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Protein

Dual oxidase 2

Gene

Duox2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.

Catalytic activityi

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

Enzyme regulationi

The NADPH oxidase activity is calcium-dependent. Peroxidase activity is inhibited by aminobenzohydrazide (By similarity).By similarity

Pathwayi: thyroid hormone biosynthesis

This protein is involved in the pathway thyroid hormone biosynthesis, which is part of Hormone biosynthesis.
View all proteins of this organism that are known to be involved in the pathway thyroid hormone biosynthesis and in Hormone biosynthesis.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi832 – 8431PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi868 – 8792PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide, Thyroid hormones biosynthesis

Keywords - Ligandi

Calcium, FAD, Flavoprotein, Metal-binding, NADP

Enzyme and pathway databases

UniPathwayiUPA00194.

Protein family/group databases

PeroxiBasei3971. RnoDuOx02-B.
3972. RnoDuOx02-A.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual oxidase 2 (EC:1.11.1.-, EC:1.6.3.1)
Alternative name(s):
Large NOX 2
Long NOX 2
NADH/NADPH thyroid oxidase THOX2
Thyroid oxidase 2
Gene namesi
Name:Duox2
Synonyms:Lnox2, Thox2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628761. Duox2.

Subcellular locationi

  • Apical cell membrane By similarity; Multi-pass membrane protein By similarity
  • Cell junction By similarity

  • 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.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 599ExtracellularSequence analysisAdd BLAST574
Transmembranei600 – 620HelicalSequence analysisAdd BLAST21
Topological domaini621 – 1010CytoplasmicSequence analysisAdd BLAST390
Transmembranei1011 – 1031HelicalSequence analysisAdd BLAST21
Topological domaini1032 – 1046ExtracellularSequence analysisAdd BLAST15
Transmembranei1047 – 1067HelicalSequence analysisAdd BLAST21
Topological domaini1068 – 1100CytoplasmicSequence analysisAdd BLAST33
Transmembranei1101 – 1121HelicalSequence analysisAdd BLAST21
Topological domaini1122 – 1154ExtracellularSequence analysisAdd BLAST33
Transmembranei1155 – 1175HelicalSequence analysisAdd BLAST21
Topological domaini1176 – 1185CytoplasmicSequence analysis10
Transmembranei1186 – 1206HelicalSequence analysisAdd BLAST21
Topological domaini1207ExtracellularSequence analysis1
Transmembranei1208 – 1228HelicalSequence analysisAdd BLAST21
Topological domaini1229 – 1517CytoplasmicSequence analysisAdd BLAST289

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000022335126 – 1517Dual oxidase 2Add BLAST1492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi100N-linked (GlcNAc...)Sequence analysis1
Glycosylationi348N-linked (GlcNAc...)Sequence analysis1
Glycosylationi455N-linked (GlcNAc...)Sequence analysis1
Glycosylationi537N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9ES45.
PRIDEiQ9ES45.

PTM databases

iPTMnetiQ9ES45.
PhosphoSitePlusiQ9ES45.

Expressioni

Tissue specificityi

Expressed in colon, duodenum, rectum and thyroid.2 Publications

Inductioni

By forskolin, thyrotropin and insulin. Down-regulated by the antithyroid drug methimazole.2 Publications

Interactioni

Subunit structurei

Interacts with TXNDC11, TPO and CYBA.By similarity

Protein-protein interaction databases

MINTiMINT-4998237.
STRINGi10116.ENSRNOP00000023939.

Structurei

3D structure databases

ProteinModelPortaliQ9ES45.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini819 – 854EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini855 – 890EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini899 – 934EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini1053 – 1235Ferric oxidoreductaseAdd BLAST183
Domaini1236 – 1342FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST107

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 596Peroxidase-like; mediates peroxidase activityBy similarityAdd BLAST567
Regioni960 – 1214Interaction with TXNDC11By similarityAdd BLAST255

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, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
HOGENOMiHOG000231774.
HOVERGENiHBG080428.
InParanoidiQ9ES45.
KOiK13411.
PhylomeDBiQ9ES45.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 1 hit.
1.10.640.10. 1 hit.
InterProiIPR029595. DUOX1.
IPR011992. 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]
PANTHERiPTHR11972:SF67. PTHR11972:SF67. 2 hits.
PfamiPF03098. An_peroxidase. 1 hit.
PF00036. EF-hand_1. 2 hits.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00054. EFh. 2 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ES45-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLPTSLKTLV LLGALLTGPL GPAGGQDAPS LPREVQRYDG WFNNLKYHQR
60 70 80 90 100
GAAGSQLRRL VPANYADGVY QALQEPLLPN ARLLSDAVSK GKAGLPSAHN
110 120 130 140 150
RTVLGLFFGY HVLSDLVSVE TPGCPAEFLN IYIPRGDPVF DPDKRGNVVL
160 170 180 190 200
PFQRSRWDRS TGQSPSNPRD LTNQVTGWLD GSAIYGSSHS WSDTLRSFSG
210 220 230 240 250
GQLASGPDPA FPRNSQNSLL MWMAPDPATG QGGPQGLYAF GAQRGNREPF
260 270 280 290 300
LQALGLLWFR YHNLCAKRLA QEHPHWGDEE LFQHARKRVI ATYQNIALYQ
310 320 330 340 350
WLPSFLQKTP PEYSGYRPFM DPSISPEFVA ASEQFLSTMV PPGVYMRNSS
360 370 380 390 400
CHFREFPKEG SSSSPALRVC NNYWIRENPS LKTAQDVDQL LLGMASQISE
410 420 430 440 450
LEDRIVIEDL RDYWPGPDRY SRTDYVASSI QSGRDMGLPS YSQALQALGL
460 470 480 490 500
EPPKNWSALN PKVDPQVLEA TAALYNQDLS RLELFLGGLL ESHGDPGPLF
510 520 530 540 550
SNIILDQFVR LRDGDRYWFE NTRNGLFSKE EIAEIRNTTL RDVLVAVSNV
560 570 580 590 600
DPSALQPNVF FWQEGAPCPQ PQQLTTEGLP QCVPVTVIDY FEGSGAGYGV
610 620 630 640 650
TLLAVCCFPV VSLIIAWVVA RFRNRERKML LKKGKESLKK QTASDGVPAM
660 670 680 690 700
EWPGPKESSY PVTVQLLPDR SLKVLDKRLT VLRTIQLQPT QQVNLILSSS
710 720 730 740 750
HGRRTLLLKI PKEYDLVLMF NSEEDRDAFV QLLQDLCVCS TPGLRIAEMD
760 770 780 790 800
EKELLRKAVT KQQRAGILEI FFRQLFAQVL DINQADAGTL PLDSSQQVRE
810 820 830 840 850
ALTCELSRAE FADSLGLKPQ DMFVESMFSL ADKDGNGYIS FREFLDILVV
860 870 880 890 900
FMKGSPQDKS RLMFTMYDLD GNGFLSKEEF FTMMRSFIEI SNNCLSKDQL
910 920 930 940 950
AEVVESMFRE SGFQDKEELT WEDFHFMLRD HDSDLRFTQL CVKGGAGGTG
960 970 980 990 1000
DIFKQSNACR VSFLTRTPGN RVMAPSPRLY TEALQEKMQR GFLAQKLKQF
1010 1020 1030 1040 1050
KRFVENYRRH IVCVTIFSAI CAGLFADRAY YYGFASPPTD IEETTYVGII
1060 1070 1080 1090 1100
LSRGTAASIS FMFSYILLTM CRNLITFLRE TFLNRYIPFD AAVDFHRWIA
1110 1120 1130 1140 1150
MAAVVLAVVH SLGHAVNVYI FSVSPLSLMT CVFPSVFVND GSKLPPKYYW
1160 1170 1180 1190 1200
WFFETVPGMT GVLLLLVLAI MYVFASHHFR RHSFRGFWLT HHLYVVLYAL
1210 1220 1230 1240 1250
IIIHGSYALI QLPSFHIYFL VPAIIYVGDK LVSLSRKKVE ISVVKVELLP
1260 1270 1280 1290 1300
SGVTYLQFQR PKTFEYKSGQ WVRIACLSLG TNEYHPFTLT SAPHEDTLSL
1310 1320 1330 1340 1350
HIRAVGPWTT RLREIYSPPV GGTSARYPKL YLDGPFGEGH QEWHKFEVSV
1360 1370 1380 1390 1400
LVGGGIGVTP FASILKDLVF KSSMGTQMLC KKIYFIWVTR TQRQFEWLAD
1410 1420 1430 1440 1450
IIREVEENGS RDLVSVHIYI TQLAEKFDLR TTMLYICERH FQKVLNRSLF
1460 1470 1480 1490 1500
TGLRSVTHFG RPPFELFLDS LQEVHPQVHK IGVFSCGPPG MTKNVEKACQ
1510
LINRQDRAHF VHHYENF
Length:1,517
Mass (Da):171,558
Last modified:March 1, 2001 - v1
Checksum:i07FBA427DEA299D1
GO
Isoform 2 (identifier: Q9ES45-2) [UniParc]FASTAAdd to basket
Also known as: short

The sequence of this isoform differs from the canonical sequence as follows:
     1-1061: Missing.

Note: There is no evidence for the expression of the corresponding protein in vitro.
Show »
Length:456
Mass (Da):52,576
Checksum:iB39E79E45F2DF3FE
GO

Sequence cautioni

The sequence AAN39340 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1243V → A in AAN39340 (PubMed:12538618).Curated1
Sequence conflicti1246V → A in AAN39340 (PubMed:12538618).Curated1
Sequence conflicti1409G → D in AAN39340 (PubMed:12538618).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0172641 – 1061Missing in isoform 2. 1 PublicationAdd BLAST1061

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237962 mRNA. Translation: AAG21895.1.
AF547268 mRNA. Translation: AAN39340.1. Different initiation.
RefSeqiNP_077055.1. NM_024141.1. [Q9ES45-1]
UniGeneiRn.55542.

Genome annotation databases

GeneIDi79107.
KEGGirno:79107.
UCSCiRGD:628761. rat. [Q9ES45-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237962 mRNA. Translation: AAG21895.1.
AF547268 mRNA. Translation: AAN39340.1. Different initiation.
RefSeqiNP_077055.1. NM_024141.1. [Q9ES45-1]
UniGeneiRn.55542.

3D structure databases

ProteinModelPortaliQ9ES45.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4998237.
STRINGi10116.ENSRNOP00000023939.

Protein family/group databases

PeroxiBasei3971. RnoDuOx02-B.
3972. RnoDuOx02-A.

PTM databases

iPTMnetiQ9ES45.
PhosphoSitePlusiQ9ES45.

Proteomic databases

PaxDbiQ9ES45.
PRIDEiQ9ES45.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi79107.
KEGGirno:79107.
UCSCiRGD:628761. rat. [Q9ES45-1]

Organism-specific databases

CTDi50506.
RGDi628761. Duox2.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
HOGENOMiHOG000231774.
HOVERGENiHBG080428.
InParanoidiQ9ES45.
KOiK13411.
PhylomeDBiQ9ES45.

Enzyme and pathway databases

UniPathwayiUPA00194.

Miscellaneous databases

PROiQ9ES45.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 1 hit.
1.10.640.10. 1 hit.
InterProiIPR029595. DUOX1.
IPR011992. 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]
PANTHERiPTHR11972:SF67. PTHR11972:SF67. 2 hits.
PfamiPF03098. An_peroxidase. 1 hit.
PF00036. EF-hand_1. 2 hits.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00054. EFh. 2 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...

Entry informationi

Entry nameiDUOX2_RAT
AccessioniPrimary (citable) accession number: Q9ES45
Secondary accession number(s): Q811Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.