DUOX1_RAT
ID DUOX1_RAT Reviewed; 1551 AA.
AC Q8CIY2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Dual oxidase 1;
DE EC=1.11.1.-;
DE EC=1.6.3.1;
DE Flags: Precursor;
GN Name=Duox1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344;
RX PubMed=12538618; DOI=10.1210/en.2002-220824;
RA Morand S., Dos Santos O.F., Ohayon R., Kaniewski J., Noel-Hudson M.-S.,
RA Virion A., Dupuy C.;
RT "Identification of a truncated dual oxidase 2 (DUOX2) messenger ribonucleic
RT acid (mRNA) in two rat thyroid cell lines. Insulin and forskolin regulation
RT of DUOX2 mRNA levels in FRTL-5 cells and porcine thyrocytes.";
RL Endocrinology 144:567-574(2003).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=10806195; DOI=10.1074/jbc.m000916200;
RA De Deken X., Wang D., Many M.-C., Costagliola S., Libert F., Vassart G.,
RA Dumont J.E., Miot F.;
RT "Cloning of two human thyroid cDNAs encoding new members of the NADPH
RT oxidase family.";
RL J. Biol. Chem. 275:23227-23233(2000).
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: Expressed in thyrocytes (at protein level).
CC {ECO:0000269|PubMed:10806195}.
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; AF542180; AAN33120.1; -; mRNA.
DR RefSeq; NP_714961.1; NM_153739.1.
DR AlphaFoldDB; Q8CIY2; -.
DR SMR; Q8CIY2; -.
DR STRING; 10116.ENSRNOP00000045928; -.
DR PeroxiBase; 3970; RnoDuOx01.
DR GlyGen; Q8CIY2; 5 sites.
DR PhosphoSitePlus; Q8CIY2; -.
DR PaxDb; Q8CIY2; -.
DR PRIDE; Q8CIY2; -.
DR GeneID; 266807; -.
DR KEGG; rno:266807; -.
DR UCSC; RGD:628760; rat.
DR CTD; 53905; -.
DR RGD; 628760; Duox1.
DR eggNOG; KOG0039; Eukaryota.
DR InParanoid; Q8CIY2; -.
DR OrthoDB; 27424at2759; -.
DR PhylomeDB; Q8CIY2; -.
DR Reactome; R-RNO-209968; Thyroxine biosynthesis.
DR UniPathway; UPA00194; -.
DR PRO; PR:Q8CIY2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:2000147; P:positive regulation of cell motility; ISO:RGD.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:RGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
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 1: Evidence at protein 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..1551
FT /note="Dual oxidase 1"
FT /id="PRO_0000223346"
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..1044
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1080
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1081..1101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1102..1136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1137..1157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1158..1188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1189..1209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1210..1226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1227..1247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1249..1269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1270..1551
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 1087..1269
FT /note="Ferric oxidoreductase"
FT DOMAIN 1270..1376
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..1248
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 461
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 1551 AA; 177197 MW; 52B07F83EF4E1FE2 CRC64;
MAVYSAVAWI LLFGVLASLG AQNPVSWEVQ RFDGWYNNLM EHRWGSKGSR LQRLVPASYA
DGVYQPLREP YLPNPRHLSN RVMRGPAGQP SLRNRTVLGV FFGYHVLSDL VSVETPGCPA
EFLNIYIPRG DPVFDPDKRG NVVLPFQRSR WDRSTGQSPS NPRDLTNQVT GWLDGSAIYG
SSHSWSDTLR SFSGGQLASG PDPAFPRNSQ NSLLMWMAPD PATGQGGPQG LYAFGAQRGN
REPFLQALGL LWFRYHNLCA KRLAQEHPHW GDEELFQHAR KRVIATYQNI AMYEWLPSFL
KQTPPEYPGY HPFLDPSISP EFVVASEQFL STMVPPGVYM RNASCHFQGI ANRNSSVSGA
LRVCNSYWSR ENPKLQRAED VDALLLGMAS QIAEREDHLV VEDVQDFWPG PLKFSRTDYL
ASCLQRGRDL GLPSYTKARE ALGLPPVSHW QDINPALSRS NGTVLEATAA LYNQDLSRLE
LLAGGLLESH GDPGPLFSAI VLDQFVRLRD GDRYWFENNR NGLFSKEEIA EIRNTSLRDI
LVAVTNVDPS ALQPSVFFWL AGDPCPQPSQ LSTQGLPACA PLFVRDYFKG SGFGFGLTIG
TLCCFPLVSL LSAWIVARLR MRNFKRLQRQ DRQSIMCEKL VGGVEALEWQ GRKEPCRPVL
VHLQPGQIRV VDGRLTVLRT IQLRPPQQVN LILSSNRGRR TLLLKIPKEY DLVLLFNMEE
ERQALVENIR AALKENGLSF QEWELREQEL MRAAVTRQQR GHLLETFFRH LFSQVLDINQ
ADAGTLPLDS STKVREALTC ELSRAEFADS LGLKPQDMFV ESMFSLADKD GNGYLSFREF
LDILVVFMKG SPEEKSRLMF RMYDFDGNGL ISKDEFIRML RSFIEISNNC LSKDQLAEVV
ESMFRESGFQ DKEELTWEDF HFMLRDHDSD LRFTQLCVKG VEVPEVIKNL CRRASYISQE
KICPSPRMSA HCARNNTKTA SSPQRLQCPV DTDPPQEIRR RFGKKVTSFQ PLLFTEAHRE
KFQRSRRHQT VQQFKRFIEN YRRHIGCVAV FYTITGALFL ERAYYYAFAA HHSGITDTTR
VGIILSRGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY IPFDAAVDFH RFIASTAIIL
TVLHSAGHVV NVYLFSISPL SVLSCLFPDL FHDDGSEFPQ KYYWWFFQTV PGLTGVLLLL
ALAIMYVFAS HHFRRRSFRG FWLTHHLYIF LYILLIIHGS FALIQMPRFH IFFLVPAIIY
VGDKLVSLSR KKVEISVVKA ELLPSGVTHL RFQRPQGFEY KSGQWVRIAC LALGTTEYHP
FTLTSAPHED TLSLHIRAAG PWTTRLREIY SPPTGDTCAR YPKLYLDGPF GEGHQEWHKF
EVSVLVGAGI GVTPFASILK DLVFKSSVSC QVFCKKIYFI WVTRTQRQFE WLADIIREVE
ENDSRDLVSV HIYITQLAEK FDLRTTMLYI CERHFQKVLN RSLFTGLRSV THFGRPPFEP
FFNSLQEVHP QVRKIGVFSC GPPGMTKNVE KACQLINKQD RTHFSHHYEN F
