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Protein

Dual oxidase 1

Gene

DUOX1

Organism
Sus scrofa (Pig)
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 bindingi828 – 8391PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi864 – 8752PROSITE-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

PeroxiBasei3348. SscDuOx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual oxidase 1 (EC:1.11.1.-, EC:1.6.3.1)
Gene namesi
Name:DUOX1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 596ExtracellularSequence analysisAdd BLAST575
Transmembranei597 – 617HelicalSequence analysisAdd BLAST21
Topological domaini618 – 1046CytoplasmicSequence analysisAdd BLAST429
Transmembranei1047 – 1067HelicalSequence analysisAdd BLAST21
Topological domaini1068 – 1082ExtracellularSequence analysisAdd BLAST15
Transmembranei1083 – 1103HelicalSequence analysisAdd BLAST21
Topological domaini1104 – 1138CytoplasmicSequence analysisAdd BLAST35
Transmembranei1139 – 1159HelicalSequence analysisAdd BLAST21
Topological domaini1160 – 1190ExtracellularSequence analysisAdd BLAST31
Transmembranei1191 – 1211HelicalSequence analysisAdd BLAST21
Topological domaini1212 – 1228CytoplasmicSequence analysisAdd BLAST17
Transmembranei1229 – 1249HelicalSequence analysisAdd BLAST21
Topological domaini1250ExtracellularSequence analysis1
Transmembranei1251 – 1271HelicalSequence analysisAdd BLAST21
Topological domaini1272 – 1553CytoplasmicSequence analysisAdd BLAST282

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000022334522 – 1553Dual oxidase 1Add BLAST1532

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Glycosylationi342N-linked (GlcNAc...)Sequence analysis1
Glycosylationi354N-linked (GlcNAc...)Sequence analysis1
Glycosylationi534N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8HZK3.
PRIDEiQ8HZK3.

Expressioni

Tissue specificityi

Specifically expressed in thyroid.1 Publication

Interactioni

Subunit structurei

Interacts with TXNDC11, TPO and CYBA.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000005035.

Structurei

3D structure databases

ProteinModelPortaliQ8HZK3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini815 – 850EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini851 – 886EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini895 – 930EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini1089 – 1271Ferric oxidoreductaseAdd BLAST183
Domaini1272 – 1378FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST107

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 593Peroxidase-like; mediates peroxidase activityBy similarityAdd BLAST568
Regioni956 – 1250Interaction with TXNDC11By similarityAdd BLAST295

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.
InParanoidiQ8HZK3.
KOiK13411.

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:SF75. PTHR11972:SF75. 2 hits.
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.

Q8HZK3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFRLALAWT LLVGPWMPMG ARNSISWEVQ RFDGWYNNLM EHKWGSKGSR
60 70 80 90 100
LQRLVPASYA DGVYQPLGEP HLPNPRDLSN TAMRGPAGQA SLRNRTVLGV
110 120 130 140 150
FFGYHVLSDL VSIEKPGCPA EFLNIHIPPG DPVFDPHKSG DVVLPFQRSR
160 170 180 190 200
WDPNTGQSPS NPRDLTNEVT GWLDGSAIYG SSHSWSDELR SFSGGQLASG
210 220 230 240 250
PDPAFPRQAQ DPLFMWTPPD PATGQRGPQG LYAFGAEQGN REPFLQALGL
260 270 280 290 300
LWFRYHNLCA QKLAREHPLW GDEELFQHAR KRVIATYQSI TMYEWLPSFL
310 320 330 340 350
RKMPQEYTGY RPFLDPSISP EFLAASEQFF STMVPPGVYM RNASCHFQGV
360 370 380 390 400
INRNSSVSRA LRVCNSYWSR EHPNLQRAED VDALLLGMAS QIAEREDHMV
410 420 430 440 450
VEDVQDFWPG PLKFSRTDHL ASCLQRGRDL GLPSYTKARA RLGLPPVTRW
460 470 480 490 500
QDINPALSRS DGIVLEATAA LYNQDLSRLE LLPGGLLESY GDPGPLFSTI
510 520 530 540 550
VLDQFVRLRD GDRYWFENTK NGLFSEKEIA EIRNTSLRDV LVAVTNMTPG
560 570 580 590 600
ALQPNVFFWH AGDPCPQPRQ LSTKDLPACA PLIMRDYFKG SGFGFGVTIG
610 620 630 640 650
TLCCFPLVSL LSAWIVAQLR RRNFKRLQVQ NRQSIMCEKL VGGMKALEWQ
660 670 680 690 700
GRKEPCRPVL VHLQSGQIHV MDGRLSVLRT IQLRPPQQVN LILSSNHGRR
710 720 730 740 750
TLLLKIPKEY DLVLMFDLEE ERQVMVENLQ SALKESGLSF QEWELREQEL
760 770 780 790 800
MRAAVTREQR SHLLETFFRH LFSQVLDIDQ ADAGALPLDS SQKVREALTC
810 820 830 840 850
ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF LDILVVFMKG
860 870 880 890 900
SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLTEVV
910 920 930 940 950
ESMFREAGFQ DKQELTWEDF HFMLRDHDSE LRFTQLCVKG VEVPEVIKDL
960 970 980 990 1000
CRRASYISQE KLCPSPRVSA HCPRSNVDVE VELTPWKLQC PTDTDPPQEI
1010 1020 1030 1040 1050
RRRFGKKVTS FQPLLFTEAH REKFQRSRRH QTVQQFKRFV ENYRRHIGCL
1060 1070 1080 1090 1100
AVFYTIAGGL FLERAYYYAF AAHHMGITDT TRVGIILSRG TAASISFMFS
1110 1120 1130 1140 1150
YILLTMCRNL ITFLRETFLN RYVPFDAAVD FHRLIASTAI ILTVLHSAGH
1160 1170 1180 1190 1200
VVNVYLFSIS PLSVLSCLFP GLFHDNGSEF PQKYYWWFFQ TVPGLTGVML
1210 1220 1230 1240 1250
LLILAIMYVF ASHHFRRCSF RGFWLTHHLY ILLYMLLIIH GSFALIQLPR
1260 1270 1280 1290 1300
FHIFFLVPAL IYVGDKLVSL SRKKVEISVV KAELLPSGVT HLQFQRPQGF
1310 1320 1330 1340 1350
EYKSGQWVRI ACLALGTTEY HPFTLTSAPH EDTLSLHIRA AGPWTTRLRE
1360 1370 1380 1390 1400
IYSPPTDDNC AKYPKLYLDG PFGEGHQEWH KFEVSVLVGG GIGVTPFASI
1410 1420 1430 1440 1450
LKDLVFKSSV SCQVFCKKIY FIWVTRTQRQ FEWLADIIRE VEENDHRDLV
1460 1470 1480 1490 1500
SVHIYITQLA EKFDLRTTML YICERHFQKV LNRSLFTGLR SITHFGRPPF
1510 1520 1530 1540 1550
EPFFNSLQEV HPQVRKIGVF SCGPPGMTKN VEKACQLINR QDRTHFSHHY

ENF
Length:1,553
Mass (Da):177,861
Last modified:March 1, 2003 - v1
Checksum:i9F9364322977B710
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF547266 mRNA. Translation: AAN39338.1.
RefSeqiNP_999261.1. NM_214096.2.
UniGeneiSsc.35919.

Genome annotation databases

GeneIDi397177.
KEGGissc:397177.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF547266 mRNA. Translation: AAN39338.1.
RefSeqiNP_999261.1. NM_214096.2.
UniGeneiSsc.35919.

3D structure databases

ProteinModelPortaliQ8HZK3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000005035.

Protein family/group databases

PeroxiBasei3348. SscDuOx01.

Proteomic databases

PaxDbiQ8HZK3.
PRIDEiQ8HZK3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397177.
KEGGissc:397177.

Organism-specific databases

CTDi53905.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
HOGENOMiHOG000231774.
HOVERGENiHBG080428.
InParanoidiQ8HZK3.
KOiK13411.

Enzyme and pathway databases

UniPathwayiUPA00194.

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:SF75. PTHR11972:SF75. 2 hits.
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...

Entry informationi

Entry nameiDUOX1_PIG
AccessioniPrimary (citable) accession number: Q8HZK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: March 1, 2003
Last modified: November 30, 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.