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Q8HZK3 (DUOX1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Dual oxidase 1

EC=1.11.1.-
EC=1.6.3.1
Gene names
Name:DUOX1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length1553 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain.

Catalytic activity

NAD(P)H + O2 = NAD(P)+ + H2O2.

Enzyme regulation

The NADPH oxidase activity is calcium-dependent. Peroxidase activity is inhibited by aminobenzohydrazide By similarity.

Pathway

Hormone biosynthesis; thyroid hormone biosynthesis.

Subunit structure

Interacts with TXNDC11, TPO and CYBA By similarity.

Subcellular location

Apical cell membrane; Multi-pass membrane protein By similarity. Note: Localizes to the apical membrane of epithelial cells By similarity.

Tissue specificity

Specifically expressed in thyroid. Ref.2

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

In the N-terminal section; belongs to the peroxidase family.

Contains 3 EF-hand domains.

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 15531532Dual oxidase 1
PRO_0000223345

Regions

Topological domain22 – 596575Extracellular Potential
Transmembrane597 – 61721Helical; Potential
Topological domain618 – 1046429Cytoplasmic Potential
Transmembrane1047 – 106721Helical; Potential
Topological domain1068 – 108215Extracellular Potential
Transmembrane1083 – 110321Helical; Potential
Topological domain1104 – 113835Cytoplasmic Potential
Transmembrane1139 – 115921Helical; Potential
Topological domain1160 – 119031Extracellular Potential
Transmembrane1191 – 121121Helical; Potential
Topological domain1212 – 122817Cytoplasmic Potential
Transmembrane1229 – 124921Helical; Potential
Topological domain12501Extracellular Potential
Transmembrane1251 – 127121Helical; Potential
Topological domain1272 – 1553282Cytoplasmic Potential
Domain815 – 85036EF-hand 1
Domain851 – 88636EF-hand 2
Domain895 – 93036EF-hand 3
Domain1089 – 1271183Ferric oxidoreductase
Domain1272 – 1378107FAD-binding FR-type
Calcium binding828 – 839121 Potential
Calcium binding864 – 875122 Potential
Region26 – 593568Peroxidase-like; mediates peroxidase activity By similarity
Region956 – 1250295Interaction with TXNDC11 By similarity

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8HZK3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 9F9364322977B710

FASTA1,553177,861
        10         20         30         40         50         60 
MGFRLALAWT LLVGPWMPMG ARNSISWEVQ RFDGWYNNLM EHKWGSKGSR LQRLVPASYA 

        70         80         90        100        110        120 
DGVYQPLGEP HLPNPRDLSN TAMRGPAGQA SLRNRTVLGV FFGYHVLSDL VSIEKPGCPA 

       130        140        150        160        170        180 
EFLNIHIPPG DPVFDPHKSG DVVLPFQRSR WDPNTGQSPS NPRDLTNEVT GWLDGSAIYG 

       190        200        210        220        230        240 
SSHSWSDELR SFSGGQLASG PDPAFPRQAQ DPLFMWTPPD PATGQRGPQG LYAFGAEQGN 

       250        260        270        280        290        300 
REPFLQALGL LWFRYHNLCA QKLAREHPLW GDEELFQHAR KRVIATYQSI TMYEWLPSFL 

       310        320        330        340        350        360 
RKMPQEYTGY RPFLDPSISP EFLAASEQFF STMVPPGVYM RNASCHFQGV INRNSSVSRA 

       370        380        390        400        410        420 
LRVCNSYWSR EHPNLQRAED VDALLLGMAS QIAEREDHMV VEDVQDFWPG PLKFSRTDHL 

       430        440        450        460        470        480 
ASCLQRGRDL GLPSYTKARA RLGLPPVTRW QDINPALSRS DGIVLEATAA LYNQDLSRLE 

       490        500        510        520        530        540 
LLPGGLLESY GDPGPLFSTI VLDQFVRLRD GDRYWFENTK NGLFSEKEIA EIRNTSLRDV 

       550        560        570        580        590        600 
LVAVTNMTPG ALQPNVFFWH AGDPCPQPRQ LSTKDLPACA PLIMRDYFKG SGFGFGVTIG 

       610        620        630        640        650        660 
TLCCFPLVSL LSAWIVAQLR RRNFKRLQVQ NRQSIMCEKL VGGMKALEWQ GRKEPCRPVL 

       670        680        690        700        710        720 
VHLQSGQIHV MDGRLSVLRT IQLRPPQQVN LILSSNHGRR TLLLKIPKEY DLVLMFDLEE 

       730        740        750        760        770        780 
ERQVMVENLQ SALKESGLSF QEWELREQEL MRAAVTREQR SHLLETFFRH LFSQVLDIDQ 

       790        800        810        820        830        840 
ADAGALPLDS SQKVREALTC ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF 

       850        860        870        880        890        900 
LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLTEVV 

       910        920        930        940        950        960 
ESMFREAGFQ DKQELTWEDF HFMLRDHDSE LRFTQLCVKG VEVPEVIKDL CRRASYISQE 

       970        980        990       1000       1010       1020 
KLCPSPRVSA HCPRSNVDVE VELTPWKLQC PTDTDPPQEI RRRFGKKVTS FQPLLFTEAH 

      1030       1040       1050       1060       1070       1080 
REKFQRSRRH QTVQQFKRFV ENYRRHIGCL AVFYTIAGGL FLERAYYYAF AAHHMGITDT 

      1090       1100       1110       1120       1130       1140 
TRVGIILSRG TAASISFMFS YILLTMCRNL ITFLRETFLN RYVPFDAAVD FHRLIASTAI 

      1150       1160       1170       1180       1190       1200 
ILTVLHSAGH VVNVYLFSIS PLSVLSCLFP GLFHDNGSEF PQKYYWWFFQ TVPGLTGVML 

      1210       1220       1230       1240       1250       1260 
LLILAIMYVF ASHHFRRCSF RGFWLTHHLY ILLYMLLIIH GSFALIQLPR FHIFFLVPAL 

      1270       1280       1290       1300       1310       1320 
IYVGDKLVSL SRKKVEISVV KAELLPSGVT HLQFQRPQGF EYKSGQWVRI ACLALGTTEY 

      1330       1340       1350       1360       1370       1380 
HPFTLTSAPH EDTLSLHIRA AGPWTTRLRE IYSPPTDDNC AKYPKLYLDG PFGEGHQEWH 

      1390       1400       1410       1420       1430       1440 
KFEVSVLVGG GIGVTPFASI LKDLVFKSSV SCQVFCKKIY FIWVTRTQRQ FEWLADIIRE 

      1450       1460       1470       1480       1490       1500 
VEENDHRDLV SVHIYITQLA EKFDLRTTML YICERHFQKV LNRSLFTGLR SITHFGRPPF 

      1510       1520       1530       1540       1550 
EPFFNSLQEV HPQVRKIGVF SCGPPGMTKN VEKACQLINR QDRTHFSHHY ENF 

« Hide

References

[1]"Effect of iodide on nicotinamide adenine dinucleotide phosphate oxidase activity and Duox2 protein expression in isolated porcine thyroid follicles."
Morand S., Chaaraoui M., Kaniewski J., Deme D., Ohayon R., Noel-Hudson M.-S., Virion A., Dupuy C.
Endocrinology 144:1241-1248(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Thyroid.
[2]"Dual oxidase2 is expressed all along the digestive tract."
Ameziane-El-Hassani R., Benfares N., Caillou B., Talbot M., Sabourin J.-C., Belotte V., Morand S., Gnidehou S., Agnandji D., Ohayon R., Kaniewski J., Noel-Hudson M.-S., Bidart J.-M., Schlumberger M., Virion A., Dupuy C.
Am. J. Physiol. 288:G933-G942(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF547266 mRNA. Translation: AAN39338.1.
RefSeqNP_999261.1. NM_214096.2.
UniGeneSsc.35919.

3D structure databases

ProteinModelPortalQ8HZK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000005035.

Protein family/group databases

PeroxiBase3348. SscDuOx01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397177.
KEGGssc:397177.

Organism-specific databases

CTD53905.

Phylogenomic databases

eggNOGCOG5126.
HOGENOMHOG000231774.
HOVERGENHBG080428.
KOK13411.

Enzyme and pathway databases

UniPathwayUPA00194.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.640.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
PF13499. EF-hand_7. 1 hit.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF48113. SSF48113. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS51384. FAD_FR. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDUOX1_PIG
AccessionPrimary (citable) accession number: Q8HZK3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways