Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Dual oxidase 2 (EC 1.11.1.-) (EC 1.6.3.1) (Large NOX 2) (Long NOX 2) (NADH/NADPH thyroid oxidase p138-tox) (NADPH oxidase/peroxidase DUOX2) (NADPH thyroid oxidase 2) (Thyroid oxidase 2) (p138 thyroid oxidase)

 DUOX2_HUMAN             Reviewed;        1548 AA.
Q9NRD8; A8MQ13; D2XI64; Q9NR02; Q9UHF9;
21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
22-NOV-2017, entry version 148.
RecName: Full=Dual oxidase 2;
EC=1.11.1.-;
EC=1.6.3.1;
AltName: Full=Large NOX 2;
AltName: Full=Long NOX 2;
AltName: Full=NADH/NADPH thyroid oxidase p138-tox;
AltName: Full=NADPH oxidase/peroxidase DUOX2;
AltName: Full=NADPH thyroid oxidase 2;
AltName: Full=Thyroid oxidase 2;
AltName: Full=p138 thyroid oxidase;
Flags: Precursor;
Name=DUOX2; Synonyms=LNOX2, THOX2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY, AND VARIANT
LEU-1067.
TISSUE=Thyroid;
PubMed=10806195; DOI=10.1074/jbc.M000916200;
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], VARIANTS LEU-138 AND LEU-1067,
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
TISSUE=Pancreas, and Thyroid;
PubMed=11514595; DOI=10.1083/jcb.200103132;
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 GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 339-1548, AND VARIANT LEU-1067.
TISSUE=Thyroid;
PubMed=10601291; DOI=10.1074/jbc.274.52.37265;
Dupuy C., Ohayon R., Valent A., Noel-Hudson M.-S., Deme D., Virion A.;
"Purification of a novel flavoprotein involved in the thyroid NADPH
oxidase. Cloning of the porcine and human cDNAs.";
J. Biol. Chem. 274:37265-37269(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1509-1548, VARIANT TDH6 SER-1518,
AND CHARACTERIZATION OF VARIANT TDH6 SER-1518.
PubMed=20187165; DOI=10.1002/humu.21227;
Hoste C., Rigutto S., Van Vliet G., Miot F., De Deken X.;
"Compound heterozygosity for a novel hemizygous missense mutation and
a partial deletion affecting the catalytic core of the H2O2-generating
enzyme DUOX2 associated with transient congenital hypothyroidism.";
Hum. Mutat. 31:E1304-E1319(2010).
[6]
GLYCOSYLATION.
PubMed=11822874; DOI=10.1006/excr.2001.5444;
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]
INVOLVEMENT IN TDH6.
PubMed=12110737; DOI=10.1056/NEJMoa012752;
Moreno J.C., Bikker H., Kempers M.J.E., van Trotsenburg A.S., Baas F.,
de Vijlder J.J.M., Vulsma T., Ris-Stalpers C.;
"Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and
congenital hypothyroidism.";
N. Engl. J. Med. 347:95-102(2002).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12824283; DOI=10.1096/fj.02-1104fje;
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).
[9]
TISSUE SPECIFICITY.
PubMed=15210697; DOI=10.1074/jbc.M404983200;
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).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15591162; DOI=10.1152/ajpgi.00198.2004;
Ameziane-El-Hassani R., Benfares N., Caillou B., Talbot M.,
Sabourin J.-C., Belotte V., Morand S., Gnidehou S., Agnandji D.,
Ohayon R., Kaniewski J., Noel-Hudson M.-S., Bidart J.-M.,
Schlumberger M., Virion A., Dupuy C.;
"Dual oxidase2 is expressed all along the digestive tract.";
Am. J. Physiol. 288:G933-G942(2005).
[11]
INTERACTION WITH TXNDC11; TPO AND CYBA.
PubMed=15561711; DOI=10.1074/jbc.M407709200;
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).
[12]
CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=15972824; DOI=10.1074/jbc.M500516200;
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).
[13]
VARIANT TDH6 TRP-376.
PubMed=16134168; DOI=10.1002/humu.9372;
Vigone M.C., Fugazzola L., Zamproni I., Passoni A., Di Candia S.,
Chiumello G., Persani L., Weber G.;
"Persistent mild hypothyroidism associated with novel sequence
variants of the DUOX2 gene in two siblings.";
Hum. Mutat. 26:395-395(2005).
[14]
VARIANT TDH6 HIS-36.
PubMed=16322276; DOI=10.1373/clinchem.2005.058321;
Varela V., Rivolta C.M., Esperante S.A., Gruneiro-Papendieck L.,
Chiesa A., Targovnik H.M.;
"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.";
Clin. Chem. 52:182-191(2006).
[15]
POSSIBLE INVOLVEMENT IN INFLAMMATORY BOWEL DISEASE, VARIANTS CYS-1211
AND CYS-1492, AND SUBCELLULAR LOCATION.
PubMed=26301257; DOI=10.1016/j.jcmgh.2015.06.005;
Hayes P., Dhillon S., O'Neill K., Thoeni C., Hui K.Y., Elkadri A.,
Guo C.H., Kovacic L., Aviello G., Alvarez L.A., Griffiths A.M.,
Snapper S.B., Brant S.R., Doroshow J.H., Silverberg M.S., Peter I.,
McGovern D.P., Cho J., Brumell J.H., Uhlig H.H., Bourke B.,
Muise A.A., Knaus U.G.;
"Defects in NADPH oxidase genes NOX1 and DUOX2 in very early onset
inflammatory bowel disease.";
Cell. Mol. Gastroenterol. Hepatol. 1:489-502(2015).
-!- 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.
{ECO:0000269|PubMed:12824283}.
-!- CATALYTIC ACTIVITY: NAD(P)H + O(2) = NAD(P)(+) + H(2)O(2).
{ECO:0000269|PubMed:15972824}.
-!- ENZYME REGULATION: Peroxidase activity is inhibited by
aminobenzohydrazide (By similarity). The NADPH oxidase activity is
calcium-dependent. {ECO:0000250, ECO:0000269|PubMed:15972824}.
-!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
-!- SUBUNIT: Interacts with TXNDC11, TPO and CYBA.
{ECO:0000269|PubMed:15561711}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:15591162, ECO:0000269|PubMed:26301257}; Multi-
pass membrane protein {ECO:0000269|PubMed:15591162}. Cell junction
{ECO:0000269|PubMed:26301257}. Note=Localizes to the apical
membrane of epithelial cells. Localizes on internal membrane
structures under resting conditions, translocates to the plasma
membrane and cell-cell junctions upon challenge with enteric
pathogens, such as Escherichia coli.
{ECO:0000269|PubMed:26301257}.
-!- TISSUE SPECIFICITY: Expressed in colon, small intestine, duodenum
and tracheal surface epithelial cells (at protein level).
Expressed in thyrocytes. Also detected in kidney, liver, lung,
pancreas, prostate, salivary glands, rectum and testis.
{ECO:0000269|PubMed:10806195, ECO:0000269|PubMed:11514595,
ECO:0000269|PubMed:12824283, ECO:0000269|PubMed:15210697,
ECO:0000269|PubMed:15591162}.
-!- DEVELOPMENTAL STAGE: Widely expressed in fetal tissues.
{ECO:0000269|PubMed:11514595}.
-!- INDUCTION: By forskolin, thyrotropin and the Th1-specific cytokine
IFNG/IFN-gamma. {ECO:0000269|PubMed:10806195}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:11822874}.
-!- DISEASE: Thyroid dyshormonogenesis 6 (TDH6) [MIM:607200]: A
disorder due to a defective conversion of accumulated iodide to
organically bound iodine. The iodide organification defect can be
partial or complete. {ECO:0000269|PubMed:12110737,
ECO:0000269|PubMed:16134168, ECO:0000269|PubMed:16322276,
ECO:0000269|PubMed:20187165}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Defects in DUOX2 may play a role in the pathogenesis
of very early onset inflammatory bowel disease (VEOIBD), a
chronic, relapsing inflammation of the gastrointestinal tract with
a complex etiology diagnosed before 6 years of age. VEOIBD is
subdivided into Crohn disease and ulcerative colitis phenotypes.
Crohn disease may affect any part of the gastrointestinal tract
from the mouth to the anus, but the phenotype of children with
onset of Crohn disease occurring younger than the age of 10 is
predominantly colonic, with a lower risk of ileal disease. Bowel
inflammation is transmural and discontinuous; it may contain
granulomas or be associated with intestinal or perianal fistulas.
In contrast, in ulcerative colitis, the inflammation is continuous
and limited to rectal and colonic mucosal layers; fistulas and
granulomas are not observed. Both diseases include extraintestinal
inflammation of the skin, eyes, or joints.
{ECO:0000269|PubMed:26301257}.
-!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Undiagnosed Disease Network; Note=DUOX2;
URL="https://undiagnosed.hms.harvard.edu/updates/genes-of-interest/duox2-gene/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF230496; AAF73922.1; -; mRNA.
EMBL; AF267981; AAF78954.1; -; mRNA.
EMBL; AC091117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF181972; AAF20055.1; -; mRNA.
EMBL; GU174495; ADB22378.1; -; Genomic_DNA.
CCDS; CCDS10117.1; -.
RefSeq; NP_054799.4; NM_014080.4.
UniGene; Hs.71377; -.
ProteinModelPortal; Q9NRD8; -.
IntAct; Q9NRD8; 1.
STRING; 9606.ENSP00000373691; -.
PeroxiBase; 3338; HsDuOx02.
TCDB; 5.B.1.1.7; the phagocyte (gp91(phox)) nadph oxidase family.
iPTMnet; Q9NRD8; -.
PhosphoSitePlus; Q9NRD8; -.
BioMuta; DUOX2; -.
DMDM; 296434485; -.
PaxDb; Q9NRD8; -.
PeptideAtlas; Q9NRD8; -.
PRIDE; Q9NRD8; -.
DNASU; 50506; -.
Ensembl; ENST00000603300; ENSP00000475084; ENSG00000140279.
GeneID; 50506; -.
KEGG; hsa:50506; -.
UCSC; uc010bea.4; human.
CTD; 50506; -.
DisGeNET; 50506; -.
EuPathDB; HostDB:ENSG00000140279.12; -.
GeneCards; DUOX2; -.
H-InvDB; HIX0038086; -.
HGNC; HGNC:13273; DUOX2.
MalaCards; DUOX2; -.
MIM; 606759; gene.
MIM; 607200; phenotype.
neXtProt; NX_Q9NRD8; -.
OpenTargets; ENSG00000140279; -.
Orphanet; 95716; Familial thyroid dyshormonogenesis.
Orphanet; 226316; Genetic transient congenital hypothyroidism.
PharmGKB; PA27517; -.
eggNOG; KOG0039; Eukaryota.
eggNOG; ENOG410XNZY; LUCA.
GeneTree; ENSGT00550000074350; -.
HOGENOM; HOG000231774; -.
HOVERGEN; HBG080428; -.
InParanoid; Q9NRD8; -.
KO; K13411; -.
OrthoDB; EOG091G00PO; -.
PhylomeDB; Q9NRD8; -.
TreeFam; TF105424; -.
BRENDA; 1.6.3.1; 2681.
Reactome; R-HSA-209968; Thyroxine biosynthesis.
SABIO-RK; Q9NRD8; -.
UniPathway; UPA00194; -.
ChiTaRS; DUOX2; human.
GeneWiki; Dual_oxidase_2; -.
GenomeRNAi; 50506; -.
PRO; PR:Q9NRD8; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140279; -.
CleanEx; HS_DUOX2; -.
ExpressionAtlas; Q9NRD8; baseline and differential.
Genevisible; Q9NRD8; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0016174; F:NAD(P)H oxidase activity; IDA:UniProtKB.
GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
GO; GO:0048855; P:adenohypophysis morphogenesis; IEA:Ensembl.
GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
GO; GO:0042335; P:cuticle development; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0009566; P:fertilization; IEA:Ensembl.
GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:InterPro.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0055114; P:oxidation-reduction process; TAS:UniProtKB.
GO; GO:0051591; P:response to cAMP; IDA:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
GO; GO:0006590; P:thyroid hormone generation; TAS:Reactome.
CDD; cd09820; dual_peroxidase_like; 1.
CDD; cd00051; EFh; 2.
Gene3D; 1.10.640.10; -; 1.
InterPro; IPR034818; DUOX2.
InterPro; IPR034821; DUOX_peroxidase.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR013112; FAD-bd_8.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR013130; Fe3_Rdtase_TM_dom.
InterPro; IPR013121; Fe_red_NAD-bd_6.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
InterPro; IPR037120; Haem_peroxidase_sf.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
PANTHER; PTHR11972:SF67; PTHR11972:SF67; 1.
Pfam; PF03098; An_peroxidase; 1.
Pfam; PF00036; EF-hand_1; 1.
Pfam; PF08022; FAD_binding_8; 1.
Pfam; PF01794; Ferric_reduct; 1.
Pfam; PF08030; NAD_binding_6; 1.
PRINTS; PR00457; ANPEROXIDASE.
SMART; SM00054; EFh; 2.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF48113; SSF48113; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 3.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50292; PEROXIDASE_3; 1.
1: Evidence at protein level;
Calcium; Cell junction; Cell membrane; Complete proteome;
Congenital hypothyroidism; Disease mutation; FAD; Flavoprotein;
Glycoprotein; Hydrogen peroxide; Membrane; Metal-binding; NADP;
Oxidoreductase; Peroxidase; Polymorphism; Reference proteome; Repeat;
Signal; Thyroid hormones biosynthesis; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1548 Dual oxidase 2.
/FTId=PRO_0000223349.
TOPO_DOM 26 601 Extracellular. {ECO:0000255}.
TRANSMEM 602 622 Helical. {ECO:0000255}.
TOPO_DOM 623 1041 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1042 1062 Helical. {ECO:0000255}.
TOPO_DOM 1063 1076 Extracellular. {ECO:0000255}.
TRANSMEM 1077 1097 Helical. {ECO:0000255}.
TOPO_DOM 1098 1148 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1149 1169 Helical. {ECO:0000255}.
TOPO_DOM 1170 1185 Extracellular. {ECO:0000255}.
TRANSMEM 1186 1206 Helical. {ECO:0000255}.
TOPO_DOM 1207 1223 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1224 1244 Helical. {ECO:0000255}.
TRANSMEM 1245 1265 Helical. {ECO:0000255}.
TOPO_DOM 1266 1548 Cytoplasmic. {ECO:0000255}.
DOMAIN 819 854 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 855 890 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 899 934 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 1084 1266 Ferric oxidoreductase.
DOMAIN 1267 1373 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
CA_BIND 832 843 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 868 879 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
REGION 30 596 Peroxidase-like; mediates peroxidase
activity. {ECO:0000250}.
REGION 960 1245 Interaction with TXNDC11. {ECO:0000250}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 455 455 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 537 537 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 36 36 Q -> H (in TDH6).
{ECO:0000269|PubMed:16322276}.
/FTId=VAR_025323.
VARIANT 138 138 P -> L (in dbSNP:rs2001616).
{ECO:0000269|PubMed:11514595}.
/FTId=VAR_025324.
VARIANT 376 376 R -> W (in TDH6; dbSNP:rs119472029).
{ECO:0000269|PubMed:16134168}.
/FTId=VAR_025325.
VARIANT 678 678 H -> R (in dbSNP:rs57659670).
/FTId=VAR_061177.
VARIANT 1067 1067 S -> L (in dbSNP:rs269868).
{ECO:0000269|PubMed:10601291,
ECO:0000269|PubMed:10806195,
ECO:0000269|PubMed:11514595}.
/FTId=VAR_047075.
VARIANT 1211 1211 R -> C (found in a patient with very
early onset inflammatory bowel disease;
unknown pathological significance; no
effect on subcellular location;
significantly reduced ROS generation,
which may decrease resistance to
infection by enteric pathogens, such as
Escherichia coli; dbSNP:rs747720952).
{ECO:0000269|PubMed:26301257}.
/FTId=VAR_075549.
VARIANT 1492 1492 R -> C (found in a patient with very
early onset inflammatory bowel disease;
unknown pathological significance; no
effect on subcellular location;
significantly reduced ROS generation,
which may decrease resistance to
infection by enteric pathogens, such as
Escherichia coli; dbSNP:rs374410986).
{ECO:0000269|PubMed:26301257}.
/FTId=VAR_075550.
VARIANT 1518 1518 G -> S (in TDH6; the enzyme is non-
functional; expressed at the cell surface
of cells albeit at low level;
dbSNP:rs368512412).
{ECO:0000269|PubMed:20187165}.
/FTId=VAR_064619.
CONFLICT 25 25 N -> S (in Ref. 1; AAF73922 and 2;
AAF78954). {ECO:0000305}.
CONFLICT 984 984 A -> V (in Ref. 2; AAF78954).
{ECO:0000305}.
SEQUENCE 1548 AA; 175364 MW; 7BAA2350EC0A2A7E CRC64;
MLRARPEALM LLGALLTGSL GPSGNQDALS LPWEVQRYDG WFNNLRHHER GAVGCRLQRR
VPANYADGVY QALEEPQLPN PRRLSNAATR GIAGLPSLHN RTVLGVFFGY HVLSDVVSVE
TPGCPAEFLN IRIPPGDPVF DPDQRGDVVL PFQRSRWDPE TGRSPSNPRD LANQVTGWLD
GSAIYGSSHS WSDALRSFSG GQLASGPDPA FPRDSQNPLL MWAAPDPATG QNGPRGLYAF
GAERGNREPF LQALGLLWFR YHNLWAQRLA RQHPDWEDEE LFQHARKRVI ATYQNIAVYE
WLPSFLQKTL PEYTGYRPFL DPSISPEFVV ASEQFFSTMV PPGVYMRNAS CHFRKVLNKG
FQSSQALRVC NNYWIRENPN LNSTQEVNEL LLGMASQISE LEDNIVVEDL RDYWPGPGKF
SRTDYVASSI QRGRDMGLPS YSQALLAFGL DIPRNWSDLN PNVDPQVLEA TAALYNQDLS
QLELLLGGLL ESHGDPGPLF SAIVLDQFVR LRDGDRYWFE NTRNGLFSKK EIEDIRNTTL
RDVLVAVINI DPSALQPNVF VWHKGAPCPQ PKQLTTDGLP QCAPLTVLDF FEGSSPGFAI
TIIALCCLPL VSLLLSGVVA YFRGREHKKL QKKLKESVKK EAAKDGVPAM EWPGPKERSS
PIIIQLLSDR CLQVLNRHLT VLRVVQLQPL QQVNLILSNN RGCRTLLLKI PKEYDLVLLF
SSEEERGAFV QQLWDFCVRW ALGLHVAEMS EKELFRKAVT KQQRERILEI FFRHLFAQVL
DINQADAGTL PLDSSQKVRE ALTCELSRAE FAESLGLKPQ DMFVESMFSL ADKDGNGYLS
FREFLDILVV FMKGSPEDKS RLMFTMYDLD ENGFLSKDEF FTMMRSFIEI SNNCLSKAQL
AEVVESMFRE SGFQDKEELT WEDFHFMLRD HDSELRFTQL CVKGGGGGGN GIRDIFKQNI
SCRVSFITRT PGERSHPQGL GPPAPEAPEL GGPGLKKRFG KKAAVPTPRL YTEALQEKMQ
RGFLAQKLQQ YKRFVENYRR HIVCVAIFSA ICVGVFADRA YYYGFASPPS DIAQTTLVGI
ILSRGTAASV SFMFSYILLT MCRNLITFLR ETFLNRYVPF DAAVDFHRWI AMAAVVLAIL
HSAGHAVNVY IFSVSPLSLL ACIFPNVFVN DGSKLPQKFY WWFFQTVPGM TGVLLLLVLA
IMYVFASHHF RRRSFRGFWL THHLYILLYA LLIIHGSYAL IQLPTFHIYF LVPAIIYGGD
KLVSLSRKKV EISVVKAELL PSGVTYLQFQ RPQGFEYKSG QWVRIACLAL GTTEYHPFTL
TSAPHEDTLS LHIRAVGPWT TRLREIYSSP KGNGCAGYPK LYLDGPFGEG HQEWHKFEVS
VLVGGGIGVT PFASILKDLV FKSSLGSQML CKKIYFIWVT RTQRQFEWLA DIIQEVEEND
HQDLVSVHIY VTQLAEKFDL RTTMLYICER HFQKVLNRSL FTGLRSITHF GRPPFEPFFN
SLQEVHPQVR KIGVFSCGPP GMTKNVEKAC QLVNRQDRAH FMHHYENF


Related products :

Catalog number Product name Quantity
EIAAB12031 Dual oxidase 2,DUOX2,Homo sapiens,Human,Large NOX 2,LNOX2,Long NOX 2,NADH_NADPH thyroid oxidase p138-tox,NADPH oxidase_peroxidase DUOX2,NADPH thyroid oxidase 2,p138 thyroid oxidase,THOX2,Thyroid oxida
EIAAB12028 Dual oxidase 1,DUOX,DUOX1,Homo sapiens,Human,Large NOX 1,LNOX1,Long NOX 1,NADPH thyroid oxidase 1,THOX1,Thyroid oxidase 1
EIAAB12033 Dual oxidase 2,Duox2,Large NOX 2,Lnox2,Long NOX 2,NADH_NADPH thyroid oxidase THOX2,Rat,Rattus norvegicus,Thox2,Thyroid oxidase 2
EIAAB12032 Dual oxidase 2,DUOX2,NADH_NADPH thyroid oxidase p138-tox,Pig,Sus scrofa
EIAAB12030 Canis familiaris,Canis lupus familiaris,Dog,Dual oxidase 1,DUOX1,NADPH thyroid oxidase 1,THOX1,Thyroid oxidase 1
EIAAB27575 Kidney oxidase-1,Kidney superoxide-producing NADPH oxidase,KOX-1,Mouse,Mus musculus,NADPH oxidase 4,Nox4,Renal NAD(P)H-oxidase,Renox,Superoxide-generating NADPH oxidase 4
EIAAB27574 Homo sapiens,Human,Kidney oxidase-1,Kidney superoxide-producing NADPH oxidase,KOX-1,NADPH oxidase 4,NOX4,Renal NAD(P)H-oxidase,RENOX
EIAAB27573 Kidney oxidase-1,Kidney superoxide-producing NADPH oxidase,Kox,KOX-1,NADPH oxidase 4,Nox4,Rat,Rattus norvegicus
EIAAB26522 67 kDa neutrophil oxidase factor,Homo sapiens,Human,NADPH oxidase activator 2,NCF2,NCF-2,Neutrophil cytosol factor 2,Neutrophil NADPH oxidase factor 2,NOXA2,P67PHOX,p67-phox
EIAAB26524 67 kDa neutrophil oxidase factor,Mouse,Mus musculus,NADPH oxidase activator 2,Ncf2,NCF-2,Neutrophil cytosol factor 2,Neutrophil NADPH oxidase factor 2,Noxa2,P67phox,p67-phox
EIAAB27568 Homo sapiens,Human,Mitogenic oxidase 1,MOX1,MOX-1,NADH_NADPH mitogenic oxidase subunit P65-MOX,NADPH oxidase 1,NOH1,NOH-1,NOX1,NOX-1
EIAAB27569 Mitogenic oxidase 1,Mox1,MOX-1,NADH_NADPH mitogenic oxidase subunit P65-MOX,NADPH oxidase 1,Noh1,NOH-1,Nox1,NOX-1,Rat,Rattus norvegicus
EIAAB27582 Homo sapiens,Human,NADPH oxidase organizer 1,NADPH oxidase regulatory protein,Nox organizer 1,NOXO1,Nox-organizing protein 1,P41NOX,SH3 and PX domain-containing protein 5,SH3PXD5
EIAAB27571 GP91-3,gp91phox homolog 3,Homo sapiens,Human,Mitogenic oxidase 2,MOX2,MOX-2,NADPH oxidase 3,NOX3
LF-PA40831 anti-NADPH Oxidase Organizer 1 (NOXO1) , Rabbit polyclonal to NADPH Oxidase Organizer 1 (NOXO1) , Isotype IgG, Host Rabbit 50 ug
LF-PA40830 anti-NADPH Oxidase Organizer 1 (NOXO1) , Goat polyclonal to NADPH Oxidase Organizer 1 (NOXO1) , Isotype IgG, Host Goat 100
AB000503 NADPH Oxidase Landscape (Large Format PEP) 1pk
EIAAB39256 Bos taurus,Bovine,L-pipecolate oxidase,L-pipecolic acid oxidase,Peroxisomal sarcosine oxidase,PIPOX,PSO
EIAAB39255 L-pipecolate oxidase,L-pipecolic acid oxidase,Mouse,Mus musculus,Peroxisomal sarcosine oxidase,Pipox,PSO,Pso
EIAAB39254 L-pipecolate oxidase,L-pipecolic acid oxidase,Oryctolagus cuniculus,Peroxisomal sarcosine oxidase,PIPOX,PSO,PSO,Rabbit,SOX
EIAAB39257 Homo sapiens,Human,L-pipecolate oxidase,L-pipecolic acid oxidase,LPIPOX,Peroxisomal sarcosine oxidase,PIPOX,PSO,PSO
EIAAB26517 47 kDa autosomal chronic granulomatous disease protein,47 kDa neutrophil oxidase factor,Homo sapiens,Human,NCF1,NCF-1,NCF-47K,Neutrophil cytosol factor 1,Neutrophil NADPH oxidase factor 1,Nox organize
EIAAB26518 47 kDa neutrophil oxidase factor,Mouse,Mus musculus,Ncf1,NCF-1,NCF-47K,Neutrophil cytosol factor 1,Neutrophil NADPH oxidase factor 1,p47-phox
EIAAB26516 47 kDa neutrophil oxidase factor,Bos taurus,Bovine,NCF1,NCF-1,NCF-47K,Neutrophil cytosol factor 1,Neutrophil NADPH oxidase factor 1,p47-phox
EIAAB26521 67 kDa neutrophil oxidase factor,Bos taurus,Bovine,NCF2,NCF-2,Neutrophil cytosol factor 2,Neutrophil NADPH oxidase factor 2,p67-phox


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur