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Protein

Thyroxine 5-deiodinase

Gene

Dio3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. May play a role in preventing premature exposure of developing fetal tissues to adult levels of thyroid hormones. Can regulate circulating fetal thyroid hormone concentrations throughout gestation. Essential role for regulation of thyroid hormone inactivation during embryological development.By similarity

Catalytic activityi

3,3',5'-triiodo-L-thyronine + iodide + acceptor + H+ = L-thyroxine + reduced acceptor.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei170 – 1701

GO - Molecular functioni

  • thyroxine 5'-deiodinase activity Source: MGI
  • thyroxine 5-deiodinase activity Source: UniProtKB

GO - Biological processi

  • hormone biosynthetic process Source: UniProtKB-KW
  • positive regulation of multicellular organism growth Source: MGI
  • thyroid hormone catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Thyroid hormones biosynthesis

Enzyme and pathway databases

BRENDAi1.97.1.11. 3474.
ReactomeiR-MMU-350864. Regulation of thyroid hormone activity.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroxine 5-deiodinase (EC:1.21.99.3)
Alternative name(s):
5DIII
DIOIII
Type 3 DI
Type III iodothyronine deiodinase
Gene namesi
Name:Dio3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1306782. Dio3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4444CytoplasmicSequence analysisAdd
BLAST
Transmembranei45 – 6723Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini68 – 304237ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Thyroxine 5-deiodinasePRO_0000154324Add
BLAST

Proteomic databases

PaxDbiQ91ZI8.
PRIDEiQ91ZI8.

Expressioni

Gene expression databases

BgeeiQ91ZI8.
CleanExiMM_DIO3.
ExpressionAtlasiQ91ZI8. baseline and differential.

Interactioni

Subunit structurei

Homodimer. May undergo minor heretodimerization with DIO1 and DIO2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000133920.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi120 – 1223Combined sources
Beta strandi139 – 1413Combined sources
Turni143 – 1453Combined sources
Beta strandi148 – 1503Combined sources
Helixi151 – 1544Combined sources
Beta strandi161 – 1666Combined sources
Helixi171 – 1755Combined sources
Helixi177 – 18711Combined sources
Turni188 – 1903Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi206 – 2083Combined sources
Helixi222 – 23413Combined sources
Beta strandi241 – 2444Combined sources
Helixi249 – 2535Combined sources
Beta strandi260 – 2656Combined sources
Beta strandi268 – 2725Combined sources
Helixi280 – 29718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TR3X-ray1.90A120-304[»]
4TR4X-ray1.93A120-304[»]
ProteinModelPortaliQ91ZI8.
SMRiQ91ZI8. Positions 120-301.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the iodothyronine deiodinase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IZDN. Eukaryota.
ENOG4112999. LUCA.
GeneTreeiENSGT00820000127068.
HOGENOMiHOG000007088.
HOVERGENiHBG000099.
InParanoidiQ91ZI8.
KOiK07754.
OMAiDFLCIRR.
OrthoDBiEOG79PJQC.
TreeFamiTF329721.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000643. Iodothyronine_deiodinase.
IPR008261. Iodothyronine_deiodinase_AS.
IPR027252. Iodothyronine_deiodinase_I/III.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11781. PTHR11781. 1 hit.
PfamiPF00837. T4_deiodinase. 1 hit.
[Graphical view]
PIRSFiPIRSF001330. IOD. 1 hit.
PIRSF500144. IODI_III. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS01205. T4_DEIODINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91ZI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRQAASRLV VGEGEGPPGA SGPAATMLRS LLLHSLRLCA QTASCLVLFP
60 70 80 90 100
RFLGTAFMLW LLDFLCIRKH FLRRRHPDHP EPEVELNSEG EEMPPDDPPI
110 120 130 140 150
CVSDDNRLCT LASLKAVWHG QKLDFFKQAH EGGPAPNSEV VRPDGFQSQR
160 170 180 190 200
ILDYAQGTRP LVLNFGSCTU PPFMARMSAF QRLVTKYQRD VDFLIIYIEE
210 220 230 240 250
AHPSDGWVTT DSPYVIPQHR SLEDRVSAAR VLQQGAPGCA LVLDTMANSS
260 270 280 290 300
SSAYGAYFER LYVIQSGTIM YQGGRGPDGY QVSELRTWLE RYDEQLHGTR

PHRF
Length:304
Mass (Da):34,111
Last modified:May 14, 2014 - v4
Checksum:i877DD709B4104A15
GO

Sequence cautioni

The sequence AAI06848.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAI06849.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL23960.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE24483.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAE26869.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei170 – 1701Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF426023 Genomic DNA. Translation: AAL23960.1. Different initiation.
AK140797 mRNA. Translation: BAE24483.1. Different initiation.
AK146060 mRNA. Translation: BAE26869.1. Different initiation.
AL591207 Genomic DNA. No translation available.
BC106847 mRNA. Translation: AAI06848.1. Different initiation.
BC106848 mRNA. Translation: AAI06849.1. Different initiation.
CCDSiCCDS26171.2.
RefSeqiNP_742117.2. NM_172119.2.
UniGeneiMm.154427.

Genome annotation databases

EnsembliENSMUST00000173014; ENSMUSP00000133920; ENSMUSG00000075707.
GeneIDi107585.
KEGGimmu:107585.
UCSCiuc007pbi.1. mouse.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF426023 Genomic DNA. Translation: AAL23960.1. Different initiation.
AK140797 mRNA. Translation: BAE24483.1. Different initiation.
AK146060 mRNA. Translation: BAE26869.1. Different initiation.
AL591207 Genomic DNA. No translation available.
BC106847 mRNA. Translation: AAI06848.1. Different initiation.
BC106848 mRNA. Translation: AAI06849.1. Different initiation.
CCDSiCCDS26171.2.
RefSeqiNP_742117.2. NM_172119.2.
UniGeneiMm.154427.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TR3X-ray1.90A120-304[»]
4TR4X-ray1.93A120-304[»]
ProteinModelPortaliQ91ZI8.
SMRiQ91ZI8. Positions 120-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000133920.

Proteomic databases

PaxDbiQ91ZI8.
PRIDEiQ91ZI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000173014; ENSMUSP00000133920; ENSMUSG00000075707.
GeneIDi107585.
KEGGimmu:107585.
UCSCiuc007pbi.1. mouse.

Organism-specific databases

CTDi1735.
MGIiMGI:1306782. Dio3.

Phylogenomic databases

eggNOGiENOG410IZDN. Eukaryota.
ENOG4112999. LUCA.
GeneTreeiENSGT00820000127068.
HOGENOMiHOG000007088.
HOVERGENiHBG000099.
InParanoidiQ91ZI8.
KOiK07754.
OMAiDFLCIRR.
OrthoDBiEOG79PJQC.
TreeFamiTF329721.

Enzyme and pathway databases

BRENDAi1.97.1.11. 3474.
ReactomeiR-MMU-350864. Regulation of thyroid hormone activity.

Miscellaneous databases

PROiQ91ZI8.
SOURCEiSearch...

Gene expression databases

BgeeiQ91ZI8.
CleanExiMM_DIO3.
ExpressionAtlasiQ91ZI8. baseline and differential.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000643. Iodothyronine_deiodinase.
IPR008261. Iodothyronine_deiodinase_AS.
IPR027252. Iodothyronine_deiodinase_I/III.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11781. PTHR11781. 1 hit.
PfamiPF00837. T4_deiodinase. 1 hit.
[Graphical view]
PIRSFiPIRSF001330. IOD. 1 hit.
PIRSF500144. IODI_III. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS01205. T4_DEIODINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the mouse gene for the type 3 iodothyronine deiodinase."
    Hernandez A., Lyon G.J., Schneider M.J., St Germain D.L.
    Endocrinology 140:124-130(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  2. "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: Head and Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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] OF 11-304.

Entry informationi

Entry nameiIOD3_MOUSE
AccessioniPrimary (citable) accession number: Q91ZI8
Secondary accession number(s): G3UY28, Q3UKD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: May 14, 2014
Last modified: June 8, 2016
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-27 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.