ID A0A3B3QM78_9TELE Unreviewed; 524 AA.
AC A0A3B3QM78;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NADPH oxidase 4 {ECO:0000313|Ensembl:ENSPKIP00000007213.1};
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:ENSPKIP00000007213.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000007213.1}
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; A0A3B3QM78; -.
DR Ensembl; ENSPKIT00000031258.1; ENSPKIP00000007213.1; ENSPKIG00000023153.1.
DR GeneTree; ENSGT00940000167196; -.
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 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:SF209; NADPH OXIDASE 4; 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 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 20..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 251..366
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 524 AA; 60219 MW; 83470F090089D661 CRC64;
MPLSWRSWIA NEGSKHFILV LWLSTNIALF WKTFVSYCSG PQHYYLHKML GVTSRKARRI
LDKRKTFHMA CGIAIGLFSV IHVSAHLANV YSFSAWYSDE FPALNLARHR GEDPRIIMFT
TVPGATGVLL VLVLFLMFTA SSYSMRVSHY DIFWYTHNLS IVFYVLLLVH VIGGVLKYQT
NVEHHPPDCF RPNRTAPGGQ NSGFVNSSQV DGLSKVCREE PQFQAHFPET WLWVSGPLCL
YCAERLYRYM RGCRPVTVAS VVRHPCRVVE VHMQKSGFRA RPGQYIVLNC PHVSSFESHP
FTLTTCPTER NATFGIHLRV LGDWTERFTD LLLAEPEVGA EILPVALQRR YPRVYVDGPF
GSPSEDVFNY EVSVCVAGGI GVTPFASVLQ ALLDDWQHHK LRRLYFIWVC RELQSFRWFA
ELLCSLHQKL WQENRPDYLN IRLYVSKERG LQSLSEGRYQ VLSARLLIGR PRWEMLFEEI
GRANKQKRVG VFCSGPKGLS TTLHKMCNSN HFGATFEYNK ESFS
//
