ID A0A2Y9L7F3_ENHLU Unreviewed; 567 AA.
AC A0A2Y9L7F3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=NADPH oxidase 1 isoform X3 {ECO:0000313|RefSeq:XP_022377365.1};
GN Name=LOC111159214 {ECO:0000313|RefSeq:XP_022377365.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022377365.1};
RN [1] {ECO:0000313|RefSeq:XP_022377365.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022377365.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_022377365.1; XM_022521657.1.
DR AlphaFoldDB; A0A2Y9L7F3; -.
DR STRING; 391180.A0A2Y9L7F3; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000248482; 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: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 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:UP000248482};
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 106..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 287..394
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 567 AA; 65552 MW; 0A3DC16B53BFE37B CRC64;
MGNWVVNHWF SVLFLLSDAT WLGLNIFLFV HAFQSYEKAD KYYYTREVLG SALAWARASA
RCLNFNSMLI LLPVCRNLLS FLRGTCSFCR RTLRKQLGHN LTFHKLVAYM ICLLTVIHII
AHLFNFEHYN RSRQARDGSL AFVLSTLSHK EKREDSWLNP LQSPNMTVEY VTFTSIAGLT
GLIITVALVL MVTSAMEFIR RSYFEVFWYT HHIFIIYIIG LGIHGIGGLV RGQTEESLNE
SHPHRCAESF KHWDDQESHC KHPQFEGLPA ESWKWILAPG VLYIFERILR FYRSQQKVVI
TKVVMHPSKV LELQMNKRGF SMEVGQYIFV NCPSISYLEW HPFTLTSAPE EDFFSIHIRA
AGDWTENLIR VFEQQPSPIP RIEVDGPFGT VSEDVFQYEV AVLVGAGIGV TPFASILKSI
WYKFRHADHN LKTQTIYFYW ICRETGAFAW FNNLLASLER EMEELGKVDF LNYRLFLTGW
DSNIAGHATL NFDKATDILT GLKQKTSFGR PMWDNEFSTI ANAHPRSVVG VFLCGPQTLA
KSLSKRCHQY SSLDPRKVQF YFNKENF
//
