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   04-NOV-2026, entry version 182.
DE   RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212};
DE            Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212};
DE            Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212};
DE            EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
GN   Name=ccr1; ORFNames=SPBC29A10.01, SPBC365.17;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1417773; DOI=10.1042/bj2870195;
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 pombe
RT   cDNA.";
RL   Biochem. J. 287:195-200(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   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., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   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   PubMed=10759889; 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 to
CC       cytochrome P450 in microsomes. It can also provide electron transfer to
CC       heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 oxidized [cytochrome P450] + NADPH = 2 reduced [cytochrome
CC         P450] + NADP(+) + H(+); Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627,
CC         Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03212};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03212};
CC       Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03212};
CC       Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_03212}. Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
CC       Cell membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side
CC       {ECO:0000255|HAMAP-Rule:MF_03212}.
CC   -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03212}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family. {ECO:0000255|HAMAP-Rule:MF_03212}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC       Rule:MF_03212}.
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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; NM_001021956.3.
DR   AlphaFoldDB; P36587; -.
DR   SMR; P36587; -.
DR   BioGRID; 277553; 29.
DR   FunCoup; P36587; 623.
DR   STRING; 284812.P36587; -.
DR   iPTMnet; P36587; -.
DR   PaxDb; 284812-P36587; -.
DR   GeneID; 2541038; -.
DR   KEGG; spo:2541038; -.
DR   PomBase; SPBC29A10.01; ccr1.
DR   VEuPathDB; FungiDB:SPBC29A10.01; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_001570_17_3_1; -.
DR   InParanoid; P36587; -.
DR   OMA; AADFYQF; -.
DR   PhylomeDB; P36587; -.
DR   BRENDA; 1.6.2.4; 5613.
DR   Reactome; R-SPO-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-SPO-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR   Reactome; R-SPO-203615; eNOS activation.
DR   Reactome; R-SPO-392154; Nitric oxide stimulates guanylate cyclase.
DR   Reactome; R-SPO-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-SPO-5578775; Ion homeostasis.
DR   Reactome; R-SPO-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-SPO-9033241; Peroxisomal protein import.
DR   Reactome; R-SPO-9856530; High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells.
DR   PRO; PR:P36587; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:PomBase.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IMP:PomBase.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; ISS:PomBase.
DR   CDD; cd06204; CYPOR; 1.
DR   FunFam; 1.20.990.10:FF:000009; NADPH--cytochrome P450 reductase; 1.
DR   FunFam; 2.40.30.10:FF:000111; NADPH--cytochrome P450 reductase; 1.
DR   FunFam; 3.40.50.360:FF:000075; NADPH--cytochrome P450 reductase; 1.
DR   FunFam; 3.40.50.80:FF:000001; NADPH--cytochrome P450 reductase 1; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 1.20.990.10; NADPH-cytochrome p450 Reductase, Chain A, domain 3; 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; 2.
DR   HAMAP; MF_03212; NCPR; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR023208; P450R.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF000208; P450R; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Endoplasmic reticulum; FAD; Flavoprotein; FMN;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; NADP; Oxidoreductase; Reference proteome;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..678
FT                   /note="NADPH--cytochrome P450 reductase"
FT                   /id="PRO_0000167609"
FT   TOPO_DOM        1..5
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   TOPO_DOM        27..678
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   DOMAIN          53..208
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   DOMAIN          267..514
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         59..64
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         110..113
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         156..165
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         191
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         285
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         441..444
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         459..461
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         476..479
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         540
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         602..603
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         608..612
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         644
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         678
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
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
//