Reviewed, UniProtKB/Swiss-Prot Q9NRD9 (DUOX1_HUMAN)

Names and origin

Protein names

Recommended name:
    Dual oxidase 1
    EC=1.6.3.1
    EC=1.11.1.-
Alternative name(s):
    NADPH thyroid oxidase 1
    Large NOX 1
    Long NOX 1
    Thyroid oxidase 1

Gene names

Name:	DUOX1
Synonyms:	DUOX, LNOX1, THOX1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1551 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.2 Ref.7 Ref.1 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.9
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.

Ontologies

Keywords
Biological process	Hydrogen peroxide Thyroid hormones biosynthesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane
Ligand	Calcium FAD NADP
Molecular function	Oxidoreductase Peroxidase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cuticle development Ref.2 Inferred from mutant phenotype. Source: UniProtKB cytokine-mediated signaling pathway Ref.9 Inferred from direct assay. Source: UniProtKB hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW hydrogen peroxide biosynthetic process Ref.1 Non-traceable author statement. Source: UniProtKB hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Traceable author statement. Source: UniProtKB response to cAMP Inferred from direct assay. Source: UniProtKB superoxide release Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	apical plasma membrane Ref.1 Non-traceable author statement. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NAD(P)H oxidase activity Ref.1 Non-traceable author statement. Source: UniProtKB NADP or NADPH binding Ref.1 Non-traceable author statement. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 1551	1530	Dual oxidase 1		PRO_0000223344
Regions
	Topological domain	22 – 596	575	Extracellular Potential
	Transmembrane	597 – 617	21	Potential
	Topological domain	618 – 1044	427	Cytoplasmic Potential
	Transmembrane	1045 – 1065	21	Potential
	Topological domain	1066 – 1080	15	Extracellular Potential
	Transmembrane	1081 – 1101	21	Potential
	Topological domain	1102 – 1148	47	Cytoplasmic Potential
	Transmembrane	1149 – 1171	23	Potential
	Topological domain	1172 – 1188	17	Extracellular Potential
	Transmembrane	1189 – 1209	21	Potential
	Topological domain	1210 – 1226	17	Cytoplasmic Potential
	Transmembrane	1227 – 1247	21	Potential
	Topological domain	1248	1	Extracellular Potential
	Transmembrane	1249 – 1269	21	Potential
	Topological domain	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
	Calcium binding	828 – 839	12	1 Potential
	Calcium binding	864 – 875	12	2 Potential
	Region	26 – 593	568	Peroxidase-like; mediates peroxidase activity
	Region	956 – 1248	293	Interaction with TXNDC11 By similarity
Amino acid modifications
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	342	1	N-linked (GlcNAc...) Potential
	Glycosylation	354	1	N-linked (GlcNAc...) Potential
	Glycosylation	461	1	N-linked (GlcNAc...) Potential
	Glycosylation	534	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 354	354	Missing in isoform 2.		VSP_017262
	Alternative sequence	355 – 405	51	SSVSR…VEDVR → MWMHCCWAWPPRSQSERTMC WLKMCGVSLRLSLQVVNSWP LGRGSAGLPEP in isoform 2.		VSP_017263
	Natural variant	962	1	I → T: dbSNP rs16939743.		VAR_049104
	Natural variant	1026	1	C → R: dbSNP rs16939752. Ref.3		VAR_025321
	Natural variant	1178	1	L → F: dbSNP rs2458236. Ref.2		VAR_025322
Experimental info
	Sequence conflict	413	1	K → E in AK128591. Ref.3
	Sequence conflict	1388	1	G → R in BAD18816. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 37CF124A579446B0	FASTA	1,551	177,235
	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
	Isoform 2. Checksum: 44391BD31C81E18F	FASTA	1,197	137,604
	10 20 30 40 50 60 MWMHCCWAWP PRSQSERTMC WLKMCGVSLR LSLQVVNSWP LGRGSAGLPE PDFWPGPLKF 70 80 90 100 110 120 SRTDHLASCL QRGRDLGLPS YTKARAALGL SPITRWQDIN PALSRSNDTV LEATAALYNQ 130 140 150 160 170 180 DLSWLELLPG GLLESHRDPG PLFSTIVLEQ FVRLRDGDRY WFENTRNGLF SKKEIEEIRN 190 200 210 220 230 240 TTLQDVLVAV INIDPSALQP NVFVWHKGDP CPQPRQLSTE GLPACAPSVV RDYFEGSGFG 250 260 270 280 290 300 FGVTIGTLCC FPLVSLLSAW IVARLRMRNF KRLQGQDRQS IVSEKLVGGM EALEWQGHKE 310 320 330 340 350 360 PCRPVLVYLQ PGQIRVVDGR LTVLRTIQLQ PPQKVNFVLS SNRGRRTLLL KIPKEYDLVL 370 380 390 400 410 420 LFNLEEERQA LVENLRGALK ESGLSIQEWE LREQELMRAA VTREQRRHLL ETFFRHLFSQ 430 440 450 460 470 480 VLDINQADAG TLPLDSSQKV REALTCELSR AEFAESLGLK PQDMFVESMF SLADKDGNGY 490 500 510 520 530 540 LSFREFLDIL VVFMKGSPEE KSRLMFRMYD FDGNGLISKD EFIRMLRSFI EISNNCLSKA 550 560 570 580 590 600 QLAEVVESMF RESGFQDKEE LTWEDFHFML RDHNSELRFT QLCVKGVEVP EVIKDLCRRA 610 620 630 640 650 660 SYISQDMICP SPRVSARCSR SDIETELTPQ RLQCPMDTDP PQEIRRRFGK KVTSFQPLLF 670 680 690 700 710 720 TEAHREKFQR SCLHQTVQQF KRFIENYRRH IGCVAVFYAI AGGLFLERAY YYAFAAHHTG 730 740 750 760 770 780 ITDTTRVGII LSRGTAASIS FMFSYILLTM CRNLITFLRE TFLNRYVPFD AAVDFHRLIA 790 800 810 820 830 840 STAIVLTVLH SVGHVVNVYL FSISPLSVLS CLFPGLFHDD GSELPQKYYW WFFQTVPGLT 850 860 870 880 890 900 GVVLLLILAI MYVFASHHFR RRSFRGFWLT HHLYILLYVL LIIHGSFALI QLPRFHIFFL 910 920 930 940 950 960 VPAIIYGGDK LVSLSRKKVE ISVVKAELLP SGVTHLRFQR PQGFEYKSGQ WVRIACLALG 970 980 990 1000 1010 1020 TTEYHPFTLT SAPHEDTLSL HIRAAGPWTT RLREIYSAPT GDRCARYPKL YLDGPFGEGH 1030 1040 1050 1060 1070 1080 QEWHKFEVSV LVGGGIGVTP FASILKDLVF KSSVSCQVFC KKIYFIWVTR TQRQFEWLAD 1090 1100 1110 1120 1130 1140 IIREVEENDH QDLVSVHIYI TQLAEKFDLR TTMLYICERH FQKVLNRSLF TGLRSITHFG 1150 1160 1170 1180 1190 RPPFEPFFNS LQEVHPQVRK IGVFSCGPPG MTKNVEKACQ LINRQDRTHF SHHYENF

References

	« Hide 'large scale' referencesShow '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: 10806195] [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: 11514595] [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. , 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: 14702039] [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. , 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: 16572171] [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: 15489334] [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: 11822874] [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: 12824283] [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: 15210697] [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: 16111680] [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: 15561711] [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: 15972824] [Abstract] Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00185038. IPI00719817.
RefSeq	NP_059130.2. NP_787954.1.
UniGene	Hs.272813
3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	3339. HsDuOx01.
TCDB	5.B.1.2.1. phagocyte (gp91phox) NADPH oxidase family.
PTM databases
PhosphoSite	Q9NRD9.
Proteomic databases
PRIDE	Q9NRD9.
Genome annotation databases
Ensembl	ENSG00000137857. Homo sapiens. [Contig view]
GeneID	53905.
KEGG	hsa:53905.
UCSC	uc001zus.1. human.
Organism-specific databases
GeneCards	GC15P043209.
H-InvDB	HIX0018395.
HGNC	HGNC:3062. DUOX1.
MIM	606758. gene.
PharmGKB	PA27516.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9NRD9.
HOVERGEN	Q9NRD9.
OMA	Q9NRD9. WLAGDPC.
Enzyme and pathway databases
BRENDA	1.6.3.1. 247.
Gene expression databases
Bgee	Q9NRD9.
CleanEx	HS_DUOX1.
GermOnline	ENSG00000137857. Homo sapiens.
Family and domain databases
InterPro	IPR011992. EF-Hand_type. IPR018248. EF_hand. IPR018247. EF_HAND_1. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR013112. FAD_bd_8. IPR017927. Fd_Rdtase_FAD-bd. IPR013130. Fe3_reduct_TM_N. IPR013121. Fe_red_NAD_bd_6. IPR002007. Haem_peroxidase_animal. IPR019791. Haem_peroxidase_animal_sg. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:1.10.640.10. Haem_peroxidase_animal. 1 hit.
Pfam	PF03098. An_peroxidase. 1 hit. PF00036. efhand. 2 hits. PF08022. FAD_binding_8. 1 hit. PF01794. Ferric_reduct. 1 hit. PF08030. NAD_binding_6. 1 hit. [Graphical view]
PRINTS	PR00457. ANPEROXIDASE.
ProDom	PD000012. EF-hand. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00054. EFh. 2 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 3 hits. PS51384. FAD_FR. 1 hit. PS50292. PEROXIDASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	56216.
SOURCE	Search...

Entry information

Entry name

DUOX1_HUMAN

Accession

Primary (citable) accession number: Q9NRD9
Secondary accession number(s): A6NH28 , Q14C94, Q6ZMB3, Q6ZR09, Q9NZC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	October 1, 2000
Last modified:	July 7, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)