ID A0A2Y9D3V5_ANOQN Unreviewed; 1142 AA.
AC A0A2Y9D3V5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=NADPH oxidase 5 {ECO:0008006|Google:ProtNLM};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA016945-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA016945-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA016945-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; A0A2Y9D3V5; -.
DR STRING; 34691.A0A2Y9D3V5; -.
DR EnsemblMetazoa; AQUA016945-RA; AQUA016945-PA; AQUA016945.
DR VEuPathDB; VectorBase:AQUA016945; -.
DR Proteomes; UP000076407; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 2.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 2.
DR Gene3D; 1.10.238.10; EF-hand; 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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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:SF58; NADPH OXIDASE 5; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
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 287..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..165
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 166..201
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 487..606
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 639..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1142 AA; 128889 MW; 4E298E4A6C54828D CRC64;
MDNENFLVQD KWIEHLKGRL TDEKQIDFAE QLESVAYVLC GDGTVTYDKF CQIWHAKGIL
DKLYRLIDVD CTNLISTNQI MEFISNLTNS RPRTGFDKSS LERLEQLFIK TVGNEKEIRR
EEFKKIVTSK NPFFTERVFQ IFDKDNSGSI SLQEFIDAIH QFAGQSPEDK IKFLFKVYDL
DGDGLIQHRE LQHVMRACME ENGMRFSEDQ IEDLTMAMFE DADKYNRGAI TYEALKNQLE
KHGGLLENLS ISIDRWLVPL PQEDTKKKRK KKPLPHQLTA PYIKNNYVYL SFLTVFTLIN
VGLFVSRAIQ YRNSNGFVIM ARACGQCLNF NCAFILVLML RQCITFLRTR GFTAFLPLDQ
HIYLHKLTGV LVAIFSLVHT IMHLFNFTTI VVYDPVLNAN NYTTAEWLFT ARPGLFGLIG
GCANPTGVVL VLILLIMFIC SQPFVRRGGS FEVFYWTHLL YVPFWILVLF HGPNFWKWFI
VPGLIYLVER TIRLVWMRTE HGKTYISSGL LLPSKVTHLV IKRPLHFCFR PGDYVFVNIP
AIAQYEWHPF TLSSAPEQED YIWLHIRGVG EWTNRLHNFF EREQERLHNG EIPALVAGSS
GSASVAAVAA SAKATGGTVD VIQEKLKSTP VATIHKSSSY ESALNKAKPS GVGGAGGPGG
PRAGDATTPA GIMKQRHPPG TSKLAMEGYS APSPVATSTA QPAKFERQMS DNRAFKKIQA
TLQRTFSRRD QLIPRSGGAG GVGGIANEGF SGDGADGGAD GSELKDAKRK VTPEQSLHKL
IFQQKVPLEK SLSMPDMQNK FKKRERMMVL REYMRSESER SFDEVQIRKA RLQSLGLAYL
SPQNKSLAQS FRYMRNKPTI IAFKTPSLEN CEPRDSTNSI VVSPGVFTQK DAEEGRTAGA
LPTSGPASSV VAVGSGAASA ASSNPASRPV NYPVGKPLEI YIDGPYGAPS SHIFQAQHAI
LIATGIGVTP FASILQSIMH RYWKARHCCP RCSYEWSSEI PPTIMNLRKV DFFWINRDQR
SFEWFVNLLS QLEIEQAELG SAMERFLEMH MYITSALQKT DMKAVGLQLA LDLLHEKEKR
DLITGLKTRT NAGRPNWDKV FKQIQDQKKG KVTVFYCGPP QLAKTLRYKC DQFGFQFRKE
VF
//
