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5.B.1.1.7
Thyroid NADPH oxidase/peroxidase 2 (Dual oxidase 2; Duox2) with two EF band domains, responsive to Ca2+ regulation (De Deken et al., 2000; Edens et al., 2001)

Accession Number:Q9NRD8
Protein Name:Duox2 aka Large Nox2
Length:1548
Molecular Weight:175364.00
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: Q9NRD8
eggNOG: prNOG13704
RefSeq: NP_054799.4   
Entrez Gene ID: 50506   
Pfam: PF03098    PF00036    PF08022    PF01794    PF08030   
OMIM: 606759  gene
607200  phenotype
KEGG: hsa:50506   

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:0004601 F:peroxidase activity
GO:0042335 P:cuticle development
GO:0019221 P:cytokine-mediated signaling pathway
GO:0042446 P:hormone biosynthetic process
GO:0042744 P:hydrogen peroxide catabolic process
GO:0055114 P:oxidation reduction
GO:0051591 P:response to cAMP
GO:0009615 P:response to virus

References (13)

[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] “Analysis of the DNA sequence and duplication history of human chromosome 15.”  Zody M.C.et.al.   16572171
[4] “Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs.”  Dupuy C.et.al.   10601291
[5] “Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system.”  De Deken X.et.al.   11822874
[6] “Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism.”  Moreno J.C.et.al.   12110737
[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] “Dual oxidase2 is expressed all along the digestive tract.”  Ameziane-El-Hassani R.et.al.   15591162
[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
[12] “Persistent mild hypothyroidism associated with novel sequence variants of the DUOX2 gene in two siblings.”  Vigone M.C.et.al.   16134168
[13] “Three mutations (p.Q36H, p.G418fsX482, and g.IVS19-2A-->C) in the dual oxidase 2 gene responsible for congenital goiter and iodide organification defect.”  Varela V.et.al.   16322276

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)
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FASTA formatted sequence
1:	MLRARPEALM LLGALLTGSL GPSGNQDALS LPWEVQRYDG WFNNLRHHER GAVGCRLQRR 
61:	VPANYADGVY QALEEPQLPN PRRLSNAATR GIAGLPSLHN RTVLGVFFGY HVLSDVVSVE 
121:	TPGCPAEFLN IRIPPGDPVF DPDQRGDVVL PFQRSRWDPE TGRSPSNPRD LANQVTGWLD 
181:	GSAIYGSSHS WSDALRSFSG GQLASGPDPA FPRDSQNPLL MWAAPDPATG QNGPRGLYAF 
241:	GAERGNREPF LQALGLLWFR YHNLWAQRLA RQHPDWEDEE LFQHARKRVI ATYQNIAVYE 
301:	WLPSFLQKTL PEYTGYRPFL DPSISPEFVV ASEQFFSTMV PPGVYMRNAS CHFRKVLNKG 
361:	FQSSQALRVC NNYWIRENPN LNSTQEVNEL LLGMASQISE LEDNIVVEDL RDYWPGPGKF 
421:	SRTDYVASSI QRGRDMGLPS YSQALLAFGL DIPRNWSDLN PNVDPQVLEA TAALYNQDLS 
481:	QLELLLGGLL ESHGDPGPLF SAIVLDQFVR LRDGDRYWFE NTRNGLFSKK EIEDIRNTTL 
541:	RDVLVAVINI DPSALQPNVF VWHKGAPCPQ PKQLTTDGLP QCAPLTVLDF FEGSSPGFAI 
601:	TIIALCCLPL VSLLLSGVVA YFRGREHKKL QKKLKESVKK EAAKDGVPAM EWPGPKERSS 
661:	PIIIQLLSDR CLQVLNRHLT VLRVVQLQPL QQVNLILSNN RGCRTLLLKI PKEYDLVLLF 
721:	SSEEERGAFV QQLWDFCVRW ALGLHVAEMS EKELFRKAVT KQQRERILEI FFRHLFAQVL 
781:	DINQADAGTL PLDSSQKVRE ALTCELSRAE FAESLGLKPQ DMFVESMFSL ADKDGNGYLS 
841:	FREFLDILVV FMKGSPEDKS RLMFTMYDLD ENGFLSKDEF FTMMRSFIEI SNNCLSKAQL 
901:	AEVVESMFRE SGFQDKEELT WEDFHFMLRD HDSELRFTQL CVKGGGGGGN GIRDIFKQNI 
961:	SCRVSFITRT PGERSHPQGL GPPAPEAPEL GGPGLKKRFG KKAAVPTPRL YTEALQEKMQ 
1021:	RGFLAQKLQQ YKRFVENYRR HIVCVAIFSA ICVGVFADRA YYYGFASPPS DIAQTTLVGI 
1081:	ILSRGTAASV SFMFSYILLT MCRNLITFLR ETFLNRYVPF DAAVDFHRWI AMAAVVLAIL 
1141:	HSAGHAVNVY IFSVSPLSLL ACIFPNVFVN DGSKLPQKFY WWFFQTVPGM TGVLLLLVLA 
1201:	IMYVFASHHF RRRSFRGFWL THHLYILLYA LLIIHGSYAL IQLPTFHIYF LVPAIIYGGD 
1261:	KLVSLSRKKV EISVVKAELL PSGVTYLQFQ RPQGFEYKSG QWVRIACLAL GTTEYHPFTL 
1321:	TSAPHEDTLS LHIRAVGPWT TRLREIYSSP KGNGCAGYPK LYLDGPFGEG HQEWHKFEVS 
1381:	VLVGGGIGVT PFASILKDLV FKSSLGSQML CKKIYFIWVT RTQRQFEWLA DIIQEVEEND 
1441:	HQDLVSVHIY VTQLAEKFDL RTTMLYICER HFQKVLNRSL FTGLRSITHF GRPPFEPFFN 
1501:	SLQEVHPQVR KIGVFSCGPP GMTKNVEKAC QLVNRQDRAH FMHHYENF