ID A0A2K5DM26_AOTNA Unreviewed; 515 AA.
AC A0A2K5DM26;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=NADPH oxidase 1 {ECO:0000313|Ensembl:ENSANAP00000022008.1};
GN Name=NOX1 {ECO:0000313|Ensembl:ENSANAP00000022008.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000022008.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000022008.1}
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; A0A2K5DM26; -.
DR Ensembl; ENSANAT00000039900.1; ENSANAP00000022008.1; ENSANAG00000028753.1.
DR GeneTree; ENSGT00940000161632; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IEA:UniProt.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:UniProt.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 2.
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 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 284..391
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 515 AA; 58911 MW; 78FA35313B1230D7 CRC64;
MGNWVVNHWF SVLFLAVWFG LNVFLFVDAF LKYEKADKYY YTRKILGSTL ACARASALCL
NFNSMLILLP VCRNLLSFLR GTCSFCSRTL RKQLDHNLTF HKLVAYMICL HTAIHIIAHL
FNFDCYSRSR QATDGSLASI LSGLSHDEKK GGSWLNPIQS PNMTVKYVTF TSIAGLTGVI
MTIALILMVT SATEFIRRSY FEVFWYTHHL FIFYILGLGI HGIGGIVRGQ TEKSMKESHP
CKCAESFEMW DDRDSHCKRP EFEGHPPESW KWILAPVILY ICERILRFYR SQQKVVITKV
VMHPSKVLEL QMNKRGFSME VGQYIFVNCP SISLLEWHPF TLTSAPEEDF FSIHIRAAGD
WTENLIRAFE QQYSTIPRIE VDGPFGTASE DVFQYEVAVL VGAGIGVTPF ASILKSIWYK
FQCADHNLKT KKVGHAALNF DKATDILTGL KQKTSFGRPM WDNEFSKIAT SHPKSVVGVF
LCGPQILAKS LRKCCHRYSS LDPRKVQFYF NKENF
//
