Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9DCX8

- IYD1_MOUSE

UniProt

Q9DCX8 - IYD1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Iodotyrosine dehalogenase 1

Gene

Iyd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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

  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

Membrane By similarity; Single-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 210187ExtracellularSequence AnalysisAdd
BLAST
Transmembranei211 – 23121HelicalSequence AnalysisAdd
BLAST
Topological domaini232 – 28554CytoplasmicSequence AnalysisAdd
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 – 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 .
CCDSi CCDS56670.1.
RefSeqi NP_081667.1. NM_027391.3.
UniGenei Mm.24153.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

ChiTaRSi Iyd. mouse.
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: November 26, 2014
This is version 90 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