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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//