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NCPR_MOUSE
ID   NCPR_MOUSE              Reviewed;         678 AA.
AC   P37040;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 180.
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=Por {ECO:0000255|HAMAP-Rule:MF_03212};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ddY;
RX   PubMed=8011664; DOI=10.1016/0005-2728(94)90146-5;
RA   Ohgiya S., Ishizaki K., Kamataki T., Shinriki N.;
RT   "Mouse NADPH-cytochrome P-450 oxidoreductase: molecular cloning and
RT   functional expression in yeast.";
RL   Biochim. Biophys. Acta 1186:137-141(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. {ECO:0000255|HAMAP-Rule:MF_03212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC         reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC         COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03212};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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; D17571; BAA04496.1; -; mRNA.
DR   EMBL; BC031463; AAH31463.1; -; mRNA.
DR   CCDS; CCDS39318.1; -.
DR   RefSeq; NP_032924.1; NM_008898.2.
DR   RefSeq; XP_006504461.1; XM_006504398.1.
DR   RefSeq; XP_006504462.1; XM_006504399.1.
DR   AlphaFoldDB; P37040; -.
DR   SMR; P37040; -.
DR   BioGRID; 202299; 8.
DR   IntAct; P37040; 3.
DR   MINT; P37040; -.
DR   STRING; 10090.ENSMUSP00000005651; -.
DR   ChEMBL; CHEMBL4105861; -.
DR   iPTMnet; P37040; -.
DR   PhosphoSitePlus; P37040; -.
DR   SwissPalm; P37040; -.
DR   SWISS-2DPAGE; P37040; -.
DR   EPD; P37040; -.
DR   jPOST; P37040; -.
DR   MaxQB; P37040; -.
DR   PaxDb; P37040; -.
DR   PeptideAtlas; P37040; -.
DR   PRIDE; P37040; -.
DR   ProteomicsDB; 252930; -.
DR   Antibodypedia; 2433; 454 antibodies from 35 providers.
DR   DNASU; 18984; -.
DR   Ensembl; ENSMUST00000005651; ENSMUSP00000005651; ENSMUSG00000005514.
DR   GeneID; 18984; -.
DR   KEGG; mmu:18984; -.
DR   UCSC; uc008zyt.1; mouse.
DR   CTD; 5447; -.
DR   MGI; MGI:97744; Por.
DR   VEuPathDB; HostDB:ENSMUSG00000005514; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   GeneTree; ENSGT00940000156847; -.
DR   HOGENOM; CLU_001570_17_3_1; -.
DR   InParanoid; P37040; -.
DR   OMA; QKRYQRD; -.
DR   OrthoDB; 318396at2759; -.
DR   PhylomeDB; P37040; -.
DR   TreeFam; TF105719; -.
DR   BioGRID-ORCS; 18984; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Por; mouse.
DR   PRO; PR:P37040; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P37040; protein.
DR   Bgee; ENSMUSG00000005514; Expressed in nasal cavity epithelium and 296 other tissues.
DR   ExpressionAtlas; P37040; baseline and differential.
DR   Genevisible; P37040; MM.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; ISO:MGI.
DR   GO; GO:0009055; F:electron transfer activity; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
DR   GO; GO:0010181; F:FMN binding; ISO:MGI.
DR   GO; GO:0016787; F:hydrolase activity; ISO:MGI.
DR   GO; GO:0047726; F:iron-cytochrome-c reductase activity; ISO:MGI.
DR   GO; GO:0050661; F:NADP binding; ISO:MGI.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; ISO:MGI.
DR   GO; GO:0008941; F:nitric oxide dioxygenase activity; ISO:MGI.
DR   GO; GO:0016491; F:oxidoreductase activity; IMP:MGI.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:Ensembl.
DR   GO; GO:0090346; P:cellular organofluorine metabolic process; ISO:MGI.
DR   GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
DR   GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
DR   GO; GO:0070988; P:demethylation; ISO:MGI.
DR   GO; GO:0022900; P:electron transport chain; ISO:MGI.
DR   GO; GO:0019395; P:fatty acid oxidation; ISO:MGI.
DR   GO; GO:0009812; P:flavonoid metabolic process; IEA:Ensembl.
DR   GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR   GO; GO:0060192; P:negative regulation of lipase activity; ISO:MGI.
DR   GO; GO:0043602; P:nitrate catabolic process; ISO:MGI.
DR   GO; GO:0046210; P:nitric oxide catabolic process; ISO:MGI.
DR   GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISO:MGI.
DR   GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISO:MGI.
DR   GO; GO:0032770; P:positive regulation of monooxygenase activity; ISO:MGI.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISO:MGI.
DR   GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; ISO:MGI.
DR   GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:MGI.
DR   GO; GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; ISO:MGI.
DR   GO; GO:0071548; P:response to dexamethasone; ISO:MGI.
DR   GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
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   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; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P16435"
FT   CHAIN           2..678
FT                   /note="NADPH--cytochrome P450 reductase"
FT                   /id="PRO_0000167597"
FT   TOPO_DOM        2..22
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   TOPO_DOM        44..678
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   DOMAIN          80..224
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   DOMAIN          279..521
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         86..91
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         138..141
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         173..182
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         208
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         298
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         424
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         454..457
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         472..474
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         478
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         488..491
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         535
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         596..597
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         602..606
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         639
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         677
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P16435"
SQ   SEQUENCE   678 AA;  77044 MW;  060282A7A55483AF CRC64;
     MGDSHEDTSA TVPEAVAEEV SLFSTTDIVL FSLIVGVLTY WFIFKKKKEE IPEFSKIQTT
     APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA
     DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLTGVKFAV FGLGNKTYEH
     FNAMGKYVDQ RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES
     SIRQYELVVH EDMDTAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTTNR KLNQGTERHL
     MHLELDISDS KIRYESGDHV AVYPANDSTL VNQIGEILGA DLDVIMSLNN LDEESNKKHP
     FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE HLHKMASSSG EGKELYLSWV
     VEARRHILAI LQDYPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVAVEYEA
     KSGRVNKGVA TSWLRTKEPA GENGRRALVP MFVRKSQFRL PFKPTTPVIM VGPGTGVAPF
     MGFIQERAWL REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA
     HKVYVQHLLK RDKEHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE FGPMEHTQAV
     DYVKKLMTKG RYSLDVWS
 
 
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