ID A0A340Y187_LIPVE Unreviewed; 1549 AA.
AC A0A340Y187;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
GN Name=DUOX1 {ECO:0000313|RefSeq:XP_007467093.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007467093.1};
RN [1] {ECO:0000313|RefSeq:XP_007467093.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00003796}.
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 Evidence={ECO:0000256|ARBA:ARBA00000518};
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 Evidence={ECO:0000256|ARBA:ARBA00000547};
CC -!- PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005197}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC family. {ECO:0000256|ARBA:ARBA00005644}.
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DR RefSeq; XP_007467093.1; XM_007467031.1.
DR STRING; 118797.A0A340Y187; -.
DR GeneID; 103076766; -.
DR KEGG; lve:103076766; -.
DR CTD; 53905; -.
DR InParanoid; A0A340Y187; -.
DR OrthoDB; 367877at2759; -.
DR UniPathway; UPA00194; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:UniProtKB-UniPathway.
DR CDD; cd09820; dual_peroxidase_like; 1.
DR CDD; cd00051; EFh; 2.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
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; 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; DUAL OXIDASE 1; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1549
FT /note="NAD(P)H oxidase (H2O2-forming)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016397725"
FT TRANSMEM 596..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1045..1067
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1079..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1149..1170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1182..1208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1228..1261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 813..848
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 849..884
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1269..1375
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 129..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1549 AA; 176627 MW; C0F3461F56D364C1 CRC64;
MGFRLALAWT LLVGPWVPMG AQNPISWEVQ RSDGWYNNLM EHRWGSKGSP LHRLIPASYA
VGVYQPFREP HLPNPRALSN TAMRGPAGQA SLRNHTVLGV FFGYHVLSDL VSVEKPGCPA
EFLNIHIPPG DPVFDRDQNG DVVLPFQRSR WDPETGQSPS NPRDQTNEAT GWLDGSAIYG
SSHSWSDELR SFNGGQLASG PDPAFPRNAQ DPLRMWTAPD PATGRRGPRG LYAFGAERGN
REPFLQALGL LWFRYHNLWA QRLARQHPLW GDEELFQHAR KRVIATYQNI AMYEWLPSFL
QQAPPNYTEY RPFLDPSISP EFLAASEPFF STMVPPGVYM RNASCHFQGV INRNSSVSRA
LRVCNSYWSR EHPNLQRAED VDSLLLAMAS QIAEREDHVV VEDSVSHPDF WPGPLKFSRT
DHLASCLQPG RDLVLPSYTE ARATLGLPPV TRWQDVNPAL FRSDGTVLEA TAALFSQDWS
RLELLPGGLL ESHGDPGPLL STIVLHQFVR LRDGDRYWFE NSGNGLFSEK EVAEVGNTSL
QDVLVAVTNV NPGALQPNVF FWHAGDPCPQ PRQLSTEGLP ACAPRIMRDY FEGSGFGFGV
TIRILCCFPL VSLLSAWIVA QLWRRYLKRI QGQNRQSIVS EKLVGSMKAS EWQGRKEPCR
PVLVHLQPWQ IHVVGGRLSE LCTVQLRPLQ QVHLILSSNR GRRAVLLRIR KDYDLVLLFD
LGEEMLENLR GPLKESGLSF QEWGLQELMS AAMTREQRSH LLEAFFRHLF SRVLDIDQAD
TDTLPLDLSQ KVQEALMCEL SRAEFAESLG LKPQDVFVES MFSLADQDGN GYLPFREFLD
VLVVFMKGSP EEKSRLMFRM YDXDGNGLIS KDEFIRMLRS FIEISSNCLS KAQLAEVVES
MFQESGFQDK QELTWEDFHF MLQDHDNELR CTQLCVKGVE VPEVIKDLCQ XASYISQGKL
CPSPRVSAHC PRRDADVKVG LTTWRMQCLM DTDPPQEIQR RFDKKVMSFQ PLLFTEAHRE
KFQRNRGHQT VQQFKRFVEN YQRHIGCLAV FYPIAGVLFL ERTYYYAFEA HHVGITDTTL
VGIILSXGTA ASISFMFSYI LLTMCRNLIT FLRETFLNRY VPFNAAVDFH CLIASTVIVL
PXHSAGRAVN VYLFSISPLS ILSCLLPGLF HDNGSEFPQK CYWWFFQLLP GPTGVMLLLV
LTVMYVFASH HFRRRSFRGF WLTHNLYILL YVLLIIHGSF ALVQLPHFHI FFLVPVLIYM
GDKLVSLSRE KVEISVVKAE LLPSGVTRLE FQRPQGFEYK SGQWVPITCL ALGTNEYHPF
ILTSAPHEDT LSLHIRAAGP WTTRLREIYS PPTGDSCTKH PKLYLDGPFG EGHQEWHKFE
VSVLVGGGIG VTPFASILKD LVFKSSLGSQ MLCKKTYFIW VTRTQRQFEW LADIIREVEE
NDHQDLVSVH IYVTQLAEKF DLRTTMLYIC ERHFQKVLNR TVFTGLRSIT HFGRPPFEPF
FDSLREVHPK VKDRGVSCDP RGMTKNVEKA CQLINREDGI HFSHHHENF
//
