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Protein

Dual oxidase 1

Gene

Duox1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi828 – 839121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi864 – 875122PROSITE-ProRule annotationAdd
BLAST

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

PeroxiBasei3970. RnoDuOx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual oxidase 1 (EC:1.11.1.-, EC:1.6.3.1)
Gene namesi
Name:Duox1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628760. Duox1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 596575ExtracellularSequence analysisAdd
BLAST
Transmembranei597 – 61721HelicalSequence analysisAdd
BLAST
Topological domaini618 – 1044427CytoplasmicSequence analysisAdd
BLAST
Transmembranei1045 – 106521HelicalSequence analysisAdd
BLAST
Topological domaini1066 – 108015ExtracellularSequence analysisAdd
BLAST
Transmembranei1081 – 110121HelicalSequence analysisAdd
BLAST
Topological domaini1102 – 113635CytoplasmicSequence analysisAdd
BLAST
Transmembranei1137 – 115721HelicalSequence analysisAdd
BLAST
Topological domaini1158 – 118831ExtracellularSequence analysisAdd
BLAST
Transmembranei1189 – 120921HelicalSequence analysisAdd
BLAST
Topological domaini1210 – 122617CytoplasmicSequence analysisAdd
BLAST
Transmembranei1227 – 124721HelicalSequence analysisAdd
BLAST
Topological domaini1248 – 12481ExtracellularSequence analysis
Transmembranei1249 – 126921HelicalSequence analysisAdd
BLAST
Topological domaini1270 – 1551282CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 15511530Dual oxidase 1PRO_0000223346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence analysis
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence analysis
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence analysis
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence analysis
Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8CIY2.
PRIDEiQ8CIY2.

Expressioni

Tissue specificityi

Expressed in thyrocytes (at protein level).1 Publication

Interactioni

Subunit structurei

Interacts with TXNDC11, TPO and CYBA.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045928.

Structurei

3D structure databases

ProteinModelPortaliQ8CIY2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini815 – 85036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini851 – 88636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini895 – 93036EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini1087 – 1269183Ferric oxidoreductaseAdd
BLAST
Domaini1270 – 1376107FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 593568Peroxidase-like; mediates peroxidase activityBy similarityAdd
BLAST
Regioni956 – 1248293Interaction with TXNDC11By similarityAdd
BLAST

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.
InParanoidiQ8CIY2.
KOiK13411.
PhylomeDBiQ8CIY2.

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. 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]

Sequencei

Sequence statusi: Complete.

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

Q8CIY2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVYSAVAWI LLFGVLASLG AQNPVSWEVQ RFDGWYNNLM EHRWGSKGSR
60 70 80 90 100
LQRLVPASYA DGVYQPLREP YLPNPRHLSN RVMRGPAGQP SLRNRTVLGV
110 120 130 140 150
FFGYHVLSDL VSVETPGCPA EFLNIYIPRG DPVFDPDKRG NVVLPFQRSR
160 170 180 190 200
WDRSTGQSPS NPRDLTNQVT GWLDGSAIYG SSHSWSDTLR SFSGGQLASG
210 220 230 240 250
PDPAFPRNSQ NSLLMWMAPD PATGQGGPQG LYAFGAQRGN REPFLQALGL
260 270 280 290 300
LWFRYHNLCA KRLAQEHPHW GDEELFQHAR KRVIATYQNI AMYEWLPSFL
310 320 330 340 350
KQTPPEYPGY HPFLDPSISP EFVVASEQFL STMVPPGVYM RNASCHFQGI
360 370 380 390 400
ANRNSSVSGA LRVCNSYWSR ENPKLQRAED VDALLLGMAS QIAEREDHLV
410 420 430 440 450
VEDVQDFWPG PLKFSRTDYL ASCLQRGRDL GLPSYTKARE ALGLPPVSHW
460 470 480 490 500
QDINPALSRS NGTVLEATAA LYNQDLSRLE LLAGGLLESH GDPGPLFSAI
510 520 530 540 550
VLDQFVRLRD GDRYWFENNR NGLFSKEEIA EIRNTSLRDI LVAVTNVDPS
560 570 580 590 600
ALQPSVFFWL AGDPCPQPSQ LSTQGLPACA PLFVRDYFKG SGFGFGLTIG
610 620 630 640 650
TLCCFPLVSL LSAWIVARLR MRNFKRLQRQ DRQSIMCEKL VGGVEALEWQ
660 670 680 690 700
GRKEPCRPVL VHLQPGQIRV VDGRLTVLRT IQLRPPQQVN LILSSNRGRR
710 720 730 740 750
TLLLKIPKEY DLVLLFNMEE ERQALVENIR AALKENGLSF QEWELREQEL
760 770 780 790 800
MRAAVTRQQR GHLLETFFRH LFSQVLDINQ ADAGTLPLDS STKVREALTC
810 820 830 840 850
ELSRAEFADS LGLKPQDMFV ESMFSLADKD GNGYLSFREF LDILVVFMKG
860 870 880 890 900
SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKDQLAEVV
910 920 930 940 950
ESMFRESGFQ DKEELTWEDF HFMLRDHDSD LRFTQLCVKG VEVPEVIKNL
960 970 980 990 1000
CRRASYISQE KICPSPRMSA HCARNNTKTA SSPQRLQCPV DTDPPQEIRR
1010 1020 1030 1040 1050
RFGKKVTSFQ PLLFTEAHRE KFQRSRRHQT VQQFKRFIEN YRRHIGCVAV
1060 1070 1080 1090 1100
FYTITGALFL ERAYYYAFAA HHSGITDTTR VGIILSRGTA ASISFMFSYI
1110 1120 1130 1140 1150
LLTMCRNLIT FLRETFLNRY IPFDAAVDFH RFIASTAIIL TVLHSAGHVV
1160 1170 1180 1190 1200
NVYLFSISPL SVLSCLFPDL FHDDGSEFPQ KYYWWFFQTV PGLTGVLLLL
1210 1220 1230 1240 1250
ALAIMYVFAS HHFRRRSFRG FWLTHHLYIF LYILLIIHGS FALIQMPRFH
1260 1270 1280 1290 1300
IFFLVPAIIY VGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY
1310 1320 1330 1340 1350
KSGQWVRIAC LALGTTEYHP FTLTSAPHED TLSLHIRAAG PWTTRLREIY
1360 1370 1380 1390 1400
SPPTGDTCAR YPKLYLDGPF GEGHQEWHKF EVSVLVGAGI GVTPFASILK
1410 1420 1430 1440 1450
DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE ENDSRDLVSV
1460 1470 1480 1490 1500
HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSV THFGRPPFEP
1510 1520 1530 1540 1550
FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINKQD RTHFSHHYEN

F
Length:1,551
Mass (Da):177,197
Last modified:March 1, 2003 - v1
Checksum:i52B07F83EF4E1FE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF542180 mRNA. Translation: AAN33120.1.
RefSeqiNP_714961.1. NM_153739.1.
UniGeneiRn.162682.

Genome annotation databases

GeneIDi266807.
KEGGirno:266807.
UCSCiRGD:628760. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF542180 mRNA. Translation: AAN33120.1.
RefSeqiNP_714961.1. NM_153739.1.
UniGeneiRn.162682.

3D structure databases

ProteinModelPortaliQ8CIY2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000045928.

Protein family/group databases

PeroxiBasei3970. RnoDuOx01.

Proteomic databases

PaxDbiQ8CIY2.
PRIDEiQ8CIY2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi266807.
KEGGirno:266807.
UCSCiRGD:628760. rat.

Organism-specific databases

CTDi53905.
RGDi628760. Duox1.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
HOGENOMiHOG000231774.
HOVERGENiHBG080428.
InParanoidiQ8CIY2.
KOiK13411.
PhylomeDBiQ8CIY2.

Enzyme and pathway databases

UniPathwayiUPA00194.

Miscellaneous databases

PROiQ8CIY2.

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. 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...

Publicationsi

  1. "Identification of a truncated dual oxidase 2 (DUOX2) messenger ribonucleic acid (mRNA) in two rat thyroid cell lines. Insulin and forskolin regulation of DUOX2 mRNA levels in FRTL-5 cells and porcine thyrocytes."
    Morand S., Dos Santos O.F., Ohayon R., Kaniewski J., Noel-Hudson M.-S., Virion A., Dupuy C.
    Endocrinology 144:567-574(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344.
  2. "Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family."
    De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G., Dumont J.E., Miot F.
    J. Biol. Chem. 275:23227-23233(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiDUOX1_RAT
AccessioniPrimary (citable) accession number: Q8CIY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 91 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.