ID A0A3B3ZTC3_9GOBI Unreviewed; 1469 AA.
AC A0A3B3ZTC3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000007556.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000007556.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}. 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}.
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DR STRING; 409849.ENSPMGP00000007556; -.
DR Ensembl; ENSPMGT00000008039.1; ENSPMGP00000007556.1; ENSPMGG00000006095.1.
DR UniPathway; UPA00194; -.
DR Proteomes; UP000261520; 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; 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; PF00036; EF-hand_1; 1.
DR Pfam; PF13833; EF-hand_8; 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; 2.
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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 TRANSMEM 578..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 969..988
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1000..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1047..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1102..1127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1139..1161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 781..816
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 817..852
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1188..1294
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1469 AA; 168120 MW; E25D2473ACEAE2A9 CRC64;
CPLMSRSEVA WEVSRFDGWY NSLACPKRGA VGSHLVRLLP ARFWDGVYQP IQEPQLPNPR
ALSRVLTQGP SGLPSTRNQT VLSLFFGYHV TFEIFDSRNP GCPPEFMNIP VPKGDPIFDP
SSTGKVLLPY QRTQYAEETG QSPSNPRIQL NLVSAWIDGS SIYGHSSSWS DSLRSFSGGL
LASGSERDMP RLESGLRFMW SAPNPSTREH GTNGLYGEDP INTNMFTAAE GIIWFRYHNY
VASKLHEEHP EWSDERLFQN ARKTVVATFQ NIVAYEWLPA YLGDKMLSAY PGYQKFVDPG
ISPEFQVAAI RFGITMAPPG VYMRNKTCNF REIINSDGRP SPAIRLCNSF WIRQSPNMKT
SQDIDELIMG MASQISEKED NIVVEDLRDF MYGPLRFTRT DLVALTINRG RDFGLPTYTE
VRKAFDLPLL KTIKDINPEL YRANPQLLKG IAELYDADIS KLELFVGGLL ESVDGPGPVF
SAIILDQFER IRNGDRFWFE NKQNGLFTDE EIQIIRNTTF HDVIVAVTSS GSTDIQENVF
FWTNGDPCPQ PTQLTASALQ PCTNATKLNY FDGDKAGFIF FITVLILFPF VSLLVAWLVA
ILKKYKYNKL QRERKSVNRT DEPTFDEKSR VHVFDRAGPA LRTLYVGNQD CLDIILSNDC
QRKALLLKVP KEYDLVLFFD DENMRSLFVN NLCSESLEGA GIGKKVTMRE MRERDLLKEA
LTKEQRERIV ETFIRQAFSK VLEIDRGEAG DMSGVSHQKA KEVLQCELTA SEFAEALSLK
PDSLFVESMF TLADKDGNGY LSFQEFLDVI VIFMKGSSEE KSKLMFAMND IDRNGYLSKD
EFVRMLRSFF EISNGSLSKT QADDGIKALM QAGGFENKEK ITWQDFHFLL QDHEKELQFA
QINVKGLTQI CSALPPPFEK VCLFLFIYLF YFRLHIKTPN IYVKPKREQY IKNPVQQKVQ
QFKRFVENYR RHIVCFLFVY GITAGVTIER CYSTGMPEVS AVGVIVARGS AAAISFLFPY
RNLITICRET FLNHYIPFDA AIDFHRFMAM TAIVLSVVHT LGHIINIYVF SVSNLSILSC
LFPRVFSNNG YVKSKLPPKW SWWFFETVPG ITGILLLIVF SIMYVFASHY FRRISFRGFW
ITHYLYVIVY ILVMIHGSFA LLQEPRFHIF LIPPALLFLL DKLISLNRKK VEIPVIRAEL
LPSGVTHLEF KKPQGFVYRS GQWVRVACLM LGTDEYHPFT LTSAPHEETL SLHIRAVGPW
TSRLREIYTE ESLLEFGAYP KLYLDGPFGE GHQEWVDFEV SVLVGGGIGV TPFASILKDL
VFKSSIKSKF LCKKVYFIWV TRTQRQFEWV SDIIREVEEL DTQELVSVHT YITQVAEKFD
LRTTMLYVCE RHFQKVWNRS LFTGLRSVTH FGRPPFVSFF SSLQEVHPEV AKIGVFSCGP
PGLTKNVEKA CQQMNKRDQA HFVHHYENF
//
