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NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4)

 NCPR_HUMAN              Reviewed;         677 AA.
P16435; Q16455; Q197M5; Q8N181; Q9H3M8; Q9UDT3;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 213.
RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212};
Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212};
Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212};
EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
Name=POR {ECO:0000255|HAMAP-Rule:MF_03212}; Synonyms=CYPOR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-500.
PubMed=1550342; DOI=10.1016/0003-9861(92)90152-M;
Shephard E.A., Palmer C.N., Segall H.J., Phillips I.R.;
"Quantification of cytochrome P450 reductase gene expression in human
tissues.";
Arch. Biochem. Biophys. 294:168-172(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Czerwinski M., Sahni M., Madan A., Parkinson A.;
"Polymorphism of human CYPOR: expression of new allele.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Murakami H.O., Ogawa H., Nisimoto Y.;
"cDNA cloning and characterization of NADPH-cytochrome P-450 reductase
in human HL-60 cell.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-225; ASN-252 AND
VAL-500.
NIEHS SNPs program;
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS LEU-225 AND
VAL-500.
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-677, CLEAVAGE OF INITIATOR METHIONINE, AND
ACETYLATION AT GLY-2.
TISSUE=Liver;
PubMed=2513880; DOI=10.1021/bi00447a054;
Haniu M., McManus M.E., Birkett D.J., Lee T.D., Shively J.E.;
"Structural and functional analysis of NADPH-cytochrome P-450
reductase from human liver: complete sequence of human enzyme and
NADPH-binding sites.";
Biochemistry 28:8639-8645(1989).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 61-241 IN COMPLEX WITH FMN.
PubMed=10048323; DOI=10.1110/ps.8.2.298;
Zhao Q., Modi S., Smith G., Paine M., McDonagh P.D., Wolf C.R.,
Tew D., Lian L.Y., Roberts G.C., Driessen H.P.;
"Crystal structure of the FMN-binding domain of human cytochrome P450
reductase at 1.93 A resolution.";
Protein Sci. 8:298-306(1999).
[13]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 232-677 IN COMPLEX WITH FAD.
PubMed=19483672; DOI=10.1038/embor.2009.82;
Aigrain L., Pompon D., Morera S., Truan G.;
"Structure of the open conformation of a functional chimeric NADPH
cytochrome P450 reductase.";
EMBO Rep. 10:742-747(2009).
[14]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 241-677 IN COMPLEX WITH FAD;
FMN AND NADP.
PubMed=21808038; DOI=10.1073/pnas.1106632108;
Xia C., Panda S.P., Marohnic C.C., Martasek P., Masters B.S.,
Kim J.J.;
"Structural basis for human NADPH-cytochrome P450 oxidoreductase
deficiency.";
Proc. Natl. Acad. Sci. U.S.A. 108:13486-13491(2011).
[15]
VARIANT ABS1 HIS-454.
PubMed=15264278; DOI=10.1002/ajmg.a.30169;
Adachi M., Tachibana K., Asakura Y., Yamamoto T., Hanaki K., Oka A.;
"Compound heterozygous mutations of cytochrome P450 oxidoreductase
gene (POR) in two patients with Antley-Bixler syndrome.";
Am. J. Med. Genet. A 128:333-339(2004).
[16]
VARIANTS ABS1 HIS-454; CYS-575 AND 608-LEU--TRP-617 DELINS ARG, AND
VARIANT VAL-500.
PubMed=15483095; DOI=10.1210/jc.2004-0810;
Fukami M., Horikawa R., Nagai T., Tanaka T., Naiki Y., Sato N.,
Okuyama T., Nakai H., Soneda S., Tachibana K., Matsuo N., Sato S.,
Homma K., Nishimura G., Hasegawa T., Ogata T.;
"Cytochrome P450 oxidoreductase gene mutations and Antley-Bixler
syndrome with abnormal genitalia and/or impaired steroidogenesis:
molecular and clinical studies in 10 patients.";
J. Clin. Endocrinol. Metab. 90:414-426(2005).
[17]
VARIANTS DISPORD ASP-178; PRO-284; HIS-454 AND TYR-566, AND
CHARACTERIZATION OF VARIANTS DISPORD ASP-178; PRO-284; HIS-454 AND
TYR-566.
PubMed=15220035; DOI=10.1016/S0140-6736(04)16503-3;
Arlt W., Walker E.A., Draper N., Ivison H.E., Ride J.P., Hammer F.,
Chalder S.M., Borucka-Mankiewicz M., Hauffa B.P., Malunowicz E.M.,
Stewart P.M., Shackleton C.H.L.;
"Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase
and human androgen synthesis: analytical study.";
Lancet 363:2128-2135(2004).
[18]
VARIANTS ABS1 PRO-284; HIS-454 AND GLU-489, VARIANTS DISPORD TYR-566
AND PHE-605, CHARACTERIZATION OF VARIANTS ABS1 PRO-284; HIS-454 AND
GLU-489, AND CHARACTERIZATION OF VARIANTS DISPORD TYR-566 AND PHE-605.
PubMed=14758361; DOI=10.1038/ng1300;
Flueck C.E., Tajima T., Pandey A.V., Arlt W., Okuhara K., Verge C.F.,
Jabs E.W., Mendonca B.B., Fujieda K., Miller W.L.;
"Mutant P450 oxidoreductase causes disordered steroidogenesis with and
without Antley-Bixler syndrome.";
Nat. Genet. 36:228-230(2004).
[19]
VARIANT HIS-454.
PubMed=27610946; DOI=10.1002/humu.23116;
Igarashi M., Takasawa K., Hakoda A., Kanno J., Takada S., Miyado M.,
Baba T., Morohashi K.I., Tajima T., Hata K., Nakabayashi K.,
Matsubara Y., Sekido R., Ogata T., Kashimada K., Fukami M.;
"Identical NR5A1 missense mutations in two unrelated 46,XX individuals
with testicular tissues.";
Hum. Mutat. 38:39-42(2017).
-!- FUNCTION: This enzyme is required for electron transfer from NADP
to cytochrome P450 in microsomes. It can also provide electron
transfer to heme oxygenase and cytochrome B5. {ECO:0000255|HAMAP-
Rule:MF_03212}.
-!- CATALYTIC ACTIVITY:
Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-
Rule:MF_03212};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:21808038};
Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:21808038};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:21808038};
Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:21808038};
-!- INTERACTION:
P00181:CYP2C2 (xeno); NbExp=4; IntAct=EBI-726554, EBI-4320576;
O00264:PGRMC1; NbExp=5; IntAct=EBI-726554, EBI-1045534;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side
{ECO:0000255|HAMAP-Rule:MF_03212}.
-!- DISEASE: Antley-Bixler syndrome, with genital anomalies and
disordered steroidogenesis (ABS1) [MIM:201750]: A disease
characterized by the association of Antley-Bixler syndrome with
steroidogenesis defects and abnormal genitalia. Antley-Bixler
syndrome is characterized by craniosynostosis, radiohumeral
synostosis present from the perinatal period, midface hypoplasia,
choanal stenosis or atresia, femoral bowing and multiple joint
contractures. {ECO:0000269|PubMed:14758361,
ECO:0000269|PubMed:15264278, ECO:0000269|PubMed:15483095}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Disordered steroidogenesis due to cytochrome P450
oxidoreductase deficiency (DISPORD) [MIM:613571]: A disorder
resulting in a rare variant of congenital adrenal hyperplasia,
with apparent combined P450C17 and P450C21 deficiency and
accumulation of steroid metabolites. Affected girls are born with
ambiguous genitalia, but their circulating androgens are low and
virilization does not progress. Conversely, affected boys are
sometimes born undermasculinized. Boys and girls can present with
bone malformations, in some cases resembling the pattern seen in
patients with Antley-Bixler syndrome.
{ECO:0000269|PubMed:14758361, ECO:0000269|PubMed:15220035}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase
family. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
family. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
pyridine nucleotide cytochrome reductase family.
{ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SEQUENCE CAUTION:
Sequence=AAH34277.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/por/";
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EMBL; S90469; AAB21814.1; -; mRNA.
EMBL; AF258341; AAG09798.1; -; mRNA.
EMBL; AB051763; BAB18572.1; -; mRNA.
EMBL; DQ640499; ABF70199.1; -; Genomic_DNA.
EMBL; AC005067; AAD45961.1; -; Genomic_DNA.
EMBL; AC006330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC034277; AAH34277.1; ALT_INIT; mRNA.
PIR; A33421; A60557.
RefSeq; NP_000932.3; NM_000941.2.
UniGene; Hs.354056; -.
PDB; 1B1C; X-ray; 1.93 A; A=61-241.
PDB; 3FJO; X-ray; 2.50 A; A=232-677.
PDB; 3QE2; X-ray; 1.75 A; A/B=64-677.
PDB; 3QFC; X-ray; 1.80 A; A/B=64-677.
PDB; 3QFR; X-ray; 2.40 A; A/B=64-677.
PDB; 3QFS; X-ray; 1.40 A; A=241-677.
PDB; 3QFT; X-ray; 1.40 A; A=241-677.
PDB; 5EMN; X-ray; 2.20 A; A/B=64-677.
PDB; 5FA6; X-ray; 2.30 A; A/B=64-677.
PDBsum; 1B1C; -.
PDBsum; 3FJO; -.
PDBsum; 3QE2; -.
PDBsum; 3QFC; -.
PDBsum; 3QFR; -.
PDBsum; 3QFS; -.
PDBsum; 3QFT; -.
PDBsum; 5EMN; -.
PDBsum; 5FA6; -.
ProteinModelPortal; P16435; -.
SMR; P16435; -.
BioGrid; 111443; 38.
DIP; DIP-29682N; -.
IntAct; P16435; 11.
MINT; P16435; -.
STRING; 9606.ENSP00000419970; -.
ChEMBL; CHEMBL2169731; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB00865; Benzphetamine.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB01466; Ethylmorphine.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB00166; Lipoic Acid.
DrugBank; DB00305; Mitomycin.
DrugBank; DB00665; Nilutamide.
DrugBank; DB00698; Nitrofurantoin.
DrugBank; DB03247; Riboflavin Monophosphate.
GlyConnect; 1535; -.
iPTMnet; P16435; -.
PhosphoSitePlus; P16435; -.
SwissPalm; P16435; -.
BioMuta; POR; -.
DMDM; 2851393; -.
EPD; P16435; -.
MaxQB; P16435; -.
PaxDb; P16435; -.
PeptideAtlas; P16435; -.
PRIDE; P16435; -.
ProteomicsDB; 53360; -.
DNASU; 5447; -.
Ensembl; ENST00000394893; ENSP00000378355; ENSG00000127948.
Ensembl; ENST00000412064; ENSP00000404731; ENSG00000127948.
Ensembl; ENST00000412521; ENSP00000409238; ENSG00000127948.
Ensembl; ENST00000414186; ENSP00000399327; ENSG00000127948.
Ensembl; ENST00000418341; ENSP00000389719; ENSG00000127948.
Ensembl; ENST00000432753; ENSP00000389409; ENSG00000127948.
Ensembl; ENST00000439963; ENSP00000390540; ENSG00000127948.
Ensembl; ENST00000449920; ENSP00000399556; ENSG00000127948.
Ensembl; ENST00000453773; ENSP00000395813; ENSG00000127948.
Ensembl; ENST00000454934; ENSP00000414263; ENSG00000127948.
Ensembl; ENST00000461988; ENSP00000419970; ENSG00000127948.
GeneID; 5447; -.
KEGG; hsa:5447; -.
UCSC; uc003udy.4; human.
CTD; 5447; -.
DisGeNET; 5447; -.
EuPathDB; HostDB:ENSG00000127948.13; -.
GeneCards; POR; -.
GeneReviews; POR; -.
HGNC; HGNC:9208; POR.
HPA; CAB004372; -.
HPA; HPA010136; -.
MalaCards; POR; -.
MIM; 124015; gene.
MIM; 201750; phenotype.
MIM; 613571; phenotype.
neXtProt; NX_P16435; -.
Orphanet; 95699; Congenital adrenal hyperplasia due to cytochrome P450 oxidoreductase deficiency.
PharmGKB; PA33532; -.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
HOGENOM; HOG000282027; -.
HOVERGEN; HBG000432; -.
InParanoid; P16435; -.
KO; K00327; -.
PhylomeDB; P16435; -.
TreeFam; TF105719; -.
BioCyc; MetaCyc:HS05140-MONOMER; -.
BRENDA; 1.6.2.4; 2681.
Reactome; R-HSA-211897; Cytochrome P450 - arranged by substrate type.
SABIO-RK; P16435; -.
SIGNOR; P16435; -.
ChiTaRS; POR; human.
EvolutionaryTrace; P16435; -.
GeneWiki; Cytochrome_P450_reductase; -.
GenomeRNAi; 5447; -.
PRO; PR:P16435; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000127948; Expressed in 207 organ(s), highest expression level in right adrenal gland.
CleanEx; HS_POR; -.
ExpressionAtlas; P16435; baseline and differential.
Genevisible; P16435; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:Ensembl.
GO; GO:0009055; F:electron transfer activity; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
GO; GO:0010181; F:FMN binding; IBA:GO_Central.
GO; GO:0016787; F:hydrolase activity; IEA:Ensembl.
GO; GO:0047726; F:iron-cytochrome-c reductase activity; IEA:Ensembl.
GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:BHF-UCL.
GO; GO:0008941; F:nitric oxide dioxygenase activity; IEA:Ensembl.
GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
GO; GO:0009437; P:carnitine metabolic process; IEA:Ensembl.
GO; GO:0090346; P:cellular organofluorine metabolic process; IDA:BHF-UCL.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
GO; GO:0070988; P:demethylation; IEA:Ensembl.
GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl.
GO; GO:0009812; P:flavonoid metabolic process; IEA:Ensembl.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; IEA:Ensembl.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0060192; P:negative regulation of lipase activity; IEA:Ensembl.
GO; GO:0043602; P:nitrate catabolic process; IEA:Ensembl.
GO; GO:0046210; P:nitric oxide catabolic process; IEA:Ensembl.
GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL.
GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IEA:Ensembl.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
GO; GO:0032770; P:positive regulation of monooxygenase activity; IDA:BHF-UCL.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IEA:Ensembl.
GO; GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IBA:GO_Central.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
Gene3D; 1.20.990.10; -; 2.
Gene3D; 3.40.50.360; -; 1.
Gene3D; 3.40.50.80; -; 1.
HAMAP; MF_03212; NCPR; 1.
InterPro; IPR003097; CysJ-like_FAD-binding.
InterPro; IPR017927; FAD-bd_FR_type.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR039261; FNR_nucleotide-bd.
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR023208; P450R.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
PIRSF; PIRSF000208; P450R; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF52343; SSF52343; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Congenital adrenal hyperplasia; Craniosynostosis;
Direct protein sequencing; Disease mutation; Endoplasmic reticulum;
FAD; Flavoprotein; FMN; Membrane; NADP; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2513880}.
CHAIN 2 677 NADPH--cytochrome P450 reductase.
/FTId=PRO_0000167596.
TOPO_DOM 2 21 Lumenal. {ECO:0000255|HAMAP-
Rule:MF_03212}.
TRANSMEM 22 42 Helical. {ECO:0000255|HAMAP-
Rule:MF_03212}.
TOPO_DOM 43 677 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03212}.
DOMAIN 80 224 Flavodoxin-like. {ECO:0000255|HAMAP-
Rule:MF_03212}.
DOMAIN 279 521 FAD-binding FR-type. {ECO:0000255|HAMAP-
Rule:MF_03212}.
NP_BIND 86 91 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:10048323,
ECO:0000269|PubMed:21808038}.
NP_BIND 138 141 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:10048323,
ECO:0000269|PubMed:21808038}.
NP_BIND 173 182 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:10048323,
ECO:0000269|PubMed:21808038}.
NP_BIND 454 457 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:19483672,
ECO:0000269|PubMed:21808038}.
NP_BIND 472 474 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:19483672,
ECO:0000269|PubMed:21808038}.
NP_BIND 488 491 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:19483672,
ECO:0000269|PubMed:21808038}.
NP_BIND 596 597 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:21808038}.
NP_BIND 602 606 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:21808038}.
BINDING 208 208 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:10048323,
ECO:0000269|PubMed:21808038}.
BINDING 298 298 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:21808038}.
BINDING 424 424 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:19483672,
ECO:0000269|PubMed:21808038}.
BINDING 478 478 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:19483672,
ECO:0000269|PubMed:21808038}.
BINDING 535 535 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:21808038}.
BINDING 638 638 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:21808038}.
BINDING 676 676 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:19483672,
ECO:0000269|PubMed:21808038}.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000269|PubMed:2513880}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 178 178 Y -> D (in DISPORD; complete loss of
activity). {ECO:0000269|PubMed:15220035}.
/FTId=VAR_021154.
VARIANT 225 225 P -> L. {ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.4}.
/FTId=VAR_047885.
VARIANT 252 252 D -> N. {ECO:0000269|Ref.4}.
/FTId=VAR_047886.
VARIANT 284 284 A -> P (in ABS1 and DISPORD; significant
reduction of activity).
{ECO:0000269|PubMed:14758361,
ECO:0000269|PubMed:15220035}.
/FTId=VAR_021155.
VARIANT 454 454 R -> H (in ABS1 and DISPORD; significant
reduction of activity).
{ECO:0000269|PubMed:14758361,
ECO:0000269|PubMed:15220035,
ECO:0000269|PubMed:15264278,
ECO:0000269|PubMed:15483095,
ECO:0000269|PubMed:27610946}.
/FTId=VAR_021156.
VARIANT 489 489 V -> E (in ABS1; significant reduction of
activity). {ECO:0000269|PubMed:14758361}.
/FTId=VAR_021157.
VARIANT 500 500 A -> V (in dbSNP:rs1057868).
{ECO:0000269|PubMed:15483095,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1550342,
ECO:0000269|Ref.4}.
/FTId=VAR_004617.
VARIANT 551 551 R -> Q.
/FTId=VAR_004618.
VARIANT 566 566 C -> Y (in DISPORD; significant reduction
of activity).
{ECO:0000269|PubMed:14758361,
ECO:0000269|PubMed:15220035}.
/FTId=VAR_021158.
VARIANT 575 575 Y -> C (in ABS1).
{ECO:0000269|PubMed:15483095}.
/FTId=VAR_021159.
VARIANT 605 605 V -> F (in DISPORD; significant reduction
of activity).
{ECO:0000269|PubMed:14758361}.
/FTId=VAR_021160.
VARIANT 609 617 LKQDREHLW -> R (in ABS1).
/FTId=VAR_021161.
CONFLICT 405 405 M -> L (in Ref. 3; BAB18572).
{ECO:0000305}.
CONFLICT 518 518 F -> L (in Ref. 1; AAB21814 and 3;
BAB18572). {ECO:0000305}.
CONFLICT 537 538 VA -> WH (in Ref. 1; AAB21814).
{ECO:0000305}.
HELIX 69 76 {ECO:0000244|PDB:3QE2}.
STRAND 79 85 {ECO:0000244|PDB:3QE2}.
STRAND 87 89 {ECO:0000244|PDB:3QE2}.
HELIX 90 101 {ECO:0000244|PDB:3QE2}.
HELIX 102 105 {ECO:0000244|PDB:3QE2}.
STRAND 109 112 {ECO:0000244|PDB:3QE2}.
HELIX 114 116 {ECO:0000244|PDB:3QE2}.
HELIX 119 127 {ECO:0000244|PDB:3QE2}.
STRAND 132 138 {ECO:0000244|PDB:3QE2}.
HELIX 141 143 {ECO:0000244|PDB:3QE2}.
HELIX 147 149 {ECO:0000244|PDB:3QE2}.
HELIX 150 158 {ECO:0000244|PDB:3QE2}.
STRAND 167 174 {ECO:0000244|PDB:3QE2}.
STRAND 178 180 {ECO:0000244|PDB:3QE2}.
HELIX 183 194 {ECO:0000244|PDB:3QE2}.
STRAND 198 201 {ECO:0000244|PDB:3QE2}.
STRAND 204 207 {ECO:0000244|PDB:3QE2}.
TURN 208 210 {ECO:0000244|PDB:5EMN}.
HELIX 212 231 {ECO:0000244|PDB:3QE2}.
STRAND 245 249 {ECO:0000244|PDB:3QFS}.
HELIX 255 257 {ECO:0000244|PDB:3QFS}.
STRAND 259 261 {ECO:0000244|PDB:3QFS}.
STRAND 263 265 {ECO:0000244|PDB:3QFS}.
TURN 266 270 {ECO:0000244|PDB:3QFS}.
STRAND 278 280 {ECO:0000244|PDB:3QFS}.
STRAND 282 291 {ECO:0000244|PDB:3QFS}.
STRAND 294 298 {ECO:0000244|PDB:3QFS}.
STRAND 300 306 {ECO:0000244|PDB:3QFS}.
STRAND 319 322 {ECO:0000244|PDB:3QFS}.
HELIX 328 338 {ECO:0000244|PDB:3QFS}.
STRAND 345 352 {ECO:0000244|PDB:3QFS}.
STRAND 360 366 {ECO:0000244|PDB:3QFS}.
HELIX 367 373 {ECO:0000244|PDB:3QFS}.
HELIX 383 389 {ECO:0000244|PDB:3QFS}.
HELIX 390 392 {ECO:0000244|PDB:3QFS}.
HELIX 396 406 {ECO:0000244|PDB:3QFS}.
STRAND 407 409 {ECO:0000244|PDB:5FA6}.
HELIX 410 419 {ECO:0000244|PDB:3QFS}.
TURN 420 424 {ECO:0000244|PDB:3QFS}.
HELIX 427 433 {ECO:0000244|PDB:3QFS}.
HELIX 441 447 {ECO:0000244|PDB:3QFS}.
STRAND 454 457 {ECO:0000244|PDB:3QFS}.
TURN 462 464 {ECO:0000244|PDB:3QFS}.
STRAND 468 474 {ECO:0000244|PDB:3QFS}.
STRAND 477 479 {ECO:0000244|PDB:3QFS}.
STRAND 485 487 {ECO:0000244|PDB:3QFS}.
HELIX 489 495 {ECO:0000244|PDB:3QFS}.
TURN 501 503 {ECO:0000244|PDB:3QE2}.
STRAND 508 514 {ECO:0000244|PDB:3QFS}.
STRAND 528 531 {ECO:0000244|PDB:3QFS}.
HELIX 534 537 {ECO:0000244|PDB:3QFS}.
HELIX 538 553 {ECO:0000244|PDB:3QFS}.
STRAND 560 567 {ECO:0000244|PDB:3QFS}.
TURN 569 571 {ECO:0000244|PDB:3QFS}.
HELIX 576 584 {ECO:0000244|PDB:3QFS}.
STRAND 587 595 {ECO:0000244|PDB:3QFS}.
STRAND 598 601 {ECO:0000244|PDB:3QFS}.
HELIX 605 611 {ECO:0000244|PDB:3QFS}.
HELIX 613 621 {ECO:0000244|PDB:3QFS}.
STRAND 625 631 {ECO:0000244|PDB:3QFS}.
TURN 632 634 {ECO:0000244|PDB:3QFS}.
HELIX 635 650 {ECO:0000244|PDB:3QFS}.
HELIX 655 667 {ECO:0000244|PDB:3QFS}.
STRAND 670 676 {ECO:0000244|PDB:3QFS}.
SEQUENCE 677 AA; 76690 MW; 2F7D4B9CDFDF5A74 CRC64;
MGDSHVDTSS TVSEAVAEEV SLFSMTDMIL FSLIVGLLTY WFLFRKKKEE VPEFTKIQTL
TSSVRESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA
DLSSLPEIDN ALVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLSGVKFAV FGLGNKTYEH
FNAMGKYVDK RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEH FGVEATGEES
SIRQYELVVH TDIDAAKVYM GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL
MHLELDISDS KIRYESGDHV AVYPANDSAL VNQLGKILGA DLDVVMSLNN LDEESNKKHP
FPCPTSYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE LLRKMASSSG EGKELYLSWV
VEARRHILAI LQDCPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVVVEYET
KAGRINKGVA TNWLRAKEPA GENGGRALVP MFVRKSQFRL PFKATTPVIM VGPGTGVAPF
IGFIQERAWL RQQGKEVGET LLYYGCRRSD EDYLYREELA QFHRDGALTQ LNVAFSREQS
HKVYVQHLLK QDREHLWKLI EGGAHIYVCG DARNMARDVQ NTFYDIVAEL GAMEHAQAVD
YIKKLMTKGR YSLDVWS


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