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Protein

Dual oxidase 1

Gene

DUOX1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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)+ + H2O2.1 Publication

Enzyme regulationi

Peroxidase activity is inhibited by aminobenzohydrazide (By similarity). The NADPH oxidase activity is calcium-dependent.By similarity1 Publication

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

  • calcium ion binding Source: InterPro
  • heme binding Source: InterPro
  • NAD(P)H oxidase activity Source: UniProtKB
  • NADP binding Source: UniProtKB
  • peroxidase activity Source: UniProtKB-KW

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

ReactomeiR-CFA-209968. Thyroxine biosynthesis.
UniPathwayiUPA00194.

Protein family/group databases

PeroxiBasei3336. CfaDuOx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual oxidase 1 (EC:1.11.1.-, EC:1.6.3.1)
Alternative name(s):
NADPH thyroid oxidase 1
Short name:
Thyroid oxidase 1
Gene namesi
Name:DUOX1
Synonyms:THOX1
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Chromosome 30

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 596ExtracellularSequence analysisAdd BLAST575
Transmembranei597 – 617HelicalSequence analysisAdd BLAST21
Topological domaini618 – 1044CytoplasmicSequence analysisAdd BLAST427
Transmembranei1045 – 1065HelicalSequence analysisAdd BLAST21
Topological domaini1066 – 1080ExtracellularSequence analysisAdd BLAST15
Transmembranei1081 – 1101HelicalSequence analysisAdd BLAST21
Topological domaini1102 – 1151CytoplasmicSequence analysisAdd BLAST50
Transmembranei1152 – 1172HelicalSequence analysisAdd BLAST21
Topological domaini1173 – 1188ExtracellularSequence analysisAdd BLAST16
Transmembranei1189 – 1209HelicalSequence analysisAdd BLAST21
Topological domaini1210 – 1226CytoplasmicSequence analysisAdd BLAST17
Transmembranei1227 – 1247HelicalSequence analysisAdd BLAST21
Topological domaini1248ExtracellularSequence analysis1
Transmembranei1249 – 1269HelicalSequence analysisAdd BLAST21
Topological domaini1270 – 1551CytoplasmicSequence analysisAdd BLAST282

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000022334722 – 1551Dual oxidase 1Add BLAST1530

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Glycosylationi342N-linked (GlcNAc...)Sequence analysis1
Glycosylationi354N-linked (GlcNAc...)Sequence analysis1
Glycosylationi461N-linked (GlcNAc...)Sequence analysis1
Glycosylationi534N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9MZF4.
PRIDEiQ9MZF4.

Expressioni

Tissue specificityi

Expressed in thyrocytes (at protein level). Specifically expressed in thyroid.1 Publication

Inductioni

By forskolin (at protein level). By thyrotropin.1 Publication

Interactioni

Subunit structurei

Interacts with TPO and CYBA (By similarity). Interacts with TXNDC11.By similarity1 Publication

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000020209.

Structurei

3D structure databases

ProteinModelPortaliQ9MZF4.
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
Domaini1087 – 1269Ferric oxidoreductaseAdd BLAST183
Domaini1270 – 1376FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST107

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 593Peroxidase-like; mediates peroxidase activityBy similarityAdd BLAST568
Regioni956 – 1248Interaction with TXNDC111 PublicationAdd BLAST293

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.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000231774.
HOVERGENiHBG080428.
InParanoidiQ9MZF4.
KOiK13411.
OMAiCHFQEVI.
OrthoDBiEOG091G00PO.
TreeFamiTF105424.

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. 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]

Sequencei

Sequence statusi: Complete.

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

Q9MZF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFCLALTWT FLVGSWTSMG AQKPISWEVQ RFDGWYNNLM EHKWGSKGSR
60 70 80 90 100
LQRLVPASYA DGVYQPLGEP HLPNPRDLSN AAMRGPAGQA SLRNRTVLGV
110 120 130 140 150
FFGYHVLSDL VSVETPGCPA EFLNIRIPPG DPVFDPNGRG DVVLPFQRSR
160 170 180 190 200
WDPESGQSPS NPRDLTNAVT GWLDGSAIYG SSHSWSDALR SFSGGQLASG
210 220 230 240 250
PDPAFPRNAQ PPLLMWSAPD PASGQRGPGG LYAFGAERGN RDPFLQALGL
260 270 280 290 300
LWFRYHNLCA QRLARQHPHW GDEELFQHAR KRVIATYQNI ALYEWLPSFL
310 320 330 340 350
QQAPVKYAGY NPFLDPSISP EFLVASEQFF STMVPPGIYM RNASCHFQEV
360 370 380 390 400
INRNSSISRA LRVCNSYWSR KHPNLRRAED VDALLLGMAS QIAEREDHVV
410 420 430 440 450
VEDVLDFWPG SLKFSRTDHV AGCLQRGRDL GLPSYTKARA ALGLPPITRW
460 470 480 490 500
QDINPALSQN NHTVLEATAA LYNQDLSQLE LLPGGLLESH GDPGPLFSAI
510 520 530 540 550
VLNQFVRLRD GDRYWFENTR NGLFSEEEIA EIRNTSLRDV LVAVTNMNPS
560 570 580 590 600
TLQPNVFFWH MGDPCPQPRQ LSTQGLPACA PSTMQDYFEG SGFGFGVTIG
610 620 630 640 650
TLCCFPLVSL LSAWIVARLR KKNFKKLQGQ DRKSVMSEKL VGGMEALEWQ
660 670 680 690 700
GHKEPCRPVL VHLQPGQICV VDGRLSVLRT IQLRPPQQVN LILSGNRGRR
710 720 730 740 750
ALLLKIPKEY DLVLLFNLEE ERQVLVENLR GALKESGLKF QEWELREQEL
760 770 780 790 800
MRTAVTRQQR SHLLETFFRH LFSQVLDIDQ ADAGTLPLDS SQKVQEALTC
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
ESMFRESGFQ DKEELTWEDF HFMLRDHDSE LRFTQLCVRG VEVPEVIKDL
960 970 980 990 1000
CRRASYISQE KICPSPRVSA RCPHSNTEVE WTPQRLQCPV DTDPPQEIRR
1010 1020 1030 1040 1050
RFGKKVTSFQ PLLFTEAQRE KFQRSRRHQT LQQFKRFIEN YRRHIGCVAV
1060 1070 1080 1090 1100
FYAITGGLFL ERAYYYAFGA HHMGITDTTR VGIILSRGTA ASISFMFSYI
1110 1120 1130 1140 1150
LLTMCRNLIT FLRETFLNRY VPFDAAVDFH RLIASTAIVL TVLHSAGHVV
1160 1170 1180 1190 1200
NVYLFSISPL SVLSCLFPGL FHNDGSEFPQ KYYWWFFQTV PGLTGVMLLL
1210 1220 1230 1240 1250
VLAIMYVFAS HHFRRHSFRG FWLTHHLYIL LYVLLIIHGS FGLIQLPRFH
1260 1270 1280 1290 1300
IFFLVPALIY VGDKLVSLSR KKVEISVVKA ELLPSGVTHL QFQRPQGFEY
1310 1320 1330 1340 1350
KSGQWVQIAC LALGTTEYHP FTLTSAPHED TLSLHIRAAG PWTTRLREIY
1360 1370 1380 1390 1400
SPPTGDGCAK YPKLYLDGPF GEGHQEWHKF EVSVLVGGGI GVTPFASILK
1410 1420 1430 1440 1450
DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE ENDCQDLVSV
1460 1470 1480 1490 1500
HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSI THFGRPPFEP
1510 1520 1530 1540 1550
FFKSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINRQD RTHFSHHYEN

F
Length:1,551
Mass (Da):176,716
Last modified:October 1, 2000 - v1
Checksum:i94F7E93F34C9F1EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230497 mRNA. Translation: AAF73923.1.
RefSeqiNP_001003122.1. NM_001003122.2.
XP_005638229.1. XM_005638172.1.
XP_005638230.1. XM_005638173.1.
XP_013964813.1. XM_014109338.1.
UniGeneiCfa.3587.

Genome annotation databases

EnsembliENSCAFT00000021757; ENSCAFP00000020209; ENSCAFG00000013715.
GeneIDi403720.
KEGGicfa:403720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230497 mRNA. Translation: AAF73923.1.
RefSeqiNP_001003122.1. NM_001003122.2.
XP_005638229.1. XM_005638172.1.
XP_005638230.1. XM_005638173.1.
XP_013964813.1. XM_014109338.1.
UniGeneiCfa.3587.

3D structure databases

ProteinModelPortaliQ9MZF4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000020209.

Protein family/group databases

PeroxiBasei3336. CfaDuOx01.

Proteomic databases

PaxDbiQ9MZF4.
PRIDEiQ9MZF4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000021757; ENSCAFP00000020209; ENSCAFG00000013715.
GeneIDi403720.
KEGGicfa:403720.

Organism-specific databases

CTDi53905.

Phylogenomic databases

eggNOGiKOG0039. Eukaryota.
ENOG410XNZY. LUCA.
GeneTreeiENSGT00550000074350.
HOGENOMiHOG000231774.
HOVERGENiHBG080428.
InParanoidiQ9MZF4.
KOiK13411.
OMAiCHFQEVI.
OrthoDBiEOG091G00PO.
TreeFamiTF105424.

Enzyme and pathway databases

UniPathwayiUPA00194.
ReactomeiR-CFA-209968. Thyroxine biosynthesis.

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. 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 nameiDUOX1_CANLF
AccessioniPrimary (citable) accession number: Q9MZF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 106 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.