ID A0A3Q2D4C6_CYPVA Unreviewed; 1392 AA.
AC A0A3Q2D4C6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=NAD(P)H oxidase (H2O2-forming) {ECO:0000256|ARBA:ARBA00012698};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000013144.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000013144.1}
RP IDENTIFICATION.
RG Ensembl;
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}. 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; 28743.ENSCVAP00000013144; -.
DR Ensembl; ENSCVAT00000020578.1; ENSCVAP00000013144.1; ENSCVAG00000015669.1.
DR GeneTree; ENSGT00940000163963; -.
DR OMA; YLRHIMC; -.
DR UniPathway; UPA00194; -.
DR Proteomes; UP000265020; 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; 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; 2.
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; 2.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
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 244..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..574
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..939
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 951..984
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1004..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1032..1054
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1066..1084
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 746..781
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 782..817
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1111..1217
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1392 AA; 158077 MW; 5C356CEB76E85945 CRC64;
RRPAGLKTVW RIRSAEPSVG PCAQDDRPAS PRTLTDSVFL TGSHLLRLVP ARYWDGVYQP
VHEPVQPNAR ALSRLLARGP SGLPSARNRT VLSLFFGYHV AFEIFDLRAP GCPPQFMNIK
VPKGDPVFDR NATGKVLLPF QRAQWDKQSG QSPSNPRIQV NSVTAWIDGS SIYGPSSSWS
DFLRNFSGGL LTSGSEWKMP NQGGGRNFMW SAPDPSTGEN GPQGLYGETL CCYIFCLLQD
PSSFLTFLCL LLMFAVISPG ICLLGKCALL YVFLSAGYQK FVDPGISPEF QAAAFRFGVT
MAPPGVYMRN RTCHFRKIIN IDGSESPAMR LCNSFWKRAN MKSGQDVDEL LMGMASQIAE
KEDNIVVEDL RDYLYGPLRF SRTDLVALTI QRGRDFGLQS YTETRRALDL PPVKTFEEIN
PELSRTNPQV TATQYGGDIS KLELFPGGLL ESTDGPGPVF TAIILDQFER IRNGDRFWFE
NKQNGLFTDE EIRRIRSVTY QDVLIAVTSA EPTDLQKNVF SWMSGDPCPQ PAQLEASMLH
PCTNFTTLNY FDGSQAGFGI SIIIMCLFPV GLCVERRTKT RPYEWQGHKK LLHPVSVEIE
NRRLQVFDRS GAMQRSLSLK NQDHLDIFLS SSHTHKAVLL KVPKEYDLVL FFDDESKRSE
FVSHLRLELE DMRKEIRVKE MREGELLKEA LTKEQRAQIV ETFIRHAFSK VQSASGCLPH
ILLSSREVLQ CELTASEFAD ALGLKPDSLF VDSMFTLADK DGNGYLSFQE FLDVIVIFMK
GSPEEKSQLM FSMNDIGGTG FLSKEEFARM LRSFIEISNG VLSKAQAEDG IKAMMQAAGF
DNKEKISWRD FHSLLKDHEK ELQFAQLNVK GVNKFSFGSA FAPAVYVKPK REQYIRNPVQ
QKVQQFKRFI ENYRRHIVCF IIVFGITAGV ITERCYFYSS QAEATGVPET TVMGIIIARG
TAAGISFLLP YILLTVCRNL ITLLRETFLN RYIPFDAAID LHRIMAMTAV VLSVAHSLGH
VVNVYIFCTS DLRITGVLLL FAFAFMYVFA SHYFRRISFR GFWMTHYLYV VVYILTVIHG
SYALLQEPRF HIYLIPPSLL FLLDKLISLS RKKVEIPVVR AELLLSGVTH LEFKRPKGFV
YRSGQWVRIA CLMLDTDEYH PFTLTSAPHE ETLSLHIRAV GPWTSRLREL YTEESLLELG
GYPKLYLDGP FGEGHQEWND FEVSVLVGGG IGVTPFTSIL KDLVFKSSIK SKILCKKVYF
IWVTRTQRQF EWVSDIIREV EEMDTQELVS VHTYITQVAE KFDLRTTMLY VCERHFQKVW
NRSLFTGLRS VTHFGRPPFV SFFSSLQEVH PEVGKIGVFS CGPPGLTKNV EKACQKMNKR
DQTYFLHHYE NF
//
