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5.B.1.1.6
Thyroid NADPH oxidase/peroxidase 1 (Dual oxidase 1; Duox1) with two EF band domains, responsive to Ca2+ regulation (De Deken et al., 2000; Edens et al., 2001)

Accession Number:Q9NRD9
Protein Name:Duox1 aka Large Nox1
Length:1551
Molecular Weight:177235.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Apical cell membrane1 / Multi-pass membrane protein2
Substrate Electrons

Cross database links:

Genevestigator: Q9NRD9
eggNOG: prNOG08405
HEGENOM: HBG357816
RefSeq: NP_059130.2    NP_787954.1   
Entrez Gene ID: 53905   
Pfam: PF03098    PF00036    PF08022    PF01794    PF08030   
OMIM: 606758  gene
KEGG: hsa:53905   

Gene Ontology

GO:0016324 C:apical plasma membrane
GO:0016021 C:integral to membrane
GO:0005509 F:calcium ion binding
GO:0009055 F:electron carrier activity
GO:0050660 F:FAD binding
GO:0020037 F:heme binding
GO:0016174 F:NAD(P)H oxidase activity
GO:0050661 F:NADP or NADPH binding
GO:0004601 F:peroxidase activity
GO:0042335 P:cuticle development
GO:0019221 P:cytokine-mediated signaling pathway
GO:0042446 P:hormone biosynthetic process
GO:0050665 P:hydrogen peroxide biosynthetic process
GO:0042744 P:hydrogen peroxide catabolic process
GO:0055114 P:oxidation reduction
GO:0051591 P:response to cAMP
GO:0042554 P:superoxide anion generation

References (11)

[1] “Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family.”  De Deken X.et.al.   10806195
[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.et.al.   11514595
[3] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[4] “Analysis of the DNA sequence and duplication history of human chromosome 15.”  Zody M.C.et.al.   16572171
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system.”  De Deken X.et.al.   11822874
[7] “Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense.”  Geiszt M.et.al.   12824283
[8] “NADPH oxidase-dependent acid production in airway epithelial cells.”  Schwarzer C.et.al.   15210697
[9] “Differential regulation of dual NADPH oxidases/peroxidases, Duox1 and Duox2, by Th1 and Th2 cytokines in respiratory tract epithelium.”  Harper R.W.et.al.   16111680
[10] “Identification of a novel partner of duox: EFP1, a thioredoxin-related protein.”  Wang D.et.al.   15561711
[11] “Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity.”  Ameziane-El-Hassani R.et.al.   15972824

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
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FASTA formatted sequence
1:	MGFCLALAWT LLVGAWTPLG AQNPISWEVQ RFDGWYNNLM EHRWGSKGSR LQRLVPASYA 
61:	DGVYQPLGEP HLPNPRDLSN TISRGPAGLA SLRNRTVLGV FFGYHVLSDL VSVETPGCPA 
121:	EFLNIRIPPG DPMFDPDQRG DVVLPFQRSR WDPETGRSPS NPRDPANQVT GWLDGSAIYG 
181:	SSHSWSDALR SFSRGQLASG PDPAFPRDSQ NPLLMWAAPD PATGQNGPRG LYAFGAERGN 
241:	REPFLQALGL LWFRYHNLWA QRLARQHPDW EDEELFQHAR KRVIATYQNI AVYEWLPSFL 
301:	QKTLPEYTGY RPFLDPSISS EFVAASEQFL STMVPPGVYM RNASCHFQGV INRNSSVSRA 
361:	LRVCNSYWSR EHPSLQSAED VDALLLGMAS QIAEREDHVL VEDVRDFWPG PLKFSRTDHL 
421:	ASCLQRGRDL GLPSYTKARA ALGLSPITRW QDINPALSRS NDTVLEATAA LYNQDLSWLE 
481:	LLPGGLLESH RDPGPLFSTI VLEQFVRLRD GDRYWFENTR NGLFSKKEIE EIRNTTLQDV 
541:	LVAVINIDPS ALQPNVFVWH KGDPCPQPRQ LSTEGLPACA PSVVRDYFEG SGFGFGVTIG 
601:	TLCCFPLVSL LSAWIVARLR MRNFKRLQGQ DRQSIVSEKL VGGMEALEWQ GHKEPCRPVL 
661:	VYLQPGQIRV VDGRLTVLRT IQLQPPQKVN FVLSSNRGRR TLLLKIPKEY DLVLLFNLEE 
721:	ERQALVENLR GALKESGLSI QEWELREQEL MRAAVTREQR RHLLETFFRH LFSQVLDINQ 
781:	ADAGTLPLDS SQKVREALTC ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF 
841:	LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLAEVV 
901:	ESMFRESGFQ DKEELTWEDF HFMLRDHNSE LRFTQLCVKG VEVPEVIKDL CRRASYISQD 
961:	MICPSPRVSA RCSRSDIETE LTPQRLQCPM DTDPPQEIRR RFGKKVTSFQ PLLFTEAHRE 
1021:	KFQRSCLHQT VQQFKRFIEN YRRHIGCVAV FYAIAGGLFL ERAYYYAFAA HHTGITDTTR 
1081:	VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY VPFDAAVDFH RLIASTAIVL 
1141:	TVLHSVGHVV NVYLFSISPL SVLSCLFPGL FHDDGSELPQ KYYWWFFQTV PGLTGVVLLL 
1201:	ILAIMYVFAS HHFRRRSFRG FWLTHHLYIL LYVLLIIHGS FALIQLPRFH IFFLVPAIIY 
1261:	GGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY KSGQWVRIAC LALGTTEYHP 
1321:	FTLTSAPHED TLSLHIRAAG PWTTRLREIY SAPTGDRCAR YPKLYLDGPF GEGHQEWHKF 
1381:	EVSVLVGGGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE 
1441:	ENDHQDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSI THFGRPPFEP 
1501:	FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINRQD RTHFSHHYEN F