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Q8HZK3

- DUOX1_PIG

UniProt

Q8HZK3 - DUOX1_PIG

Protein

Dual oxidase 1

Gene

DUOX1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi828 – 839121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi864 – 875122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. heme binding Source: InterPro
    3. NAD(P)H oxidase activity Source: UniProtKB-EC
    4. peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cuticle development Source: UniProtKB
    2. cytokine-mediated signaling pathway Source: UniProtKB
    3. hormone biosynthetic process Source: UniProtKB-KW
    4. hydrogen peroxide catabolic process Source: UniProtKB-KW
    5. response to cAMP Source: UniProtKB
    6. thyroid hormone generation Source: UniProtKB-UniPathway

    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
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

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

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 15531532Dual oxidase 1PRO_0000223345Add
    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
    Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Glycoprotein

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 596575ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini618 – 1046429CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1068 – 108215ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1104 – 113835CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1160 – 119031ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1212 – 122817CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1250 – 12501ExtracellularSequence Analysis
    Topological domaini1272 – 1553282CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei597 – 61721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1047 – 106721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1083 – 110321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1139 – 115921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1191 – 121121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1229 – 124921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1251 – 127121HelicalSequence AnalysisAdd
    BLAST

    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
    Domaini1089 – 1271183Ferric oxidoreductaseAdd
    BLAST
    Domaini1272 – 1378107FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 593568Peroxidase-like; mediates peroxidase activityBy similarityAdd
    BLAST
    Regioni956 – 1250295Interaction 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

    eggNOGiCOG5126.
    HOGENOMiHOG000231774.
    HOVERGENiHBG080428.
    KOiK13411.

    Family and domain databases

    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:SF37. PTHR11972:SF37. 1 hit.
    PfamiPF03098. An_peroxidase. 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]
    SUPFAMiSSF48113. 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

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    MGFRLALAWT LLVGPWMPMG ARNSISWEVQ RFDGWYNNLM EHKWGSKGSR     50
    LQRLVPASYA DGVYQPLGEP HLPNPRDLSN TAMRGPAGQA SLRNRTVLGV 100
    FFGYHVLSDL VSIEKPGCPA EFLNIHIPPG DPVFDPHKSG DVVLPFQRSR 150
    WDPNTGQSPS NPRDLTNEVT GWLDGSAIYG SSHSWSDELR SFSGGQLASG 200
    PDPAFPRQAQ DPLFMWTPPD PATGQRGPQG LYAFGAEQGN REPFLQALGL 250
    LWFRYHNLCA QKLAREHPLW GDEELFQHAR KRVIATYQSI TMYEWLPSFL 300
    RKMPQEYTGY RPFLDPSISP EFLAASEQFF STMVPPGVYM RNASCHFQGV 350
    INRNSSVSRA LRVCNSYWSR EHPNLQRAED VDALLLGMAS QIAEREDHMV 400
    VEDVQDFWPG PLKFSRTDHL ASCLQRGRDL GLPSYTKARA RLGLPPVTRW 450
    QDINPALSRS DGIVLEATAA LYNQDLSRLE LLPGGLLESY GDPGPLFSTI 500
    VLDQFVRLRD GDRYWFENTK NGLFSEKEIA EIRNTSLRDV LVAVTNMTPG 550
    ALQPNVFFWH AGDPCPQPRQ LSTKDLPACA PLIMRDYFKG SGFGFGVTIG 600
    TLCCFPLVSL LSAWIVAQLR RRNFKRLQVQ NRQSIMCEKL VGGMKALEWQ 650
    GRKEPCRPVL VHLQSGQIHV MDGRLSVLRT IQLRPPQQVN LILSSNHGRR 700
    TLLLKIPKEY DLVLMFDLEE ERQVMVENLQ SALKESGLSF QEWELREQEL 750
    MRAAVTREQR SHLLETFFRH LFSQVLDIDQ ADAGALPLDS SQKVREALTC 800
    ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF LDILVVFMKG 850
    SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLTEVV 900
    ESMFREAGFQ DKQELTWEDF HFMLRDHDSE LRFTQLCVKG VEVPEVIKDL 950
    CRRASYISQE KLCPSPRVSA HCPRSNVDVE VELTPWKLQC PTDTDPPQEI 1000
    RRRFGKKVTS FQPLLFTEAH REKFQRSRRH QTVQQFKRFV ENYRRHIGCL 1050
    AVFYTIAGGL FLERAYYYAF AAHHMGITDT TRVGIILSRG TAASISFMFS 1100
    YILLTMCRNL ITFLRETFLN RYVPFDAAVD FHRLIASTAI ILTVLHSAGH 1150
    VVNVYLFSIS PLSVLSCLFP GLFHDNGSEF PQKYYWWFFQ TVPGLTGVML 1200
    LLILAIMYVF ASHHFRRCSF RGFWLTHHLY ILLYMLLIIH GSFALIQLPR 1250
    FHIFFLVPAL IYVGDKLVSL SRKKVEISVV KAELLPSGVT HLQFQRPQGF 1300
    EYKSGQWVRI ACLALGTTEY HPFTLTSAPH EDTLSLHIRA AGPWTTRLRE 1350
    IYSPPTDDNC AKYPKLYLDG PFGEGHQEWH KFEVSVLVGG GIGVTPFASI 1400
    LKDLVFKSSV SCQVFCKKIY FIWVTRTQRQ FEWLADIIRE VEENDHRDLV 1450
    SVHIYITQLA EKFDLRTTML YICERHFQKV LNRSLFTGLR SITHFGRPPF 1500
    EPFFNSLQEV HPQVRKIGVF SCGPPGMTKN VEKACQLINR QDRTHFSHHY 1550
    ENF 1553
    Length:1,553
    Mass (Da):177,861
    Last modified:March 1, 2003 - v1
    Checksum:i9F9364322977B710
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF547266 mRNA. Translation: AAN39338.1 .
    RefSeqi NP_999261.1. NM_214096.2.
    UniGenei Ssc.35919.

    3D structure databases

    ProteinModelPortali Q8HZK3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000005035.

    Protein family/group databases

    PeroxiBasei 3348. SscDuOx01.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397177.
    KEGGi ssc:397177.

    Organism-specific databases

    CTDi 53905.

    Phylogenomic databases

    eggNOGi COG5126.
    HOGENOMi HOG000231774.
    HOVERGENi HBG080428.
    KOi K13411.

    Enzyme and pathway databases

    UniPathwayi UPA00194 .

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.640.10. 1 hit.
    InterProi IPR029595. 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 ]
    PANTHERi PTHR11972:SF37. PTHR11972:SF37. 1 hit.
    Pfami PF03098. An_peroxidase. 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 ]
    PRINTSi PR00457. ANPEROXIDASE.
    SMARTi SM00054. EFh. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48113. SSF48113. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS51384. FAD_FR. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Effect of iodide on nicotinamide adenine dinucleotide phosphate oxidase activity and Duox2 protein expression in isolated porcine thyroid follicles."
      Morand S., Chaaraoui M., Kaniewski J., Deme D., Ohayon R., Noel-Hudson M.-S., Virion A., Dupuy C.
      Endocrinology 144:1241-1248(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Thyroid.
    2. Cited for: TISSUE SPECIFICITY.

    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: October 1, 2014
    This is version 81 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

    External Data

    Dasty 3