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Protein

Type I iodothyronine deiodinase

Gene

dio1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine) and of T3 into T2 (3,3'-diiodothyronine).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei130 – 1301

GO - Molecular functioni

  1. thyroxine 5'-deiodinase activity Source: UniProtKB-EC

GO - Biological processi

  1. hormone biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Thyroid hormones biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Type I iodothyronine deiodinase (EC:1.97.1.10)
Alternative name(s):
5DI
DIOI
Type 1 DI
Type-I 5'-deiodinase
Gene namesi
Name:dio1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-979948. dio1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei18 – 3821HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252Type I iodothyronine deiodinasePRO_0000318637Add
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the iodothyronine deiodinase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG000099.
KOiK01562.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q2QEI3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESLLQTIKL MLRYIQKALI LFFLFLYVVV GKVLMFLFPQ TMASVLKSRF
60 70 80 90 100
EISGVHDPKF QYEDWGPTFF TYKFLRSVLE IMWMRLEDEA FVGHSAPNTP
110 120 130 140 150
VVDLSGELHH IWDYLQGTRP LVLSFGSCTU PPFLFRLGEF NKLVNEFNSI
160 170 180 190 200
ADFLIIYIDE AHAADEWALK NNLHIKKHRS LQDRLAAAKR LMEESPSCPV
210 220 230 240 250
VLDTMSNLCS AKYAALPERL YILQEGKIIY KGKMGPWGYK PEEVCSVLEK

KK
Length:252
Mass (Da):29,187
Last modified:February 26, 2008 - v2
Checksum:i026288D0E636D131
GO

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei130 – 1301Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ098656 mRNA. Translation: AAZ43088.1.
RefSeqiNP_001089136.1. NM_001095667.1.
UniGeneiXl.17649.

Genome annotation databases

GeneIDi733447.
KEGGixla:733447.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ098656 mRNA. Translation: AAZ43088.1.
RefSeqiNP_001089136.1. NM_001095667.1.
UniGeneiXl.17649.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi733447.
KEGGixla:733447.

Organism-specific databases

CTDi1733.
XenbaseiXB-GENE-979948. dio1.

Phylogenomic databases

HOVERGENiHBG000099.
KOiK01562.

Family and domain databases

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

Publicationsi

  1. "Characterization of recombinant Xenopus laevis type I iodothyronine deiodinase: substitution of a proline residue in the catalytic center by serine (Pro132Ser) restores sensitivity to 6-propyl-2-thiouracil."
    Kuiper G.G., Klootwijk W., Morvan Dubois G., Destree O., Darras V.M., Van der Geyten S., Demeneix B., Visser T.J.
    Endocrinology 147:3519-3529(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiIOD1_XENLA
AccessioniPrimary (citable) accession number: Q2QEI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: January 7, 2015
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.