ID   NCPR_MUSDO              Reviewed;         671 AA.
AC   Q07994;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-NOV-2008, entry version 65.
DE   RecName: Full=NADPH--cytochrome P450 reductase;
DE            Short=CPR;
DE            Short=P450R;
DE            EC=1.6.2.4;
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Rutgers; TISSUE=Abdomen;
RX   MEDLINE=93284260; PubMed=8508186; DOI=10.1016/0965-1748(93)90051-S;
RA   Koener J.F., Carino F.A., Feyereisen R.;
RT   "The cDNA and deduced protein sequence of house fly NADPH-cytochrome
RT   P450 reductase.";
RL   Insect Biochem. Mol. Biol. 23:439-447(1993).
CC   -!- FUNCTION: This enzyme is required for electron transfer from NADP
CC       to cytochrome P450 in microsomes. It can also provide electron
CC       transfer to heme oxygenase and cytochrome B5.
CC   -!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
CC       reduced hemoprotein.
CC   -!- COFACTOR: FAD.
CC   -!- COFACTOR: FMN.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Note=Anchored to the ER membrane by its N-
CC       terminal hydrophobic region.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development, with high
CC       levels before metamorphosis and low levels in pupae.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; L19897; AAA29295.1; -; mRNA.
DR   PIR; A56592; A56592.
DR   HSSP; P00388; 1AMO.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR001094; Flavdoxin_like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; FPN_cyt_redctse.
DR   InterPro; IPR015702; NADPH_Cyt_Red.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   PANTHER; PTHR19384:SF17; NADPH_Cyt_Red; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    671       NADPH--cytochrome P450 reductase.
FT                                /FTId=PRO_0000167603.
FT   DOMAIN       77    221       Flavodoxin-like.
FT   DOMAIN      276    515       FAD-binding FR-type.
FT   NP_BIND     167    198       FMN (By similarity).
FT   NP_BIND     311    322       FAD (By similarity).
FT   NP_BIND     448    458       FAD (By similarity).
FT   NP_BIND     524    542       NADP (By similarity).
FT   NP_BIND     618    634       NADP (By similarity).
SQ   SEQUENCE   671 AA;  76358 MW;  A00A2C35DFD8D129 CRC64;
     MSAEHVEEVV SEEPFLGTLD IALLVVLLVG ATWYFMRSRK KEEAPIRSYS IQPTTVSTVS
     TTENSFIKKL KASGRSLVVF YGSQTGTAEE FAGRLAKEGL RYRMKGMVAD PEECDMEELL
     QMKDIPNSLA VFCLATYGEG DPTDNAMEFY EWITNGEVDL TGLNYAVFGL GNKTYEHYNK
     VAIYVDKRLE ELGATRVFEL GLGDDDANIE DDFITWKDRF WPSVCDFFGI EGSGEEVLMR
     QFRLLEQPDV QPDRIYTGEI ARLHSMQNQR PPFDAKNPFL ASVIVNRELH KGGGRSCMHI
     ELDIDGSKMR YDAGDHIAMY PINDKILVEK LGKLCDANLD TVFSLINTDT DSSKKHPFPC
     PTTYRTALTH YLEITAIPRT HILKELAEYC SDEKDKEFLR NMASITPEGK EKYQNWIQNS
     SRNIVHILED IKSCRPPIDH ICELLPRLQP RYYSISSSSK LYPTNVHITA VLVQYETPTG
     RVNKGVATSY MKEKNPSVGE VKVPVFIRKS QFRLPTKSEI PIIMVGPGTG LAPFRGFIQE
     RQFLRDGGKV VGDTILYFGC RKKDEDFIYR EELEQYVQNG TLTLKTAFSR DQQEKIYVTH
     LIEQDADLIW KVIGEQKGHF YICGDAKNMA VDVRNILVKI LSTKGNMNES DAVQYIKKME
     AQKRYSADVW S
//