ID   Q59ED7_HUMAN            Unreviewed;       686 AA.
AC   Q59ED7;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE            EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD93111.1};
RN   [1] {ECO:0000313|EMBL:BAD93111.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Aorta endothelial cell {ECO:0000313|EMBL:BAD93111.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; AB209874; BAD93111.1; -; mRNA.
DR   AlphaFoldDB; Q59ED7; -.
DR   IntAct; Q59ED7; 1.
DR   PeptideAtlas; Q59ED7; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-EC.
DR   CDD; cd06204; CYPOR; 1.
DR   Gene3D; 3.40.50.360; -; 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; 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   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   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..233
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          288..530
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD93111.1"
SQ   SEQUENCE   686 AA;  77737 MW;  453DAD59A3F48655 CRC64;
     PGCQRFMINM GDSHVDTSST VSEAVAEEVS LFSMTDMILF SLIVGLLTYW FLFRKKKEEV
     PEFTKIQTLT SSVRESSFVE KMKKTGRNII VFYGSQTGTA EEFANRLSKD AHRYGMRGMS
     ADPEEYDLAD LSSLPEIDNA LVVFCMATYG EGDPTDNAQD FYDWLQETDV DLSGVKFAVF
     GLGNKTYEHF NAMGKYVDKR LEQLGAQRIF ELGLGDDDGN LEEDFITWRE QFWPAVCEHF
     GVEATGEESS IRQYELVVHT DIDAAKVYMG EMGRLKSYEN QKPPFDAKNP FLAAVTTNRK
     LNQGTERHLM HLELDISDSK IRYESGDHVA VYPANDSALV NQLGKILGAD LDVVMSLNNL
     DEESNKKHPF PCPTSYRTAL TYYLDITNPP RTNVLYELAQ YASEPSEQEL LRKMASSSGE
     GKELYLSWVV EARRHILAIL QDCPSLRPPI DHLCELLPRL QARYYSIASS SKVHPNSVHI
     CAVVVEYETK AGRINKGVAT NWLRAKEPAG ENGGRALVPM FVRKSQFRLP FKATTPVIMV
     GPGTGVAPFI GFIQERAWLR QQGKEVGETL LYYGCRRSDE DYLYREELAQ FHRDGALTQL
     NVAFSREQSH KVYVQHLLKQ DREHLWKLIE GGAHIYVCGD ARNMARDVQN TFYDIVAELG
     AMEHAQAVDY IKKLMTKGRY SLDVWS
//