ID A0A3Q2ZCM7_KRYMA Unreviewed; 566 AA.
AC A0A3Q2ZCM7;
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:ENSKMAP00000001411.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000001411.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000001411.1}
RP IDENTIFICATION.
RG Ensembl;
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_017263557.1; XM_017408068.1.
DR AlphaFoldDB; A0A3Q2ZCM7; -.
DR STRING; 37003.ENSKMAP00000001411; -.
DR Ensembl; ENSKMAT00000001451.1; ENSKMAP00000001411.1; ENSKMAG00000001081.1.
DR GeneID; 108231168; -.
DR KEGG; kmr:108231168; -.
DR CTD; 27035; -.
DR GeneTree; ENSGT00940000165729; -.
DR OMA; MEIHENQ; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000264800; 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 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:UP000264800};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..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 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..393
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 566 AA; 65558 MW; E940E97379B0DE9E CRC64;
MGNKIINIGF SAFIIFVWMA INIFLFVWYY FYYDLRPEFF YTRHLLGAAL AWARAPAAVL
NFNCMLILLP VCRNLLSLIR GSLMCCSRTM RKQMDKNLTF HKLVAYMIAL MTAVHMIAHL
LNLEWYNNSR QGMYDDLSNA LSDMEDTDNT TYLNPIRTTS SIHPQQIPTY FAFTSIAGIT
GVIITLALIL IITSSMEFIR RSYFEVFWYT HHLFVIFFAG LVIHGIGGIV RRQSNVDDHN
FTFCRNLTED WGKIPECPHP RFVGGPAATW WWVIGPMIIY TCERLLRLIR YAQKVQYRKI
VMRPSKVLEL QLVKKGFKME VGQYVFLNCP AISQLEWHPF TMTSAPEEDF FSVHIRSAGD
WTDKLIEIMQ KLPEGAQGPK MGVDGPFGTA SEDVFDYEVS MLVGAGIGVT PFASILKSIW
YKFKDNNPKL HTRKIYFYWL CRETHAFEWF ADLLQGQEKE MEERGLGDLL TFKLFLTGWD
ESHTNHVMVH FDEDTDVVTG LKQKTHYGRP NWDKEFEQVR KENPTATVGT FLCGPAALAT
VLEKKCAKYS DVDPRKTKFY FNKENF
//
