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Protein

Iodotyrosine dehalogenase 1

Gene

Iyd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine (By similarity).By similarity

Catalytic activityi

L-tyrosine + 2 NADP+ + 2 I- = 3,5-diiodo-L-tyrosine + 2 NADPH.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001Substrate
Binding sitei157 – 1571Substrate
Binding sitei178 – 1781Substrate
Binding sitei275 – 2751FMN

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 1005FMN
Nucleotide bindingi123 – 1253FMN
Nucleotide bindingi232 – 2354FMN

GO - Molecular functioni

  • iodide peroxidase activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NADP

Enzyme and pathway databases

BRENDAi1.22.1.1. 3474.
ReactomeiREACT_330649. Thyroxine biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Iodotyrosine dehalogenase 1 (EC:1.22.1.1)
Short name:
IYD-1
Gene namesi
Name:Iyd
Synonyms:Dehal1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1917587. Iyd.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 210187ExtracellularSequence AnalysisAdd
BLAST
Transmembranei211 – 23121HelicalSequence AnalysisAdd
BLAST
Topological domaini232 – 28554CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 285262Iodotyrosine dehalogenase 1PRO_0000230279Add
BLAST

Proteomic databases

MaxQBiQ9DCX8.
PaxDbiQ9DCX8.
PRIDEiQ9DCX8.

PTM databases

PhosphoSiteiQ9DCX8.

Expressioni

Gene expression databases

BgeeiQ9DCX8.
CleanExiMM_IYD.
GenevestigatoriQ9DCX8.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiQ9DCX8. 2 interactions.
MINTiMINT-1857005.
STRINGi10090.ENSMUSP00000019896.

Structurei

Secondary structure

1
285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi69 – 713Combined sources
Helixi79 – 9416Combined sources
Helixi109 – 11911Combined sources
Helixi125 – 1273Combined sources
Beta strandi131 – 1366Combined sources
Helixi139 – 15113Combined sources
Turni159 – 1613Combined sources
Helixi163 – 1697Combined sources
Helixi170 – 1723Combined sources
Helixi180 – 1834Combined sources
Beta strandi184 – 19310Combined sources
Beta strandi203 – 2053Combined sources
Helixi209 – 22618Combined sources
Helixi237 – 2393Combined sources
Helixi240 – 2467Combined sources
Beta strandi253 – 26210Combined sources
Beta strandi269 – 2713Combined sources
Helixi278 – 2803Combined sources
Beta strandi282 – 2843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GB5X-ray2.00A34-285[»]
3GFDX-ray2.45A/B34-285[»]
3GH8X-ray2.61A/B/C/D/E/F/G/H34-285[»]
3TNZX-ray2.25A/B34-285[»]
3TO0X-ray2.66A/B34-285[»]
ProteinModelPortaliQ9DCX8.
SMRiQ9DCX8. Positions 66-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DCX8.

Family & Domainsi

Sequence similaritiesi

Belongs to the nitroreductase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0778.
GeneTreeiENSGT00390000004348.
HOGENOMiHOG000146731.
HOVERGENiHBG055004.
InParanoidiQ9DCX8.
KOiK17231.
OMAiRPAHEKL.
OrthoDBiEOG7HMS24.
PhylomeDBiQ9DCX8.
TreeFamiTF313415.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
InterProiIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DCX8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLLTPVLVA VVCILVVWVF KNADRNLEKK KEEAQVQPWV DEDLKDSTED
60 70 80 90 100
LQVEEDAEEW QEAEESVEHI PFSHTRYPEQ EMRMRSQEFY ELLNKRRSVR
110 120 130 140 150
FISSEHVPME VIENVIKAAG TAPSGAHTEP WTFVVVKDPD MKHKIREIIE
160 170 180 190 200
EEEEINYMKR MGKRWVTDLK KLRTNWIKEY LDTAPVLILI FKQVHGFAAN
210 220 230 240 250
GKKKVHYYNE ISVSIACGLL LAALQNAGLV TVTTTPLNCG PRLRVLLGRP
260 270 280
SHEKLLVLLP VGYPSRDATV PDLKRKALDQ IMVTV
Length:285
Mass (Da):32,814
Last modified:June 1, 2001 - v1
Checksum:i7B7415D6C28B1A58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002363 mRNA. Translation: BAB22041.1.
BC023358 mRNA. Translation: AAH23358.1.
CCDSiCCDS56670.1.
RefSeqiNP_081667.1. NM_027391.3.
UniGeneiMm.24153.

Genome annotation databases

EnsembliENSMUST00000019896; ENSMUSP00000019896; ENSMUSG00000019762.
GeneIDi70337.
KEGGimmu:70337.
UCSCiuc007ehp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002363 mRNA. Translation: BAB22041.1.
BC023358 mRNA. Translation: AAH23358.1.
CCDSiCCDS56670.1.
RefSeqiNP_081667.1. NM_027391.3.
UniGeneiMm.24153.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GB5X-ray2.00A34-285[»]
3GFDX-ray2.45A/B34-285[»]
3GH8X-ray2.61A/B/C/D/E/F/G/H34-285[»]
3TNZX-ray2.25A/B34-285[»]
3TO0X-ray2.66A/B34-285[»]
ProteinModelPortaliQ9DCX8.
SMRiQ9DCX8. Positions 66-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DCX8. 2 interactions.
MINTiMINT-1857005.
STRINGi10090.ENSMUSP00000019896.

PTM databases

PhosphoSiteiQ9DCX8.

Proteomic databases

MaxQBiQ9DCX8.
PaxDbiQ9DCX8.
PRIDEiQ9DCX8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019896; ENSMUSP00000019896; ENSMUSG00000019762.
GeneIDi70337.
KEGGimmu:70337.
UCSCiuc007ehp.1. mouse.

Organism-specific databases

CTDi389434.
MGIiMGI:1917587. Iyd.

Phylogenomic databases

eggNOGiCOG0778.
GeneTreeiENSGT00390000004348.
HOGENOMiHOG000146731.
HOVERGENiHBG055004.
InParanoidiQ9DCX8.
KOiK17231.
OMAiRPAHEKL.
OrthoDBiEOG7HMS24.
PhylomeDBiQ9DCX8.
TreeFamiTF313415.

Enzyme and pathway databases

BRENDAi1.22.1.1. 3474.
ReactomeiREACT_330649. Thyroxine biosynthesis.

Miscellaneous databases

ChiTaRSiIyd. mouse.
EvolutionaryTraceiQ9DCX8.
NextBioi331404.
PROiQ9DCX8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCX8.
CleanExiMM_IYD.
GenevestigatoriQ9DCX8.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
InterProiIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Kidney.
  2. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  3. "Crystal structure of iodotyrosine deiodinase, a novel flavoprotein responsible for iodide salvage in thyroid glands."
    Thomas S.R., McTamney P.M., Adler J.M., Laronde-Leblanc N., Rokita S.E.
    J. Biol. Chem. 284:19659-19667(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-285 IN COMPLEXES WITH 3,5-DIIODOTYROSINE; 3-IODO-TYROSINE AND FMN, SUBUNIT.

Entry informationi

Entry nameiIYD1_MOUSE
AccessioniPrimary (citable) accession number: Q9DCX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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.