ID   NCPR_SCHPO              Reviewed;         678 AA.
AC   P36587; Q9USU6; Q9UU68;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   22-JUL-2008, entry version 74.
DE   RecName: Full=NADPH--cytochrome P450 reductase;
DE            Short=CPR;
DE            Short=P450R;
DE            EC=1.6.2.4;
GN   Name=ccr1; ORFNames=SPBC29A10.01, SPBC365.17;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93038553; PubMed=1417773;
RA   Miles J.S.;
RT   "Structurally and functionally conserved regions of cytochrome P-450
RT   reductase as targets for DNA amplification by the polymerase chain
RT   reaction. Cloning and nucleotide sequence of the Schizosaccharomyces
RT   pombe cDNA.";
RL   Biochem. J. 287:195-200(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 128-276.
RC   STRAIN=ATCC 38364 / 968;
RX   MEDLINE=20223868; PubMed=10759889;
RX   DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
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; Single-pass
CC       membrane protein.
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; X64702; CAA45956.1; -; mRNA.
DR   EMBL; CU329671; CAB44769.1; -; Genomic_DNA.
DR   EMBL; AB027780; BAA87084.1; -; Genomic_DNA.
DR   PIR; S29123; S29123.
DR   PIR; T40056; T40056.
DR   RefSeq; NP_596046.1; -.
DR   HSSP; P00388; 1AMO.
DR   GeneID; 2541038; -.
DR   KEGG; spo:SPBC29A10.01; -.
DR   NMPDR; fig|4896.1.peg.1912; -.
DR   GeneDB_Spombe; SPBC29A10.01; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004880-MON; -.
DR   ArrayExpress; P36587; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:GeneDB_SPombe.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; TAS:GeneDB_SPombe.
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   Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; FMN;
KW   Membrane; NADP; Oxidoreductase; Transmembrane.
FT   CHAIN         1    678       NADPH--cytochrome P450 reductase.
FT                                /FTId=PRO_0000167609.
FT   TRANSMEM      6     26       Potential.
FT   DOMAIN       53    208       Flavodoxin-like.
FT   DOMAIN      267    514       FAD-binding FR-type.
FT   NP_BIND     153    184       FMN (By similarity).
FT   NP_BIND     306    317       FAD (By similarity).
FT   NP_BIND     437    448       FAD (By similarity).
FT   NP_BIND     535    553       NADP (By similarity).
FT   NP_BIND     630    646       NADP (By similarity).
SQ   SEQUENCE   678 AA;  76775 MW;  6AEDDFBA6DE39C8F CRC64;
     MKTYEYVLLV IILILSLCYF IYNNFLNKPK APERRVVATD SIVELMEAEK LTAAVFFGSQ
     TGTAEDFAYR FSTEAKANFN LTNMVFDLEN YDLTDLDNFD RSKLLVFFLA TYGEGEPTDN
     AEAFLQLLEG DDTVFSSGKG IEDTPFEGIR YAIFGLGNHT YEYYNAMAKK VDAAMTRLGA
     TRVGNLGLGD DAAGMLEEDY LQWKDDTLPE IGKLFHLQEV HKEYNPMFEV IEKPEISNTS
     STVFLGEPSR QQLKGNVASK APRSQANPFF SSPVRSLELF KSGSRNCLHL ELDIADSGMR
     YQTGDYASIC PMNPSQAVDD LLEVLGLKEK RDTVIIVKPI DTLDKAPVLS PTTYDTVFRY
     YYEICGIVSR QLLSFIAPFA PTPESKQELE KLGNDYDYFK KNVVDLHLNL AQVLRRVSPD
     APFTKLPFSM LLENMAHMKP RYYSISSSSV VHPDKVHVTA VVDKKEWTDK NHIFYGLTTN
     YLLAHCRHMH GEKIPHPNGL EYTLEGPRKN WTGKIPMFVK KSTFRLAPPD VPIIMVGPGT
     GVAPFRGFVM ERANLASKGV KVAKTLLFYG CQYSDKDFLY KEEWQQYKDV LKDSFELITA
     FSREQDHKIY VQHRLLEHSD TIAKLVEEGA AFYICGDADH MAKDVVNALA SILTTVDVDG
     MKAVKALRDD NRFFEDTW
//