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Database: UniProt
Entry: A0A3P8N8G1_ASTCA
LinkDB: A0A3P8N8G1_ASTCA
Original site: A0A3P8N8G1_ASTCA 
ID   A0A3P8N8G1_ASTCA        Unreviewed;       566 AA.
AC   A0A3P8N8G1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=NADPH oxidase 1 {ECO:0000313|Ensembl:ENSACLP00000001044.1};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000001044.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000001044.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000001044.1}
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; A0A3P8N8G1; -.
DR   STRING; 8154.ENSACLP00000001044; -.
DR   Ensembl; ENSACLT00000001073.1; ENSACLP00000001044.1; ENSACLG00000000762.1.
DR   GeneTree; ENSGT00940000165729; -.
DR   OMA; MEIHENQ; -.
DR   OrthoDB; 367877at2759; -.
DR   Proteomes; UP000265100; Chromosome 2.
DR   Bgee; ENSACLG00000000762; Expressed in zone of skin and 6 other cell types or tissues.
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   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        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        169..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..225
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;  65561 MW;  E278EEC07C725C78 CRC64;
     MANCIVNYGF SAFILFVWMA INIFLFVYFY FFYDLGPQFF YTRHLLGSAL PWARAPAAVL
     NFNCMLILLP VCRNLLSLLR GSFVRCSRTM RKQLDKNLTF HKLVAYMIAL MTAVHTIAHL
     FNLERYNNSR QGLDDELSTA LSDLADTENT TYLNPVRITN LDPQQIPTYF AFTTIAGLTG
     VVITLALILI ITSSMEVIRR SYFEVFWYTH HLFIIFFAGL VFHGAGRIVR SQQRTNPPHN
     TTFCKDHPDD WGQIPECPIP QFAGGFPQTW MYVIGPMVIY LCERLVRFIR YMQRVQYKKI
     VMRPSKVLEL QLIKNGFKME VGQYVFVNCP AISQLEWHPF TMTSAPEEDF FSVHIRSAGD
     WTDKLIEIMK KVPEGAEGPK LGVDGPFGTA SEDVFDYEVS MLIGAGIGVT PFASILKSIW
     YKFKDSDPKL RTRKIYFYWL CRETHAFEWF ADLLQVLEKE MEERGMGDFL TYKLYLTGWD
     QSHATHVMVH FDKDTDVVTG LKQKTHYGRP IWDKEFEQVR KENPTSIVGT FLCGPEALGK
     VLEKKCAKYS DVDPRKTRFY FNKENF
//
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