DUOX1_PIG
ID DUOX1_PIG Reviewed; 1553 AA.
AC Q8HZK3;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Dual oxidase 1;
DE EC=1.11.1.-;
DE EC=1.6.3.1;
DE Flags: Precursor;
GN Name=DUOX1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=12639906; DOI=10.1210/en.2002-220981;
RA Morand S., Chaaraoui M., Kaniewski J., Deme D., Ohayon R.,
RA Noel-Hudson M.-S., Virion A., Dupuy C.;
RT "Effect of iodide on nicotinamide adenine dinucleotide phosphate oxidase
RT activity and Duox2 protein expression in isolated porcine thyroid
RT follicles.";
RL Endocrinology 144:1241-1248(2003).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=15591162; DOI=10.1152/ajpgi.00198.2004;
RA Ameziane-El-Hassani R., Benfares N., Caillou B., Talbot M., Sabourin J.-C.,
RA Belotte V., Morand S., Gnidehou S., Agnandji D., Ohayon R., Kaniewski J.,
RA Noel-Hudson M.-S., Bidart J.-M., Schlumberger M., Virion A., Dupuy C.;
RT "Dual oxidase2 is expressed all along the digestive tract.";
RL Am. J. Physiol. 288:G933-G942(2005).
CC -!- FUNCTION: Generates hydrogen peroxide which is required for the
CC activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a
CC role in thyroid hormones synthesis and lactoperoxidase-mediated
CC antimicrobial defense at the surface of mucosa. May have its own
CC peroxidase activity through its N-terminal peroxidase-like domain.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC -!- ACTIVITY REGULATION: The NADPH oxidase activity is calcium-dependent.
CC Peroxidase activity is inhibited by aminobenzohydrazide (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC -!- SUBUNIT: Interacts with TXNDC11, TPO and CYBA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Localizes to the apical membrane
CC of epithelial cells. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in thyroid.
CC {ECO:0000269|PubMed:15591162}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC family. {ECO:0000305}.
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DR EMBL; AF547266; AAN39338.1; -; mRNA.
DR RefSeq; NP_999261.1; NM_214096.2.
DR AlphaFoldDB; Q8HZK3; -.
DR SMR; Q8HZK3; -.
DR PeroxiBase; 3348; SscDuOx01.
DR PaxDb; Q8HZK3; -.
DR Ensembl; ENSSSCT00015061098; ENSSSCP00015024547; ENSSSCG00015044714.
DR Ensembl; ENSSSCT00015061238; ENSSSCP00015024609; ENSSSCG00015044714.
DR Ensembl; ENSSSCT00030100495; ENSSSCP00030046333; ENSSSCG00030071685.
DR Ensembl; ENSSSCT00035042519; ENSSSCP00035017004; ENSSSCG00035032081.
DR Ensembl; ENSSSCT00040084544; ENSSSCP00040036891; ENSSSCG00040061821.
DR Ensembl; ENSSSCT00045002873; ENSSSCP00045001810; ENSSSCG00045001783.
DR Ensembl; ENSSSCT00050107780; ENSSSCP00050047723; ENSSSCG00050078157.
DR Ensembl; ENSSSCT00055024871; ENSSSCP00055019747; ENSSSCG00055012477.
DR Ensembl; ENSSSCT00060054640; ENSSSCP00060023303; ENSSSCG00060040313.
DR GeneID; 397177; -.
DR KEGG; ssc:397177; -.
DR CTD; 53905; -.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; Q8HZK3; -.
DR OrthoDB; 27424at2759; -.
DR UniPathway; UPA00194; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0043020; C:NADPH oxidase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0106293; F:NADH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0042335; P:cuticle development; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051591; P:response to cAMP; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:UniProtKB-UniPathway.
DR CDD; cd09820; dual_peroxidase_like; 1.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 1.10.640.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR029595; DUOX1/Duox.
DR InterPro; IPR034821; DUOX_peroxidase.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF75; PTHR11972:SF75; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF00036; EF-hand_1; 2.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF48113; SSF48113; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; FAD; Flavoprotein; Glycoprotein; Hydrogen peroxide;
KW Membrane; Metal-binding; NADP; Oxidoreductase; Peroxidase;
KW Reference proteome; Repeat; Signal; Thyroid hormones biosynthesis;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1553
FT /note="Dual oxidase 1"
FT /id="PRO_0000223345"
FT TOPO_DOM 22..596
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..1046
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1047..1067
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1068..1082
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1104..1138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1139..1159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1160..1190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1191..1211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1212..1228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1229..1249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1251..1271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1272..1553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 815..850
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 851..886
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 895..930
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1089..1271
FT /note="Ferric oxidoreductase"
FT DOMAIN 1272..1378
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 26..593
FT /note="Peroxidase-like; mediates peroxidase activity"
FT /evidence="ECO:0000250"
FT REGION 956..1250
FT /note="Interaction with TXNDC11"
FT /evidence="ECO:0000250"
FT BINDING 828
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 830
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 832
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 834
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 839
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 864
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 866
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 868
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 875
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1553 AA; 177861 MW; 9F9364322977B710 CRC64;
MGFRLALAWT LLVGPWMPMG ARNSISWEVQ RFDGWYNNLM EHKWGSKGSR LQRLVPASYA
DGVYQPLGEP HLPNPRDLSN TAMRGPAGQA SLRNRTVLGV FFGYHVLSDL VSIEKPGCPA
EFLNIHIPPG DPVFDPHKSG DVVLPFQRSR WDPNTGQSPS NPRDLTNEVT GWLDGSAIYG
SSHSWSDELR SFSGGQLASG PDPAFPRQAQ DPLFMWTPPD PATGQRGPQG LYAFGAEQGN
REPFLQALGL LWFRYHNLCA QKLAREHPLW GDEELFQHAR KRVIATYQSI TMYEWLPSFL
RKMPQEYTGY RPFLDPSISP EFLAASEQFF STMVPPGVYM RNASCHFQGV INRNSSVSRA
LRVCNSYWSR EHPNLQRAED VDALLLGMAS QIAEREDHMV VEDVQDFWPG PLKFSRTDHL
ASCLQRGRDL GLPSYTKARA RLGLPPVTRW QDINPALSRS DGIVLEATAA LYNQDLSRLE
LLPGGLLESY GDPGPLFSTI VLDQFVRLRD GDRYWFENTK NGLFSEKEIA EIRNTSLRDV
LVAVTNMTPG ALQPNVFFWH AGDPCPQPRQ LSTKDLPACA PLIMRDYFKG SGFGFGVTIG
TLCCFPLVSL LSAWIVAQLR RRNFKRLQVQ NRQSIMCEKL VGGMKALEWQ GRKEPCRPVL
VHLQSGQIHV MDGRLSVLRT IQLRPPQQVN LILSSNHGRR TLLLKIPKEY DLVLMFDLEE
ERQVMVENLQ SALKESGLSF QEWELREQEL MRAAVTREQR SHLLETFFRH LFSQVLDIDQ
ADAGALPLDS SQKVREALTC ELSRAEFAES LGLKPQDMFV ESMFSLADKD GNGYLSFREF
LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKAQLTEVV
ESMFREAGFQ DKQELTWEDF HFMLRDHDSE LRFTQLCVKG VEVPEVIKDL CRRASYISQE
KLCPSPRVSA HCPRSNVDVE VELTPWKLQC PTDTDPPQEI RRRFGKKVTS FQPLLFTEAH
REKFQRSRRH QTVQQFKRFV ENYRRHIGCL AVFYTIAGGL FLERAYYYAF AAHHMGITDT
TRVGIILSRG TAASISFMFS YILLTMCRNL ITFLRETFLN RYVPFDAAVD FHRLIASTAI
ILTVLHSAGH VVNVYLFSIS PLSVLSCLFP GLFHDNGSEF PQKYYWWFFQ TVPGLTGVML
LLILAIMYVF ASHHFRRCSF RGFWLTHHLY ILLYMLLIIH GSFALIQLPR FHIFFLVPAL
IYVGDKLVSL SRKKVEISVV KAELLPSGVT HLQFQRPQGF EYKSGQWVRI ACLALGTTEY
HPFTLTSAPH EDTLSLHIRA AGPWTTRLRE IYSPPTDDNC AKYPKLYLDG PFGEGHQEWH
KFEVSVLVGG GIGVTPFASI LKDLVFKSSV SCQVFCKKIY FIWVTRTQRQ FEWLADIIRE
VEENDHRDLV SVHIYITQLA EKFDLRTTML YICERHFQKV LNRSLFTGLR SITHFGRPPF
EPFFNSLQEV HPQVRKIGVF SCGPPGMTKN VEKACQLINR QDRTHFSHHY ENF
