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UniProtKB/Swiss-Prot entry Q9NRD9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DUOX1_HUMAN
Primary accession number Q9NRD9
Secondary accession numbers A6NH28 Q14C94 Q6ZMB3 Q6ZR09 Q9NZC1
Integrated into Swiss-Prot on February 21, 2006
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 54)
Name and origin of the protein
Protein name Dual oxidase 1 [Precursor]
Synonyms EC 1.6.3.1
EC 1.11.1.-
NADPH thyroid oxidase 1
Large NOX 1
Long NOX 1
Thyroid oxidase 1
Gene name
Name: DUOX1
Synonyms: DUOX, LNOX1, THOX1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
TISSUE=Thyroid;
DOI=10.1074/jbc.M000916200; PubMed=10806195 [NCBI, ExPASy, EBI, Israel, Japan]
De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G., Dumont J.E., Miot F.;
"Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family.";
J. Biol. Chem. 275:23227-23233(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-1178, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
TISSUE=Lung;
DOI=10.1083/jcb.200103132; PubMed=11514595 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox.";
J. Cell Biol. 154:879-891(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1030-1551 (ISOFORMS 1/2), AND VARIANT ARG-1026.
TISSUE=Lung, and Trachea;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04601; PubMed=16572171 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Analysis of the DNA sequence and duplication history of human chromosome 15.";
Nature 440:671-675(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
GLYCOSYLATION.
DOI=10.1006/excr.2001.5444; PubMed=11822874 [NCBI, ExPASy, EBI, Israel, Japan]
De Deken X., Wang D., Dumont J.E., Miot F.;
"Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system.";
Exp. Cell Res. 273:187-196(2002).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1096/fj.02-1104fje; PubMed=12824283 [NCBI, ExPASy, EBI, Israel, Japan]
Geiszt M., Witta J., Baffi J., Lekstrom K., Leto T.L.;
"Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense.";
FASEB J. 17:1502-1504(2003).
[8]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M404983200; PubMed=15210697 [NCBI, ExPASy, EBI, Israel, Japan]
Schwarzer C., Machen T.E., Illek B., Fischer H.;
"NADPH oxidase-dependent acid production in airway epithelial cells.";
J. Biol. Chem. 279:36454-36461(2004).
[9]
INDUCTION.
DOI=10.1016/j.febslet.2005.08.002; PubMed=16111680 [NCBI, ExPASy, EBI, Israel, Japan]
Harper R.W., Xu C., Eiserich J.P., Chen Y., Kao C.-Y., Thai P., Setiadi H., Wu R.;
"Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium.";
FEBS Lett. 579:4911-4917(2005).
[10]
INTERACTION WITH TXNDC11; TPO AND CYBA.
DOI=10.1074/jbc.M407709200; PubMed=15561711 [NCBI, ExPASy, EBI, Israel, Japan]
Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.;
"Identification of a novel partner of duox: EFP1, a thioredoxin-related protein.";
J. Biol. Chem. 280:3096-3103(2005).
[11]
CATALYTIC ACTIVITY, AND ENZYME REGULATION.
DOI=10.1074/jbc.M500516200; PubMed=15972824 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity.";
J. Biol. Chem. 280:30046-30054(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF230495; AAF73921.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF213465; AAF71295.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK128591; BAC87516.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK172859; BAD18816.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC051619; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC114628; AAI14629.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_059130.2; -.
NP_787954.1; -.
UniGene Hs.272813
3D structure databases
ModBase Q9NRD9.
Protein family/group databases
PeroxiBase 3339; HsDuOx01.
PTM databases
PhosphoSite Q9NRD9; -.
Organism-specific databases
H-InvDB HIX0018395; -.
HGNC HGNC:3062; DUOX1.
GenAtlas DUOX1.
MIM 606758; gene. [NCBI / EBI]
PharmGKB PA27516; -.
GeneCards Q9NRD9.
Gene expression databases
CleanEx HS_DUOX1; -.
GermOnline ENSG00000137857; Homo sapiens.
Ontologies
GO
GO:0016324; Cellular component: apical plasma membrane (non-traceable author statement from UniProtKB).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016174; Molecular function: NAD(P)H oxidase activity (non-traceable author statement from UniProtKB).
GO:0050661; Molecular function: NADP binding (non-traceable author statement from UniProtKB).
GO:0004601; Molecular function: peroxidase activity (inferred from electronic annotation from InterPro).
GO:0042335; Biological process: cuticle development (inferred from mutant phenotype from UniProtKB).
GO:0019221; Biological process: cytokine-mediated signaling pathway (inferred from direct assay from UniProtKB).
GO:0042446; Biological process: hormone biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0050665; Biological process: hydrogen peroxide biosynthetic process (non-traceable author statement from UniProtKB).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (traceable author statement from UniProtKB).
GO:0051591; Biological process: response to cAMP (inferred from direct assay from UniProtKB).
GO:0042554; Biological process: superoxide release (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011992; EF-Hand_type.
IPR002048; EF_hand_Ca_bd.
IPR013112; FAD_bd_8.
IPR013130; Fe3_reduct_TM_N.
IPR013121; Fe_red_NAD_bd_6.
IPR002007; Haem_peroxidase_animal.
IPR001125; Recoverin.
Graphical view of domain structure.
Gene3D G3DSA:1.10.238.10; EF-Hand_type; 1.
G3DSA:1.10.640.10; Haem_peroxidase_animal; 1.
Pfam PF03098; An_peroxidase; 1.
PF00036; efhand; 2.
PF08022; FAD_binding_8; 1.
PF01794; Ferric_reduct; 1.
PF08030; NAD_binding_6; 1.
Pfam graphical view of domain structure.
PRINTS PR00457; ANPEROXIDASE.
PR00450; RECOVERIN.
ProDom PD000012; EF-hand; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00054; EFh; 2.
SMART graphical view of domain structure.
PROSITE PS00018; EF_HAND_1; 2.
PS50222; EF_HAND_2; 3.
PS51384; FAD_FR; 1.
PS50292; PEROXIDASE_3; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9NRD9.
Genome annotation databases
Ensembl ENSG00000137857; Homo sapiens. [Contig view]
GeneID 53905; -.
KEGG hsa:53905; -.
Phylogenomic databases
HOGENOM Q9NRD9; -.
HOVERGEN Q9NRD9; -.
Other
LinkHub Q9NRD9; -.
NextBio 56216; -.
SOURCE DUOX1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Calcium; Cell membrane; FAD; Glycoprotein; Hydrogen peroxide; Membrane; NADP; Oxidoreductase; Peroxidase; Polymorphism; Repeat; Signal; Thyroid hormones biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     21  21     Potential. 
CHAIN   22   1551  1530     Dual oxidase 1. PRO_0000223344
TOPO_DOM   22    596  575     Extracellular (Potential). 
TRANSMEM   597    617  21     Potential. 
TOPO_DOM   618   1044  427     Cytoplasmic (Potential). 
TRANSMEM   1045   1065  21     Potential. 
TOPO_DOM   1066   1080  15     Extracellular (Potential). 
TRANSMEM   1081   1101  21     Potential. 
TOPO_DOM   1102   1148  47     Cytoplasmic (Potential). 
TRANSMEM   1149   1171  23     Potential. 
TOPO_DOM   1172   1188  17     Extracellular (Potential). 
TRANSMEM   1189   1209  21     Potential. 
TOPO_DOM   1210   1226  17     Cytoplasmic (Potential). 
TRANSMEM   1227   1247  21     Potential. 
TOPO_DOM   1248   1248  1     Extracellular (Potential). 
TRANSMEM   1249   1269  21     Potential. 
TOPO_DOM   1270   1551  282     Cytoplasmic (Potential). 
DOMAIN   815    850  36     EF-hand 1. 
DOMAIN   851    886  36     EF-hand 2. 
DOMAIN   895    930  36     EF-hand 3. 
DOMAIN   1087   1269  183     Ferric oxidoreductase. 
DOMAIN   1270   1376  107     FAD-binding FR-type. 
CA_BIND   828    839  12     1 (Potential). 
CA_BIND   864    875  12     2 (Potential). 
REGION   26    593  568     Peroxidase-like; mediates peroxidase activity. 
REGION   956   1248  293     Interaction with TXNDC11 (By similarity). 
CARBOHYD   94     94        N-linked (GlcNAc...) (Potential). 
CARBOHYD   342    342        N-linked (GlcNAc...) (Potential). 
CARBOHYD   354    354        N-linked (GlcNAc...) (Potential). 
CARBOHYD   461    461        N-linked (GlcNAc...) (Potential). 
CARBOHYD   534    534        N-linked (GlcNAc...) (Potential). 
VAR_SEQ   1    354        Missing (in isoform 2). VSP_017262
VAR_SEQ   355    405        SSVSRALRVCNSYWSREHPSLQSAEDVDALLLGMASQIAE REDHVLVEDVR -> MWMHCCWAWPPRSQSERTMCWLKMCGVSLRLSLQVVNSWP LGRGSAGLPEP (in isoform 2). VSP_017263
VARIANT   1026   1026  1     C -> R (in dbSNP:rs16939752 [NCBI]). VAR_025321 
VARIANT   1178   1178  1     L -> F (in dbSNP:rs2458236 [NCBI]). VAR_025322 
CONFLICT   413    413        K -> E (in Ref. 3; BAC87516). 
CONFLICT   1388   1388        G -> R (in Ref. 3; BAD18816). 
Sequence information
Length: 1551 AA [This is the length of the unprocessed precursor] Molecular weight: 177235 Da [This is the MW of the unprocessed precursor] CRC64: 37CF124A579446B0 [This is a checksum on the sequence]
        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 

Q9NRD9 in FASTA format

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