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Protein

Dual oxidase

Gene

Duox

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in innate immunity limiting microbial proliferation in the gut. May generate antimicrobial oxidative burst through its peroxidase-like domain.1 Publication

Catalytic activityi

NAD(P)H + O2 = NAD(P)+ + H2O2.1 Publication

Enzyme regulationi

Peroxidase activity is inhibited by aminotriazole and azide.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi868 – 879121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi904 – 915122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, FAD, Flavoprotein, Metal-binding, NADP

Enzyme and pathway databases

ReactomeiR-DME-209968. Thyroxine biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual oxidase (EC:1.11.1.-, EC:1.6.3.1)
Gene namesi
Name:Duox
ORF Names:CG3131
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0031464. Duox.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 626626ExtracellularSequence analysisAdd
BLAST
Transmembranei627 – 64721HelicalSequence analysisAdd
BLAST
Topological domaini648 – 1029382CytoplasmicSequence analysisAdd
BLAST
Transmembranei1030 – 105021HelicalSequence analysisAdd
BLAST
Topological domaini1051 – 106515ExtracellularSequence analysisAdd
BLAST
Transmembranei1066 – 108621HelicalSequence analysisAdd
BLAST
Topological domaini1087 – 111630CytoplasmicSequence analysisAdd
BLAST
Transmembranei1117 – 113721HelicalSequence analysisAdd
BLAST
Topological domaini1138 – 117134ExtracellularSequence analysisAdd
BLAST
Transmembranei1172 – 119221HelicalSequence analysisAdd
BLAST
Topological domaini1193 – 120210CytoplasmicSequence analysis
Transmembranei1203 – 122321HelicalSequence analysisAdd
BLAST
Topological domaini1224 – 12307ExtracellularSequence analysis
Transmembranei1231 – 125121HelicalSequence analysisAdd
BLAST
Topological domaini1252 – 1537286CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15371537Dual oxidasePRO_0000223352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence analysis
Glycosylationi577 – 5771N-linked (GlcNAc...)Sequence analysis
Glycosylationi606 – 6061N-linked (GlcNAc...)Sequence analysis
Modified residuei826 – 8261PhosphoserineBy similarity
Modified residuei1105 – 11051PhosphotyrosineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9VQH2.

Expressioni

Gene expression databases

BgeeiQ9VQH2.
ExpressionAtlasiQ9VQH2. differential.
GenevisibleiQ9VQH2. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0289611.

Structurei

3D structure databases

ProteinModelPortaliQ9VQH2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini855 – 89036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini891 – 92636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini936 – 97136EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini1078 – 1218141Ferric oxidoreductaseAdd
BLAST
Domaini1253 – 1358106FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 628566Peroxidase-like; mediates peroxidase activityBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi822 – 8254Poly-Arg

Sequence similaritiesi

In the N-terminal section; belongs to the peroxidase family.Curated
Contains 3 EF-hand domains.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
Contains 1 ferric oxidoreductase domain.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000245217.
InParanoidiQ9VQH2.
KOiK13411.
OMAiREWVHAS.
OrthoDBiEOG7966FP.
PhylomeDBiQ9VQH2.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.640.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF03098. An_peroxidase. 1 hit.
PF00036. EF-hand_1. 1 hit.
PF13499. EF-hand_7. 1 hit.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF48113. SSF48113. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS51384. FAD_FR. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VQH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVPSAPHQR AESKNRVPRP GQKNRKLPKL RLHWPGATYG GALLLLLISY
60 70 80 90 100
GLELGSVHCY EKMYSQTEKQ RYDGWYNNLA HPDWGSVDSH LVRKAPPSYS
110 120 130 140 150
DGVYAMAGAN RPSTRRLSRL FMRGKDGLGS KFNRTALLAF FGQLVANEIV
160 170 180 190 200
MASESGCPIE MHRIEIEKCD EMYDRECRGD KYIPFHRAAY DRDTGQSPNA
210 220 230 240 250
PREQINQMTA WIDGSFIYST SEAWLNAMRS FHNGTLLTEK DGKLPVRNTM
260 270 280 290 300
RVPLFNNPVP SVMKMLSPER LFLLGDPRTN QNPAILSFAI LFLRWHNTLA
310 320 330 340 350
QRIKRVHPDW SDEDIYQRAR HTVIASLQNV IVYEYLPAFL GTSLPPYEGY
360 370 380 390 400
KQDIHPGIGH IFQAAAFRFG HTMIPPGIYR RDGQCNFKET PMGYPAVRLC
410 420 430 440 450
STWWDSSGFF ADTSVEEVLM GLASQISERE DPVLCSDVRD KLFGPMEFTR
460 470 480 490 500
RDLGALNIMR GRDNGLPDYN TARESYGLKR HKTWTDINPP LFETQPELLD
510 520 530 540 550
MLKEAYDNKL DDVDVYVGGM LESYGQPGEF FTAVIKEQFQ RLRDADRFWF
560 570 580 590 600
ENERNGIFTP EEIAELRKIT LWDIIVNSTD VKEEEIQKDV FMWRTGDPCP
610 620 630 640 650
QPMQLNATEL EPCTYLEGYD YFSGSELMFI YVCVFLGFVP ILCAGAGYCV
660 670 680 690 700
VKLQNSKRRR LKIRQEALRA PQHKGSVDKM LAREWLHANH KRLVTVKFGP
710 720 730 740 750
EAAIYTVDRK GEKLRTFSLK HIDVVSVEES ATNHIKKKPY ILLRVPSDHD
760 770 780 790 800
LVLELESYGA RRKFVKKLED FLLLHKKEMT LMEVNRDIML ARAETRERRQ
810 820 830 840 850
KRLEYFFREA YALTFGLRPG ERRRRSDASS DGEVMTVMRT SLSKAEFAAA
860 870 880 890 900
LGMKPNDMFV RKMFNIVDKD QDGRISFQEF LETVVLFSRG KTDDKLRIIF
910 920 930 940 950
DMCDNDRNGV IDKGELSEMM RSLVEIARTT SLGDDQVTEL IDGMFQDVGL
960 970 980 990 1000
EHKNHLTYQD FKLMMKEYKG DFVAIGLDCK GAKQNFLDTS TNVARMTSFN
1010 1020 1030 1040 1050
IEPMQDKPRH WLLAKWDAYI TFLEENRQNI FYLFLFYVVT IVLFVERFIH
1060 1070 1080 1090 1100
YSFMAEHTDL RHIMGVGIAI TRGSAASLSF CYSLLLLTMS RNLITKLKEF
1110 1120 1130 1140 1150
PIQQYIPLDS HIQFHKIAAC TALFFSVLHT VGHIVNFYHV STQSHENLRC
1160 1170 1180 1190 1200
LTREVHFASD YKPDITFWLF QTVTGTTGVM LFIIMCIIFV FAHPTIRKKA
1210 1220 1230 1240 1250
YNFFWNMHTL YIGLYLLSLI HGLARLTGPP RFWMFFLGPG IVYTLDKIVS
1260 1270 1280 1290 1300
LRTKYMALDV IDTDLLPSDV IKIKFYRPPN LKYLSGQWVR LSCTAFRPHE
1310 1320 1330 1340 1350
MHSFTLTSAP HENFLSCHIK AQGPWTWKLR NYFDPCNYNP EDQPKIRIEG
1360 1370 1380 1390 1400
PFGGGNQDWY KFEVAVMVGG GIGVTPYASI LNDLVFGTST NRYSGVACKK
1410 1420 1430 1440 1450
VYFLWICPSH KHFEWFIDVL RDVEKKDVTN VLEIHIFITQ FFHKFDLRTT
1460 1470 1480 1490 1500
MLYICENHFQ RLSKTSIFTG LKAVNHFGRP DMSSFLKFVQ KKHSYVSKIG
1510 1520 1530
VFSCGPRPLT KSVMSACDEV NKTRKLPYFI HHFENFG
Length:1,537
Mass (Da):177,690
Last modified:March 21, 2012 - v2
Checksum:iE26329E7BFBAB34C
GO

Sequence cautioni

The sequence AAT94476.1 differs from that shown. Reason: Frameshift at position 22. Curated
The sequence AAT94476.1 differs from that shown. Reason: Erroneous termination at position 497. Translated as Glu.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF51201.2.
BT015247 mRNA. Translation: AAT94476.1. Sequence problems.
RefSeqiNP_001259968.1. NM_001273039.1.
NP_608715.2. NM_134871.3.
UniGeneiDm.11399.

Genome annotation databases

EnsemblMetazoaiFBtr0300382; FBpp0289611; FBgn0031464.
FBtr0335133; FBpp0307132; FBgn0031464.
GeneIDi33477.
KEGGidme:Dmel_CG3131.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF51201.2.
BT015247 mRNA. Translation: AAT94476.1. Sequence problems.
RefSeqiNP_001259968.1. NM_001273039.1.
NP_608715.2. NM_134871.3.
UniGeneiDm.11399.

3D structure databases

ProteinModelPortaliQ9VQH2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0289611.

Proteomic databases

PaxDbiQ9VQH2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0300382; FBpp0289611; FBgn0031464.
FBtr0335133; FBpp0307132; FBgn0031464.
GeneIDi33477.
KEGGidme:Dmel_CG3131.

Organism-specific databases

CTDi565097.
FlyBaseiFBgn0031464. Duox.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000245217.
InParanoidiQ9VQH2.
KOiK13411.
OMAiREWVHAS.
OrthoDBiEOG7966FP.
PhylomeDBiQ9VQH2.

Enzyme and pathway databases

ReactomeiR-DME-209968. Thyroxine biosynthesis.

Miscellaneous databases

GenomeRNAii33477.
NextBioi783776.
PROiQ9VQH2.

Gene expression databases

BgeeiQ9VQH2.
ExpressionAtlasiQ9VQH2. differential.
GenevisibleiQ9VQH2. DM.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.640.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR013112. FAD-bd_8.
IPR017927. Fd_Rdtase_FAD-bd.
IPR013130. Fe3_Rdtase_TM_dom.
IPR013121. Fe_red_NAD-bd_6.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF03098. An_peroxidase. 1 hit.
PF00036. EF-hand_1. 1 hit.
PF13499. EF-hand_7. 1 hit.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF48113. SSF48113. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS51384. FAD_FR. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Larva and Pupae.
  4. "A direct role for dual oxidase in Drosophila gut immunity."
    Ha E.-M., Oh C.-T., Bae Y.S., Lee W.-J.
    Science 310:847-850(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  5. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiDUOX_DROME
AccessioniPrimary (citable) accession number: Q9VQH2
Secondary accession number(s): Q6AWK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 21, 2012
Last modified: May 11, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.