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Q9DCX8 (IYD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Iodotyrosine dehalogenase 1
Short name=IYD-1
EC=1.22.1.1
Gene names
Name:Iyd
Synonyms:Dehal1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

FMN.

Subunit structure

Homodimer Probable. Ref.3

Subcellular location

Membrane; Single-pass membrane protein By similarity.

Sequence similarities

Belongs to the nitroreductase family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandFMN
Flavoprotein
NADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioniodide peroxidase activity

Inferred from direct assay PubMed 16316988. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 285262Iodotyrosine dehalogenase 1
PRO_0000230279

Regions

Topological domain24 – 210187Extracellular Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 28554Cytoplasmic Potential
Nucleotide binding96 – 1005FMN
Nucleotide binding123 – 1253FMN
Nucleotide binding232 – 2354FMN

Sites

Binding site1001Substrate
Binding site1571Substrate
Binding site1781Substrate
Binding site2751FMN

Secondary structure

1 .................................... 285
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9DCX8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 7B7415D6C28B1A58

FASTA28532,814
        10         20         30         40         50         60 
MFLLTPVLVA VVCILVVWVF KNADRNLEKK KEEAQVQPWV DEDLKDSTED LQVEEDAEEW 

        70         80         90        100        110        120 
QEAEESVEHI PFSHTRYPEQ EMRMRSQEFY ELLNKRRSVR FISSEHVPME VIENVIKAAG 

       130        140        150        160        170        180 
TAPSGAHTEP WTFVVVKDPD MKHKIREIIE EEEEINYMKR MGKRWVTDLK KLRTNWIKEY 

       190        200        210        220        230        240 
LDTAPVLILI FKQVHGFAAN GKKKVHYYNE ISVSIACGLL LAALQNAGLV TVTTTPLNCG 

       250        260        270        280 
PRLRVLLGRP SHEKLLVLLP VGYPSRDATV PDLKRKALDQ IMVTV

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK002363 mRNA. Translation: BAB22041.1.
BC023358 mRNA. Translation: AAH23358.1.
IPIIPI00121498.
RefSeqNP_081667.1. NM_027391.3.
UniGeneMm.24153.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9DCX8.
SMRQ9DCX8. Positions 66-285.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1857005.
STRING10090.ENSMUSP00000019896.

PTM databases

PhosphoSiteQ9DCX8.

Proteomic databases

PaxDbQ9DCX8.
PRIDEQ9DCX8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019896; ENSMUSP00000019896; ENSMUSG00000019762.
GeneID70337.
KEGGmmu:70337.
UCSCuc007ehp.1. mouse.

Organism-specific databases

CTD389434.
MGIMGI:1917587. Iyd.

Phylogenomic databases

eggNOGCOG0778.
GeneTreeENSGT00390000004348.
HOGENOMHOG000146731.
HOVERGENHBG055004.
InParanoidQ9DCX8.
OMAHQPWHFV.
OrthoDBEOG4JQ3ZB.

Gene expression databases

BgeeQ9DCX8.
CleanExMM_IYD.
GenevestigatorQ9DCX8.
GermOnlineENSMUSG00000019762. Mus musculus.

Family and domain databases

Gene3D3.40.109.10. 1 hit.
InterProIPR000415. Nitroreductase-like.
[Graphical view]
PfamPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMSSF55469. Nitroreductase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9DCX8.
NextBio331404.
SOURCESearch...

Entry information

Entry nameIYD1_MOUSE
AccessionPrimary (citable) accession number: Q9DCX8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: June 1, 2001
Last modified: May 29, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents