ID V3ZR91_LOTGI Unreviewed; 1551 AA.
AC V3ZR91;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
GN ORFNames=LOTGIDRAFT_235234 {ECO:0000313|EMBL:ESO86842.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO86842.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO86842.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the peroxidase
CC family. {ECO:0000256|ARBA:ARBA00005644}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB202990; ESO86842.1; -; Genomic_DNA.
DR RefSeq; XP_009062536.1; XM_009064288.1.
DR STRING; 225164.V3ZR91; -.
DR EnsemblMetazoa; LotgiT235234; LotgiP235234; LotgiG235234.
DR GeneID; 20249787; -.
DR KEGG; lgi:LOTGIDRAFT_235234; -.
DR CTD; 20249787; -.
DR HOGENOM; CLU_004482_1_0_1; -.
DR OMA; YLRHIMC; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0005886; C: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:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
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; 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:SF175; NAD(P)H OXIDASE (H(2)O(2)-FORMING); 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
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 SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1551
FT /note="NAD(P)H oxidase (H2O2-forming)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004717956"
FT TRANSMEM 588..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1046..1066
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1086..1106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1133..1154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1182..1206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1218..1241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 852..887
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 888..923
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1268..1373
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 980..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1551 AA; 179793 MW; 9E0C26BC5F7FC0CA CRC64;
MHFFTCLLSF LLISPLITVC NAEPSSLPVQ RFDGYFNNEQ RPEVGSAGRH IARNITTNYR
DHTYFPSGWD RPNPRSISNI LFKGPTGLPS YHRRSALFSF FGQFVMREVL DTDDTTCPVE
VIQTHVPRCD PDFDPDCHGN QVMPYERSAY DKRTGQSPNN PRKQINKASC FIDGSVVYGT
NAVRSSYLRE PGTGKLYCED IWGKFPKLND VQMAFTNFPG QKHKYKDQSK LWRMGDTHIY
ENPGLLSLGL VFFRYHNYQA DQIMLKNPQM SNNEVFERAR RWVIATLQKI IMYDWLPLLL
NENVQNYTGY KPRVQSEVTD IFDAAAIQYI QTLIPPAIYQ RTNKCEFLKV GKSKAGRLCN
SYWDSKDVVN VNGLEKILLG LTSQIAERED HVIVEDLRSK FYGPLFYSRH DSAMLTILKG
RDYGLPDYNT ARVKMGLEPI KNWTDVNPEL NSTLISELKM LHHDKLDKID IFTGGLLETT
RNGPGELFRH IIIDQFLRLR DGDRFWFENK QNGIFSEEEI KEIHKITLNN VIIWTSNEIE
AEHLDRDAFT VSKDHPCPQP EQLTEDQLDE CPKHVGYDFF SGSEIPYIII WTCMGLIPIA
CILVAVILAK IKKWKHKQNL KEAKFEMERK RVLRRTLSNS IVVHDTCEWR CKKEPSRNIE
LHLTSKGSIE IFSLSGSHLR CIKLVEHMTM TIYLSINKGS NVMLIQIPKE YDLIPKEYDL
IPKEYDLIPK EYDLIPKEYD LIPKEYDLVL VFNSELNRNV FDEDLSQFLA SYEIETDLKE
KKLKDIYSMA MTKEKRNKQL EKFFKTVFTE AFKLDYDPAF EQNQLDMKTQ SKEILEMELS
KEEFAEALAV KPDSDFINHF FSLIDADRNG YISFREFLHA VVLFSKGSCQ DKLQTIFYMY
DAEGSGRMNR YNVCKMFSSL LELAQSNVEQ DEVEELVDSL CDKAGVASDQ DLCFENFCQI
FAPQMDKLWN ASIDWKGCKD HLPSQPKSKD RKQSEGEIRH RHSVPNEKNN ASFKNFTQVS
VREHYTPFKA KVKVIKHFIE NYRQHIFFLV LVFGIVLGLF AERFYYYTVE REHSGLMRLM
SYGISITRGA AAAMSFTFSL LLLTMCRNTI TYLRSTFLNM FIPFDSHISF HKVIAWTALF
FSGLHVIGYS FNFYHLATQP TKFLCIFDSI VFRADKLPTF SFWLFGNMTG FTGVLLVVVL
CIMYVFATQT ARSHIFNLFW LTHKLFIIMY VLVILHGASI IVQKPLFFAY FIGPAALFTL
DKMISLSRKK TEINIVKAIN LPSDVTMLEF KRPPKFEYKS GQWVRIACLS HGSNEYHPFT
LTSAPHEDTL KVHIRALGPW TWNIRQTFDL ENLKDNPYPK LFLDGPYGAG QQDWYQYEVS
LLVGAGIGVT PYASILKDFV HMTSIKNTYK VKCQKLYFIW VTGSQRHFEW LIDILREVEE
IDERGMVSID IFITQFFQNF DLRTAMLYVF EEHFQKMTGG KSVYTGLKAT THFGRPQLNN
IMTAVNRAHP MTRKIGVFSC GPPGVTKGVE RACVDASKST KAIFEHHYEN F
//
