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Q9NRD9 (DUOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Alternative name(s):
Large NOX 1
Long NOX 1
NADPH thyroid oxidase 1
Thyroid oxidase 1
Gene names
Name:DUOX1
Synonyms:DUOX, LNOX1, THOX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.2 Ref.7

Catalytic activity

NAD(P)H + O2 = NAD(P)+ + H2O2. Ref.2 Ref.11

Enzyme regulation

The NADPH oxidase activity is calcium-dependent. Peroxidase activity is inhibited by aminobenzohydrazide. Ref.2 Ref.11

Pathway

Hormone biosynthesis; thyroid hormone biosynthesis.

Subunit structure

Interacts with TXNDC11, TPO and CYBA. Ref.10

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Note: Localizes to the apical membrane of epithelial cells. Ref.1 Ref.8

Tissue specificity

Expressed in thyrocytes and tracheal surface epithelial cells (at protein level). Expressed in thyroid, trachea, bronchium, and to a lower extent, in placenta, testis, prostate, pancreas and heart. Ref.1 Ref.2 Ref.7 Ref.8

Developmental stage

Widely expressed in fetal tissues. Ref.2

Induction

By forskolin (at protein level). By thyrotropin and the Th2-specific cytokines IL-4 and IL-13. Ref.1 Ref.2 Ref.9 Ref.11

Post-translational modification

N-glycosylated. Ref.6

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 caution

The sequence AK128591 differs from that shown. Reason: Erroneous termination at position 967. Translated as Arg.

The sequence BAD18816.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHydrogen peroxide
Thyroid hormones biosynthesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
FAD
Flavoprotein
Metal-binding
NADP
   Molecular functionOxidoreductase
Peroxidase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcuticle development

Inferred from mutant phenotype Ref.2. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from direct assay Ref.9. Source: UniProtKB

hormone biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

hydrogen peroxide biosynthetic process

Non-traceable author statement Ref.1. Source: UniProtKB

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation-reduction process

Traceable author statement PubMed 10601291. Source: UniProtKB

response to cAMP

Inferred from direct assay PubMed 15062544. Source: UniProtKB

superoxide anion generation

Non-traceable author statement Ref.1. Source: UniProtKB

thyroid hormone generation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentapical plasma membrane

Non-traceable author statement Ref.1. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionNAD(P)H oxidase activity

Non-traceable author statement Ref.1. Source: UniProtKB

NADP binding

Non-traceable author statement Ref.1. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRD9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NRD9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-354: Missing.
     355-405: SSVSRALRVC...EDHVLVEDVR → MWMHCCWAWP...GRGSAGLPEP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 15511530Dual oxidase 1
PRO_0000223344

Regions

Topological domain22 – 596575Extracellular Potential
Transmembrane597 – 61721Helical; Potential
Topological domain618 – 1044427Cytoplasmic Potential
Transmembrane1045 – 106521Helical; Potential
Topological domain1066 – 108015Extracellular Potential
Transmembrane1081 – 110121Helical; Potential
Topological domain1102 – 114847Cytoplasmic Potential
Transmembrane1149 – 117123Helical; Potential
Topological domain1172 – 118817Extracellular Potential
Transmembrane1189 – 120921Helical; Potential
Topological domain1210 – 122617Cytoplasmic Potential
Transmembrane1227 – 124721Helical; Potential
Topological domain12481Extracellular Potential
Transmembrane1249 – 126921Helical; Potential
Topological domain1270 – 1551282Cytoplasmic Potential
Domain815 – 85036EF-hand 1
Domain851 – 88636EF-hand 2
Domain895 – 93036EF-hand 3
Domain1087 – 1269183Ferric oxidoreductase
Domain1270 – 1376107FAD-binding FR-type
Calcium binding828 – 839121 Potential
Calcium binding864 – 875122 Potential
Region26 – 593568Peroxidase-like; mediates peroxidase activity
Region956 – 1248293Interaction with TXNDC11 By similarity

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 354354Missing in isoform 2.
VSP_017262
Alternative sequence355 – 40551SSVSR…VEDVR → MWMHCCWAWPPRSQSERTMC WLKMCGVSLRLSLQVVNSWP LGRGSAGLPEP in isoform 2.
VSP_017263
Natural variant9621I → T.
Corresponds to variant rs16939743 [ dbSNP | Ensembl ].
VAR_049104
Natural variant10261C → R. Ref.3
Corresponds to variant rs16939752 [ dbSNP | Ensembl ].
VAR_025321
Natural variant11781L → F. Ref.2
Corresponds to variant rs2458236 [ dbSNP | Ensembl ].
VAR_025322

Experimental info

Sequence conflict4131K → E in AK128591. Ref.3
Sequence conflict13881G → R in BAD18816. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 37CF124A579446B0

FASTA1,551177,235
        10         20         30         40         50         60 
MGFCLALAWT LLVGAWTPLG AQNPISWEVQ RFDGWYNNLM EHRWGSKGSR LQRLVPASYA 

        70         80         90        100        110        120 
DGVYQPLGEP HLPNPRDLSN TISRGPAGLA SLRNRTVLGV FFGYHVLSDL VSVETPGCPA 

       130        140        150        160        170        180 
EFLNIRIPPG DPMFDPDQRG DVVLPFQRSR WDPETGRSPS NPRDPANQVT GWLDGSAIYG 

       190        200        210        220        230        240 
SSHSWSDALR SFSRGQLASG PDPAFPRDSQ NPLLMWAAPD PATGQNGPRG LYAFGAERGN 

       250        260        270        280        290        300 
REPFLQALGL LWFRYHNLWA QRLARQHPDW EDEELFQHAR KRVIATYQNI AVYEWLPSFL 

       310        320        330        340        350        360 
QKTLPEYTGY RPFLDPSISS EFVAASEQFL STMVPPGVYM RNASCHFQGV INRNSSVSRA 

       370        380        390        400        410        420 
LRVCNSYWSR EHPSLQSAED VDALLLGMAS QIAEREDHVL VEDVRDFWPG PLKFSRTDHL 

       430        440        450        460        470        480 
ASCLQRGRDL GLPSYTKARA ALGLSPITRW QDINPALSRS NDTVLEATAA LYNQDLSWLE 

       490        500        510        520        530        540 
LLPGGLLESH RDPGPLFSTI VLEQFVRLRD GDRYWFENTR NGLFSKKEIE EIRNTTLQDV 

       550        560        570        580        590        600 
LVAVINIDPS ALQPNVFVWH KGDPCPQPRQ LSTEGLPACA PSVVRDYFEG SGFGFGVTIG 

       610        620        630        640        650        660 
TLCCFPLVSL LSAWIVARLR MRNFKRLQGQ DRQSIVSEKL VGGMEALEWQ GHKEPCRPVL 

       670        680        690        700        710        720 
VYLQPGQIRV VDGRLTVLRT IQLQPPQKVN FVLSSNRGRR TLLLKIPKEY DLVLLFNLEE 

       730        740        750        760        770        780 
ERQALVENLR GALKESGLSI QEWELREQEL MRAAVTREQR RHLLETFFRH LFSQVLDINQ 

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

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

       910        920        930        940        950        960 
ESMFRESGFQ DKEELTWEDF HFMLRDHNSE LRFTQLCVKG VEVPEVIKDL CRRASYISQD 

       970        980        990       1000       1010       1020 
MICPSPRVSA RCSRSDIETE LTPQRLQCPM DTDPPQEIRR RFGKKVTSFQ PLLFTEAHRE 

      1030       1040       1050       1060       1070       1080 
KFQRSCLHQT VQQFKRFIEN YRRHIGCVAV FYAIAGGLFL ERAYYYAFAA HHTGITDTTR 

      1090       1100       1110       1120       1130       1140 
VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY VPFDAAVDFH RLIASTAIVL 

      1150       1160       1170       1180       1190       1200 
TVLHSVGHVV NVYLFSISPL SVLSCLFPGL FHDDGSELPQ KYYWWFFQTV PGLTGVVLLL 

      1210       1220       1230       1240       1250       1260 
ILAIMYVFAS HHFRRRSFRG FWLTHHLYIL LYVLLIIHGS FALIQLPRFH IFFLVPAIIY 

      1270       1280       1290       1300       1310       1320 
GGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY KSGQWVRIAC LALGTTEYHP 

      1330       1340       1350       1360       1370       1380 
FTLTSAPHED TLSLHIRAAG PWTTRLREIY SAPTGDRCAR YPKLYLDGPF GEGHQEWHKF 

      1390       1400       1410       1420       1430       1440 
EVSVLVGGGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE 

      1450       1460       1470       1480       1490       1500 
ENDHQDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSI THFGRPPFEP 

      1510       1520       1530       1540       1550 
FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINRQD RTHFSHHYEN F 

« Hide

Isoform 2 [UniParc].

Checksum: 44391BD31C81E18F
Show »

FASTA1,197137,604

References

« Hide 'large scale' references
[1]"Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family."
De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G., Dumont J.E., Miot F.
J. Biol. Chem. 275:23227-23233(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
Tissue: Thyroid.
[2]"Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox."
Edens W.A., Sharling L., Cheng G., Shapira R., Kinkade J.M., Lee T., Edens H.A., Tang X., Sullards C., Flaherty D.B., Benian G.M., Lambeth J.D.
J. Cell Biol. 154:879-891(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-1178, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Tissue: Lung.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1030-1551 (ISOFORMS 1/2), VARIANT ARG-1026.
Tissue: Lung and Trachea.
[4]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
[6]"Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system."
De Deken X., Wang D., Dumont J.E., Miot F.
Exp. Cell Res. 273:187-196(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[7]"Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense."
Geiszt M., Witta J., Baffi J., Lekstrom K., Leto T.L.
FASEB J. 17:1502-1504(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[8]"NADPH oxidase-dependent acid production in airway epithelial cells."
Schwarzer C., Machen T.E., Illek B., Fischer H.
J. Biol. Chem. 279:36454-36461(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium."
Harper R.W., Xu C., Eiserich J.P., Chen Y., Kao C.-Y., Thai P., Setiadi H., Wu R.
FEBS Lett. 579:4911-4917(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"Identification of a novel partner of duox: EFP1, a thioredoxin-related protein."
Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.
J. Biol. Chem. 280:3096-3103(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TXNDC11; TPO AND CYBA.
[11]"Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity."
Ameziane-El-Hassani R., Morand S., Boucher J.L., Frapart Y.-M., Apostolou D., Agnandji D., Gnidehou S., Ohayon R., Noel-Hudson M.-S., Francon J., Lalaoui K., Virion A., Dupuy C.
J. Biol. Chem. 280:30046-30054(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF230495 mRNA. Translation: AAF73921.1.
AF213465 mRNA. Translation: AAF71295.1.
AK128591 mRNA. No translation available.
AK172859 mRNA. Translation: BAD18816.1. Different initiation.
AC051619 Genomic DNA. No translation available.
BC114628 mRNA. Translation: AAI14629.1.
RefSeqNP_059130.2. NM_017434.4.
NP_787954.1. NM_175940.2.
UniGeneHs.272813.

3D structure databases

ProteinModelPortalQ9NRD9.
SMRQ9NRD9. Positions 8-541, 765-934, 1364-1551.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000317997.

Protein family/group databases

PeroxiBase3339. HsDuOx01.
TCDB5.B.1.2.1. the phagocyte (gp91(phox)) nadph oxidase family.

PTM databases

PhosphoSiteQ9NRD9.

Polymorphism databases

DMDM74719102.

Proteomic databases

PaxDbQ9NRD9.
PRIDEQ9NRD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321429; ENSP00000317997; ENSG00000137857. [Q9NRD9-1]
ENST00000389037; ENSP00000373689; ENSG00000137857. [Q9NRD9-1]
ENST00000561166; ENSP00000454065; ENSG00000137857. [Q9NRD9-2]
GeneID53905.
KEGGhsa:53905.
UCSCuc001zus.1. human. [Q9NRD9-1]

Organism-specific databases

CTD53905.
GeneCardsGC15P045422.
HGNCHGNC:3062. DUOX1.
HPAHPA023544.
MIM606758. gene.
neXtProtNX_Q9NRD9.
PharmGKBPA27516.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5126.
HOGENOMHOG000231774.
HOVERGENHBG080428.
InParanoidQ9NRD9.
KOK13411.
OMAIEIEKCD.
OrthoDBEOG7GN2KV.
PhylomeDBQ9NRD9.
TreeFamTF105424.

Enzyme and pathway databases

SABIO-RKQ9NRD9.
UniPathwayUPA00194.

Gene expression databases

ArrayExpressQ9NRD9.
BgeeQ9NRD9.
CleanExHS_DUOX1.
GenevestigatorQ9NRD9.

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...

Other

GeneWikiDual_oxidase_1.
GenomeRNAi53905.
NextBio56216.
PROQ9NRD9.
SOURCESearch...

Entry information

Entry nameDUOX1_HUMAN
AccessionPrimary (citable) accession number: Q9NRD9
Secondary accession number(s): A6NH28 expand/collapse secondary AC list , Q14C94, Q6ZMB3, Q6ZR09, Q9NZC1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM