ID   A0A3Q4HWZ5_NEOBR        Unreviewed;       525 AA.
AC   A0A3Q4HWZ5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=NADPH oxidase 1 {ECO:0000313|Ensembl:ENSNBRP00000028535.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000028535.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000028535.1}
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; A0A3Q4HWZ5; -.
DR   STRING; 32507.ENSNBRP00000028535; -.
DR   Ensembl; ENSNBRT00000029279.1; ENSNBRP00000028535.1; ENSNBRG00000021722.1.
DR   GeneTree; ENSGT00940000165729; -.
DR   OMA; MEIHENQ; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000021722; Expressed in zone of skin and 1 other cell type or tissue.
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:SF71; NADPH OXIDASE 1; 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   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 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   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          277..383
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   525 AA;  61243 MW;  1A9C2AF6FB786F8E CRC64;
     CNHCVMEIWF WLCLQFVWMA INIFLFVYFY FFYDLGPQFF YTRHLLGSAL PWARAPAAVL
     NFNCMLILLP VCRNLLSLLR GSFVRCSRTM RKQLDKNLTF HKLVAYTIAL MTAVHTIAHL
     FNLERFNNSR QGLGDELSAA LSELADTENT TYLNPIPTYF AFTTIAGLTG VVITLALILI
     VTSSMEVIRR SYFEVFWYTH HLFIVFFAGL VFHGAGRIVR SQQRTNPPHN TTFCKDRPDD
     WGRIPECPIP QFAGGFPQTW MYVIGPMVIY LCERLVRFIR YMQRVRYKKI VMRPSKVLEL
     QLIKNGFKMD VGQYVFVNCP AISQLEWHPF TMTSAPEEDF FSVHIRSAGD WTDKLIEIMK
     KVPEGAEGPK LGVDGPFGTA SEDVFDYEVS MLIGAGIGVT PFASILKSIW YKFKDSDPKL
     RTRKIYFYWL CRETHAFEWF ADLLQVLEKE MEERGMGDFL TYKLYLTGWD QSHATHVMVH
     FDKDTDVVTG LKQKTHYGRP IWDKEFEQVH VDPRKTRFYF NKENF
//