ID G2J629_DROME Unreviewed; 1340 AA.
AC G2J629;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=FI15205p1 {ECO:0000313|EMBL:AEO20323.1};
GN Name=Nox-RC {ECO:0000313|EMBL:AEO20323.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AEO20323.1};
RN [1] {ECO:0000313|EMBL:AEO20323.1}
RP NUCLEOTIDE SEQUENCE.
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; BT128886; AEO20323.1; -; mRNA.
DR VEuPathDB; VectorBase:FBgn0085428; -.
DR ExpressionAtlas; G2J629; baseline and differential.
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; PF13405; EF-hand_6; 1.
DR Pfam; PF13499; EF-hand_7; 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 2: Evidence at transcript level;
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 522..543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 359..394
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 395..430
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 731..844
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..893
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1340 AA; 151587 MW; 0CFE69AA36BD3415 CRC64;
MNADQESNNH RGSVSSSRSL EIPATPSRSP KKVSFSDELP QSQTPAQQPI NQQSAPTVVS
HVLQQAAQYL ERLHGARDSA EEKTEEVQPE RADIRDSSDT SEAAVLDLDA LDASADEPAA
NAGPIVASSP SILIGSVNRQ EAIGSANGNG NANPNQRQSN LYMERYNLNL DKNCSSMELE
ARREKQRWLL ISECSALFDE GEGKHTREAF RKLFLDEEFQ QKLFQLFDLE RNGYLLQDRW
IEHLKGRLTD DRQMDFAEQI ESVAYVICGE NKRVSFKNFR DIWHTRGILD KLYRLIELDG
SNLVSTNQVM EFISHLTNSR PRTGFDKSSL ARLEQLFRTT VGNEQEIRRE EFQKIVTSKN
PFFTERVFQI FDKDNSGSIS LQEFIDAIHQ FSGQSADDKI RFLFKVYDID GDGLIQHKEL
HDVIRHCIKE NGMEFSEDQI EDLTSAMFED ADPHNSGEIT YEALKNQLHK HGGLLENLSI
TIDRWLVPIA EDRQAGGAAK SGFWNSLPHQ FSLAYMKNNQ VFVTYLFFYI TVNLCLFISR
AIQYRASNGF VIIARACGQC LNFNCAWVLV LMLRHSLTYL RGRGLSSYLP LDHHVYLHKL
TGITISVLSL IHTIMHLFNF SIIVINDPNI NAGHYTIGEW LLTDRPGLFG LIPGCANPTG
VALLAILVVM FVCSQPFVRR KGSFEVFYWT HLLYVPFWIL CLFHGPNFWK WFLLPGLVYI
VERALRFIWM RGEHGKTYIS SGLLLPSKVV HLVIKRPHHF NFRPGDYVFV NIPAIANYEW
HPFTISSAPE QEDYMWLHIR TVGEWTNRLY RYFEREQQKL QQSGSSQEIP QHMHAIPTPS
FMLLNEARNP AIAGERSATP QTDFLAKNLG VQAVPPVRPP RQNRKPAPGA PIDPPATGVN
RIRSIKKTLQ RTFSRKEAVD PKKGIPNGAF IADGEREDSN LKQRPLEKSI SLPDISVKSK
KRSRLKALRA LGRSESESAF DEKRVRRARN NSVGLAYLSP QNKSLAQSFR YMRTKPTIIA
FKTPSMEERE HQVAAGEANG ASPASRAEQG QLSSRMDSAD KLQLARLSLS AEGASKPLED
QTQTGSPSRK SILRRPTFLR SLSASINNRT GGGGGGSTGS STTNSGGKVT LDAGVMEIFI
DGPYGAPSSH IFGAQHAVLI GTGIGVTPFA SILQSIMHRY WKARHSCPRC QFEWASEIPK
SVMNLRKVDF FWINRDQRSF EWFVNLLSQL EIEQAELGGA MERFLDMHMY ITSSLQRTDM
KAVGLQLALD LLHEKGKRDL ITGLKTRTNA GRPNWDKVFK QLQAQQKGKV TVFYCGPPQL
AKTLRYKCDQ YGFAFRKECF
//
