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Q9DCX8

- IYD1_MOUSE

UniProt

Q9DCX8 - IYD1_MOUSE

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Protein
Iodotyrosine dehalogenase 1
Gene
Iyd, Dehal1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

FMN.

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

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NADP

Enzyme and pathway databases

ReactomeiREACT_219697. 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: Chromosome 10

Organism-specific databases

MGIiMGI:1917587. Iyd.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 210187Extracellular Reviewed prediction
Add
BLAST
Transmembranei211 – 23121Helical; Reviewed prediction
Add
BLAST
Topological domaini232 – 28554Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 285262Iodotyrosine dehalogenase 1
PRO_0000230279Add
BLAST

Proteomic databases

MaxQBiQ9DCX8.
PaxDbiQ9DCX8.
PRIDEiQ9DCX8.

PTM databases

PhosphoSiteiQ9DCX8.

Expressioni

Gene expression databases

BgeeiQ9DCX8.
CleanExiMM_IYD.
GenevestigatoriQ9DCX8.

Interactioni

Subunit structurei

Homodimer Inferred.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ9DCX8.

Family & Domainsi

Sequence similaritiesi

Belongs to the nitroreductase family.

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

MFLLTPVLVA VVCILVVWVF KNADRNLEKK KEEAQVQPWV DEDLKDSTED    50
LQVEEDAEEW QEAEESVEHI PFSHTRYPEQ EMRMRSQEFY ELLNKRRSVR 100
FISSEHVPME VIENVIKAAG TAPSGAHTEP WTFVVVKDPD MKHKIREIIE 150
EEEEINYMKR MGKRWVTDLK KLRTNWIKEY LDTAPVLILI FKQVHGFAAN 200
GKKKVHYYNE ISVSIACGLL LAALQNAGLV TVTTTPLNCG PRLRVLLGRP 250
SHEKLLVLLP VGYPSRDATV PDLKRKALDQ IMVTV 285
Length:285
Mass (Da):32,814
Last modified:June 1, 2001 - v1
Checksum:i7B7415D6C28B1A58
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK002363 mRNA. Translation: BAB22041.1 .
BC023358 mRNA. Translation: AAH23358.1 .
CCDSi CCDS56670.1.
RefSeqi NP_081667.1. NM_027391.3.
UniGenei Mm.24153.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GB5 X-ray 2.00 A 34-285 [» ]
3GFD X-ray 2.45 A/B 34-285 [» ]
3GH8 X-ray 2.61 A/B/C/D/E/F/G/H 34-285 [» ]
3TNZ X-ray 2.25 A/B 34-285 [» ]
3TO0 X-ray 2.66 A/B 34-285 [» ]
ProteinModelPortali Q9DCX8.
SMRi Q9DCX8. Positions 66-285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9DCX8. 2 interactions.
MINTi MINT-1857005.
STRINGi 10090.ENSMUSP00000019896.

PTM databases

PhosphoSitei Q9DCX8.

Proteomic databases

MaxQBi Q9DCX8.
PaxDbi Q9DCX8.
PRIDEi Q9DCX8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000019896 ; ENSMUSP00000019896 ; ENSMUSG00000019762 .
GeneIDi 70337.
KEGGi mmu:70337.
UCSCi uc007ehp.1. mouse.

Organism-specific databases

CTDi 389434.
MGIi MGI:1917587. Iyd.

Phylogenomic databases

eggNOGi COG0778.
GeneTreei ENSGT00390000004348.
HOGENOMi HOG000146731.
HOVERGENi HBG055004.
InParanoidi Q9DCX8.
KOi K17231.
OMAi RPAHEKL.
OrthoDBi EOG7HMS24.
PhylomeDBi Q9DCX8.
TreeFami TF313415.

Enzyme and pathway databases

Reactomei REACT_219697. Thyroxine biosynthesis.

Miscellaneous databases

EvolutionaryTracei Q9DCX8.
NextBioi 331404.
PROi Q9DCX8.
SOURCEi Search...

Gene expression databases

Bgeei Q9DCX8.
CleanExi MM_IYD.
Genevestigatori Q9DCX8.

Family and domain databases

Gene3Di 3.40.109.10. 1 hit.
InterProi IPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view ]
Pfami PF00881. Nitroreductase. 1 hit.
[Graphical view ]
SUPFAMi SSF55469. SSF55469. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 88 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