]
PIRSFPIRSF001330. IOD. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS01205. T4_DEIODINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIOD2_CHICK
AccessionPrimary (citable) accession number: Q9IAX2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: February 26, 2008
Last modified: April 16, 2014
This is version 73 of the entry and version 3 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