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Q9MZF4 (DUOX1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DUOX1
Synonyms:THOX1
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length1551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

NAD(P)H + O2 = NAD(P)+ + H2O2. Ref.2

Enzyme regulation

Peroxidase activity is inhibited by aminobenzohydrazide By similarity. The NADPH oxidase activity is calcium-dependent. Ref.2

Pathway

Hormone biosynthesis; thyroid hormone biosynthesis.

Subunit structure

Interacts with TPO and CYBA By similarity. Interacts with TXNDC11. Ref.3

Subcellular location

Apical cell membrane; Multi-pass membrane protein By similarity. Note: Localizes to the apical membrane of epithelial cells By similarity. Ref.2

Tissue specificity

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

Induction

By forskolin (at protein level). By thyrotropin. Ref.1 Ref.2

Post-translational modification

N-glycosylated. Ref.2

Sequence similarities

In the N-terminal section; belongs to the peroxidase family.

Contains 3 EF-hand domains.

Contains 1 FAD-binding FR-type domain.

Contains 1 ferric oxidoreductase domain.

Ontologies

Keywords
   Biological processHydrogen peroxide
Thyroid hormones biosynthesis
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
FAD
Metal-binding
NADP
   Molecular functionOxidoreductase
Peroxidase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcuticle development

Inferred from sequence or structural similarity. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

hormone biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

hydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

superoxide anion generation

Non-traceable author statement Ref.1. Source: UniProtKB

thyroid hormone generation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentapical plasma membrane

Non-traceable author statement Ref.1. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionNAD(P)H oxidase activity

Non-traceable author statement Ref.1. Source: UniProtKB

NADP binding

Non-traceable author statement Ref.1. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 15511530Dual oxidase 1
PRO_0000223347

Regions

Topological domain22 – 596575Extracellular Potential
Transmembrane597 – 61721Helical; Potential
Topological domain618 – 1044427Cytoplasmic Potential
Transmembrane1045 – 106521Helical; Potential
Topological domain1066 – 108015Extracellular Potential
Transmembrane1081 – 110121Helical; Potential
Topological domain1102 – 115150Cytoplasmic Potential
Transmembrane1152 – 117221Helical; Potential
Topological domain1173 – 118816Extracellular Potential
Transmembrane1189 – 120921Helical; Potential
Topological domain1210 – 122617Cytoplasmic Potential
Transmembrane1227 – 124721Helical; Potential
Topological domain12481Extracellular Potential
Transmembrane1249 – 126921Helical; Potential
Topological domain1270 – 1551282Cytoplasmic Potential
Domain815 – 85036EF-hand 1
Domain851 – 88636EF-hand 2
Domain895 – 93036EF-hand 3
Domain1087 – 1269183Ferric oxidoreductase
Domain1270 – 1376107FAD-binding FR-type
Calcium binding828 – 839121 Potential
Calcium binding864 – 875122 Potential
Region26 – 593568Peroxidase-like; mediates peroxidase activity By similarity
Region956 – 1248293Interaction with TXNDC11

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9MZF4 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 94F7E93F34C9F1EE

FASTA1,551176,716
        10         20         30         40         50         60 
MGFCLALTWT FLVGSWTSMG AQKPISWEVQ RFDGWYNNLM EHKWGSKGSR LQRLVPASYA 

        70         80         90        100        110        120 
DGVYQPLGEP HLPNPRDLSN AAMRGPAGQA SLRNRTVLGV FFGYHVLSDL VSVETPGCPA 

       130        140        150        160        170        180 
EFLNIRIPPG DPVFDPNGRG DVVLPFQRSR WDPESGQSPS NPRDLTNAVT GWLDGSAIYG 

       190        200        210        220        230        240 
SSHSWSDALR SFSGGQLASG PDPAFPRNAQ PPLLMWSAPD PASGQRGPGG LYAFGAERGN 

       250        260        270        280        290        300 
RDPFLQALGL LWFRYHNLCA QRLARQHPHW GDEELFQHAR KRVIATYQNI ALYEWLPSFL 

       310        320        330        340        350        360 
QQAPVKYAGY NPFLDPSISP EFLVASEQFF STMVPPGIYM RNASCHFQEV INRNSSISRA 

       370        380        390        400        410        420 
LRVCNSYWSR KHPNLRRAED VDALLLGMAS QIAEREDHVV VEDVLDFWPG SLKFSRTDHV 

       430        440        450        460        470        480 
AGCLQRGRDL GLPSYTKARA ALGLPPITRW QDINPALSQN NHTVLEATAA LYNQDLSQLE 

       490        500        510        520        530        540 
LLPGGLLESH GDPGPLFSAI VLNQFVRLRD GDRYWFENTR NGLFSEEEIA EIRNTSLRDV 

       550        560        570        580        590        600 
LVAVTNMNPS TLQPNVFFWH MGDPCPQPRQ LSTQGLPACA PSTMQDYFEG SGFGFGVTIG 

       610        620        630        640        650        660 
TLCCFPLVSL LSAWIVARLR KKNFKKLQGQ DRKSVMSEKL VGGMEALEWQ GHKEPCRPVL 

       670        680        690        700        710        720 
VHLQPGQICV VDGRLSVLRT IQLRPPQQVN LILSGNRGRR ALLLKIPKEY DLVLLFNLEE 

       730        740        750        760        770        780 
ERQVLVENLR GALKESGLKF QEWELREQEL MRTAVTRQQR SHLLETFFRH LFSQVLDIDQ 

       790        800        810        820        830        840 
ADAGTLPLDS SQKVQEALTC ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF 

       850        860        870        880        890        900 
LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLTEVV 

       910        920        930        940        950        960 
ESMFRESGFQ DKEELTWEDF HFMLRDHDSE LRFTQLCVRG VEVPEVIKDL CRRASYISQE 

       970        980        990       1000       1010       1020 
KICPSPRVSA RCPHSNTEVE WTPQRLQCPV DTDPPQEIRR RFGKKVTSFQ PLLFTEAQRE 

      1030       1040       1050       1060       1070       1080 
KFQRSRRHQT LQQFKRFIEN YRRHIGCVAV FYAITGGLFL ERAYYYAFGA HHMGITDTTR 

      1090       1100       1110       1120       1130       1140 
VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY VPFDAAVDFH RLIASTAIVL 

      1150       1160       1170       1180       1190       1200 
TVLHSAGHVV NVYLFSISPL SVLSCLFPGL FHNDGSEFPQ KYYWWFFQTV PGLTGVMLLL 

      1210       1220       1230       1240       1250       1260 
VLAIMYVFAS HHFRRHSFRG FWLTHHLYIL LYVLLIIHGS FGLIQLPRFH IFFLVPALIY 

      1270       1280       1290       1300       1310       1320 
VGDKLVSLSR KKVEISVVKA ELLPSGVTHL QFQRPQGFEY KSGQWVQIAC LALGTTEYHP 

      1330       1340       1350       1360       1370       1380 
FTLTSAPHED TLSLHIRAAG PWTTRLREIY SPPTGDGCAK YPKLYLDGPF GEGHQEWHKF 

      1390       1400       1410       1420       1430       1440 
EVSVLVGGGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE 

      1450       1460       1470       1480       1490       1500 
ENDCQDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSI THFGRPPFEP 

      1510       1520       1530       1540       1550 
FFKSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINRQD RTHFSHHYEN F

« Hide

References

[1]"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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[2]"Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system."
De Deken X., Wang D., Dumont J.E., Miot F.
Exp. Cell Res. 273:187-196(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ENZYME REGULATION, GLYCOSYLATION.
[3]"Identification of a novel partner of duox: EFP1, a thioredoxin-related protein."
Wang D., De Deken X., Milenkovic M., Song Y., Pirson I., Dumont J.E., Miot F.
J. Biol. Chem. 280:3096-3103(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TXNDC11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF230497 mRNA. Translation: AAF73923.1.
RefSeqNP_001003122.1. NM_001003122.2.
UniGeneCfa.3587.

3D structure databases

ProteinModelPortalQ9MZF4.
ModBaseSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000020209.

Protein family/group databases

PeroxiBase3336. CfaDuOx01.

Proteomic databases

PRIDEQ9MZF4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000021757; ENSCAFP00000020209; ENSCAFG00000013715.
GeneID403720.
KEGGcfa:403720.

Organism-specific databases

CTD53905.

Phylogenomic databases

eggNOGCOG5126.
GeneTreeENSGT00550000074350.
HOGENOMHOG000231774.
HOVERGENHBG080428.
InParanoidQ9MZF4.
KOK13411.
OMAHRRHIGC.
OrthoDBEOG4VQ9ND.

Enzyme and pathway databases

UniPathwayUPA00194.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.10.640.10. 1 hit.
InterProIPR011992. EF-hand-like_dom.
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.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
PF13499. EF_hand_5. 1 hit.
PF08022. FAD_binding_8. 1 hit.
PF01794. Ferric_reduct. 1 hit.
PF08030. NAD_binding_6. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF48113. Peroxidase_super. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS51384. FAD_FR. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20817223.

Entry information

Entry nameDUOX1_CANFA
AccessionPrimary (citable) accession number: Q9MZF4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents