ID A0A3B3QDA1_9TELE Unreviewed; 524 AA.
AC A0A3B3QDA1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=NADPH oxidase 3 {ECO:0000313|Ensembl:ENSPKIP00000003590.1};
GN Name=NOX3 {ECO:0000313|Ensembl:ENSPKIP00000003590.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000003590.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000003590.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A3B3QDA1; -.
DR Ensembl; ENSPKIT00000027551.1; ENSPKIP00000003590.1; ENSPKIG00000020313.1.
DR GeneTree; ENSGT00940000160501; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 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; IPR000778; Cyt_b245_heavy_chain.
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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR PANTHER; PTHR11972:SF12; NADPH OXIDASE 3; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..359
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 524 AA; 59131 MW; 1C4A1670DD3D3B17 CRC64;
IMNLIINEGV SVFMVSGLAF ARASATCVNL NCMVILLPVS RNLVSLLRGS CTCRCRVLRK
QLDKNITFHR VVGYLLVFHS VVHVIAHLSN IERYHESQST EAGELLLKLS SLGDRLNESF
LNPIRTYNTV SGQWQVLVNV SGLSGLVITL VLALMVTSST EFIRRSSYEV FWFTHHFFVV
FLVGLVIHGI GGIVRGQTAE SLLMHNVSYC REHLDEWGDV DQCPLPHFRG SDPASWKWII
APSLLYICER ILRFTRSLQP VAITKVVTHP SNVVELQMTK TGFRMEPGQY VYLQCPAIAP
LEWHPFTLTS APEEDHFSVH VRVAGDWTAA LYATYTGHQG DSRIPHLAVD GPFGSASRDV
FRYEVSVCIA AGIGVTPFAS VLKSLQYKSS NPRKLYFFWI CRDTTAFEWF RDLLLSLEGD
TTGTGRLVSF HIYLTSWDDA QARHITLHRD SQRDVVTGFR EKTFFGRPNW DQEFRSIADS
HPGSNIGVFL CGPKAISKVI RKMCSTHSTS TLRGVHFHFN KERF
//
