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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 | electron |
Cross database links:
RefSeq: | NP_054799.4 |
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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
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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
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External Searches:
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Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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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