ID   BLVRB_HUMAN             Reviewed;         206 AA.
AC   P30043; A6NKD8; B2R5C6; P32078; P53005; Q32LZ2;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 212.
DE   RecName: Full=Flavin reductase (NADPH);
DE            Short=FR;
DE            EC=1.5.1.30 {ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:18241201};
DE   AltName: Full=Biliverdin reductase B;
DE            Short=BVR-B;
DE            EC=1.3.1.24 {ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:18241201, ECO:0000269|PubMed:7929092};
DE   AltName: Full=Biliverdin-IX beta-reductase;
DE   AltName: Full=Green heme-binding protein;
DE            Short=GHBP;
DE   AltName: Full=NADPH-dependent diaphorase;
DE   AltName: Full=NADPH-flavin reductase;
DE            Short=FLR;
GN   Name=BLVRB; Synonyms=FLR;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-34; 63-87 AND 98-206.
RC   TISSUE=Erythrocyte, and Reticulocyte;
RX   PubMed=8117274; DOI=10.1006/bbrc.1994.1165;
RA   Chikuba K., Yubisui T., Shirabe K., Takeshita M.;
RT   "Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-
RT   flavin reductase.";
RL   Biochem. Biophys. Res. Commun. 198:1170-1176(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8799475; DOI=10.1248/bpb.19.796;
RA   Komuro A., Tobe T., Hashimoto K., Nakano Y., Yamaguchi T., Nakajima H.,
RA   Tomita M.;
RT   "Molecular cloning and expression of human liver biliverdin-IXbeta
RT   reductase.";
RL   Biol. Pharm. Bull. 19:796-804(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-46.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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   [8]
RP   PROTEIN SEQUENCE OF 2-205.
RC   TISSUE=Liver;
RX   PubMed=8280170; DOI=10.1006/bbrc.1993.2649;
RA   Yamaguchi T., Komuro A., Nakano Y., Tomita M., Nakajima H.;
RT   "Complete amino acid sequence of biliverdin-IX beta reductase from human
RT   liver.";
RL   Biochem. Biophys. Res. Commun. 197:1518-1523(1993).
RN   [9]
RP   PROTEIN SEQUENCE OF 2-21, SUBUNIT, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=7929092; DOI=10.1016/s0021-9258(19)51088-2;
RA   Yamaguchi T., Komoda Y., Nakajima H.;
RT   "Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human
RT   liver. Purification and characterization.";
RL   J. Biol. Chem. 269:24343-24348(1994).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-11.
RC   TISSUE=Liver;
RX   PubMed=1286669; DOI=10.1002/elps.11501301201;
RA   Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA   Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA   Appel R.D., Hughes G.J.;
RT   "Human liver protein map: a reference database established by
RT   microsequencing and gel comparison.";
RL   Electrophoresis 13:992-1001(1992).
RN   [11]
RP   PROTEIN SEQUENCE OF 2-11.
RC   TISSUE=Erythrocyte;
RX   PubMed=8313871; DOI=10.1002/elps.11501401183;
RA   Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., Pasquali C.,
RA   Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., Balant L.,
RA   Hochstrasser D.F.;
RT   "Plasma and red blood cell protein maps: update 1993.";
RL   Electrophoresis 14:1223-1231(1993).
RN   [12]
RP   PROTEIN SEQUENCE OF 40-92; 64-78; 106-124 AND 146-170, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [13]
RP   IDENTITY OF FR AND BVR-B.
RX   PubMed=8687377; DOI=10.1042/bj3160385;
RA   Shalloe F., Elliott G., Ennis O., Mantle T.J.;
RT   "Evidence that biliverdin-IX beta reductase and flavin reductase are
RT   identical.";
RL   Biochem. J. 316:385-387(1996).
RN   [14]
RP   FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=10620517; DOI=10.1042/bj3450393;
RA   Cunningham O., Gore M.G., Mantle T.J.;
RT   "Initial-rate kinetics of the flavin reductase reaction catalysed by human
RT   biliverdin-IXbeta reductase (BVR-B).";
RL   Biochem. J. 345:393-399(2000).
RN   [15]
RP   CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-153.
RX   PubMed=18241201; DOI=10.1042/bj20071495;
RA   Smith L.J., Browne S., Mulholland A.J., Mantle T.J.;
RT   "Computational and experimental studies on the catalytic mechanism of
RT   biliverdin-IXbeta reductase.";
RL   Biochem. J. 411:475-484(2008).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [19]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEXES WITH MESOBILIVERDIN;
RP   BILIVERDIN; FLAVIN MONONUCLEOTIDE; LUMICHROME AND NADP, AND SUBUNIT.
RX   PubMed=11224564; DOI=10.1038/84948;
RA   Pereira P.J., Macedo-Ribeiro S., Parraga A., Perez-Luque R., Cunningham O.,
RA   Darcy K., Mantle T.J., Coll M.;
RT   "Structure of human biliverdin IXbeta reductase, an early fetal bilirubin
RT   IXbeta producing enzyme.";
RL   Nat. Struct. Biol. 8:215-220(2001).
CC   -!- FUNCTION: Broad specificity oxidoreductase that catalyzes the NADPH-
CC       dependent reduction of a variety of flavins, such as riboflavin, FAD or
CC       FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone).
CC       Contributes to heme catabolism and metabolizes linear tetrapyrroles.
CC       Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of
CC       FMN and NADPH. In the liver, converts biliverdin to bilirubin.
CC       {ECO:0000269|PubMed:10620517}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + reduced riboflavin = 2 H(+) + NADPH + riboflavin;
CC         Xref=Rhea:RHEA:19377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17607,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57986, ChEBI:CHEBI:58349; EC=1.5.1.30;
CC         Evidence={ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:18241201};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=bilirubin IXalpha + NAD(+) = biliverdin IXalpha + H(+) + NADH;
CC         Xref=Rhea:RHEA:15797, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:57977, ChEBI:CHEBI:57991; EC=1.3.1.24;
CC         Evidence={ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:18241201,
CC         ECO:0000269|PubMed:7929092};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=bilirubin IXalpha + NADP(+) = biliverdin IXalpha + H(+) +
CC         NADPH; Xref=Rhea:RHEA:15793, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:57977, ChEBI:CHEBI:57991, ChEBI:CHEBI:58349; EC=1.3.1.24;
CC         Evidence={ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:18241201,
CC         ECO:0000269|PubMed:7929092};
CC   -!- ACTIVITY REGULATION: Mesobiliverdin acts as a competitve inhibitor for
CC       flavin reduction, indicating that flavin and tetrapyrrole substrates
CC       compete for the same site. {ECO:0000269|PubMed:10620517}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=36 uM for NADP {ECO:0000269|PubMed:10620517,
CC         ECO:0000269|PubMed:7929092};
CC         KM=5.6 mM for NADH {ECO:0000269|PubMed:10620517,
CC         ECO:0000269|PubMed:7929092};
CC         KM=0.3 uM for biliverdin IX-beta {ECO:0000269|PubMed:10620517,
CC         ECO:0000269|PubMed:7929092};
CC         KM=52 uM for FMN {ECO:0000269|PubMed:10620517,
CC         ECO:0000269|PubMed:7929092};
CC         KM=125 uM for FAD {ECO:0000269|PubMed:10620517,
CC         ECO:0000269|PubMed:7929092};
CC         KM=53 uM for riboflavin {ECO:0000269|PubMed:10620517,
CC         ECO:0000269|PubMed:7929092};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11224564,
CC       ECO:0000269|PubMed:7929092}.
CC   -!- INTERACTION:
CC       P30043; Q9UJ72: ANXA10; NbExp=5; IntAct=EBI-2837485, EBI-8648654;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7929092}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in liver and erythrocytes.
CC       At lower levels in heart, lung, adrenal gland and cerebrum.
CC       {ECO:0000269|PubMed:7929092}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/blvrb/";
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DR   EMBL; D26308; BAA05370.1; -; mRNA.
DR   EMBL; D32143; BAA06874.1; -; mRNA.
DR   EMBL; AK312137; BAG35073.1; -; mRNA.
DR   EMBL; AY340485; AAP88933.1; -; Genomic_DNA.
DR   EMBL; AC010271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471126; EAW56969.1; -; Genomic_DNA.
DR   EMBL; BC109371; AAI09372.1; -; mRNA.
DR   CCDS; CCDS33029.1; -.
DR   PIR; JC2070; JC2070.
DR   RefSeq; NP_000704.1; NM_000713.2.
DR   PDB; 1HDO; X-ray; 1.15 A; A=2-205.
DR   PDB; 1HE2; X-ray; 1.20 A; A=2-205.
DR   PDB; 1HE3; X-ray; 1.40 A; A=2-205.
DR   PDB; 1HE4; X-ray; 1.40 A; A=2-205.
DR   PDB; 1HE5; X-ray; 1.50 A; A=2-205.
DR   PDB; 5OOG; X-ray; 1.33 A; A=1-206.
DR   PDB; 5OOH; X-ray; 1.20 A; A=1-206.
DR   PDB; 6OPL; X-ray; 1.37 A; A=1-205.
DR   PDB; 7ER6; X-ray; 1.60 A; A/B=1-206.
DR   PDB; 7ER7; X-ray; 1.70 A; A/B=1-206.
DR   PDB; 7ER8; X-ray; 1.45 A; A/B=1-206.
DR   PDB; 7ER9; X-ray; 1.45 A; A/B=1-206.
DR   PDB; 7ERA; X-ray; 1.35 A; A/B=1-206.
DR   PDB; 7ERB; X-ray; 1.50 A; A/B/C/D=1-206.
DR   PDB; 7ERC; X-ray; 1.50 A; A/B=1-206.
DR   PDB; 7ERD; X-ray; 2.00 A; A/B=1-206.
DR   PDB; 7ERE; X-ray; 1.60 A; A/B/C/D=1-206.
DR   PDB; 8ELL; X-ray; 1.52 A; A=1-206.
DR   PDB; 8ELM; X-ray; 2.19 A; A=1-206.
DR   PDBsum; 1HDO; -.
DR   PDBsum; 1HE2; -.
DR   PDBsum; 1HE3; -.
DR   PDBsum; 1HE4; -.
DR   PDBsum; 1HE5; -.
DR   PDBsum; 5OOG; -.
DR   PDBsum; 5OOH; -.
DR   PDBsum; 6OPL; -.
DR   PDBsum; 7ER6; -.
DR   PDBsum; 7ER7; -.
DR   PDBsum; 7ER8; -.
DR   PDBsum; 7ER9; -.
DR   PDBsum; 7ERA; -.
DR   PDBsum; 7ERB; -.
DR   PDBsum; 7ERC; -.
DR   PDBsum; 7ERD; -.
DR   PDBsum; 7ERE; -.
DR   PDBsum; 8ELL; -.
DR   PDBsum; 8ELM; -.
DR   AlphaFoldDB; P30043; -.
DR   SMR; P30043; -.
DR   BioGRID; 107114; 47.
DR   IntAct; P30043; 20.
DR   STRING; 9606.ENSP00000263368; -.
DR   BindingDB; P30043; -.
DR   ChEMBL; CHEMBL5019; -.
DR   DrugBank; DB02073; Biliverdine IX Alpha.
DR   DrugBank; DB03247; Flavin mononucleotide.
DR   DrugBank; DB04345; Lumichrome.
DR   DrugBank; DB04363; Mesobiliverdin IV alpha.
DR   DrugBank; DB09241; Methylene blue.
DR   DrugBank; DB00157; NADH.
DR   DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR   DrugBank; DB00140; Riboflavin.
DR   DrugCentral; P30043; -.
DR   GlyGen; P30043; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P30043; -.
DR   MetOSite; P30043; -.
DR   PhosphoSitePlus; P30043; -.
DR   BioMuta; BLVRB; -.
DR   DMDM; 1706870; -.
DR   DOSAC-COBS-2DPAGE; P30043; -.
DR   REPRODUCTION-2DPAGE; IPI00783862; -.
DR   EPD; P30043; -.
DR   jPOST; P30043; -.
DR   MassIVE; P30043; -.
DR   PaxDb; 9606-ENSP00000263368; -.
DR   PeptideAtlas; P30043; -.
DR   ProteomicsDB; 54623; -.
DR   Pumba; P30043; -.
DR   TopDownProteomics; P30043; -.
DR   Antibodypedia; 30531; 377 antibodies from 34 providers.
DR   DNASU; 645; -.
DR   Ensembl; ENST00000263368.9; ENSP00000263368.3; ENSG00000090013.11.
DR   GeneID; 645; -.
DR   KEGG; hsa:645; -.
DR   MANE-Select; ENST00000263368.9; ENSP00000263368.3; NM_000713.3; NP_000704.1.
DR   AGR; HGNC:1063; -.
DR   CTD; 645; -.
DR   DisGeNET; 645; -.
DR   GeneCards; BLVRB; -.
DR   HGNC; HGNC:1063; BLVRB.
DR   HPA; ENSG00000090013; Tissue enhanced (bone).
DR   MIM; 600941; gene.
DR   neXtProt; NX_P30043; -.
DR   OpenTargets; ENSG00000090013; -.
DR   PharmGKB; PA25374; -.
DR   VEuPathDB; HostDB:ENSG00000090013; -.
DR   eggNOG; ENOG502RY9R; Eukaryota.
DR   GeneTree; ENSGT00390000014810; -.
DR   HOGENOM; CLU_025711_2_0_1; -.
DR   InParanoid; P30043; -.
DR   OMA; DWTIICP; -.
DR   OrthoDB; 2511224at2759; -.
DR   PhylomeDB; P30043; -.
DR   TreeFam; TF324063; -.
DR   BRENDA; 1.3.1.24; 2681.
DR   BRENDA; 1.5.1.30; 2681.
DR   PathwayCommons; P30043; -.
DR   Reactome; R-HSA-189483; Heme degradation.
DR   Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR   SABIO-RK; P30043; -.
DR   SignaLink; P30043; -.
DR   BioGRID-ORCS; 645; 14 hits in 1175 CRISPR screens.
DR   ChiTaRS; BLVRB; human.
DR   EvolutionaryTrace; P30043; -.
DR   GenomeRNAi; 645; -.
DR   Pharos; P30043; Tbio.
DR   PRO; PR:P30043; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P30043; Protein.
DR   Bgee; ENSG00000090013; Expressed in trabecular bone tissue and 202 other cell types or tissues.
DR   ExpressionAtlas; P30043; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR   GO; GO:0106276; F:biliberdin reductase NAD+ activity; IEA:UniProtKB-EC.
DR   GO; GO:0004074; F:biliverdin reductase (NAD(P)+) activity; IDA:UniProtKB.
DR   GO; GO:0106277; F:biliverdin reductase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IDA:UniProtKB.
DR   GO; GO:0042167; P:heme catabolic process; IDA:UniProtKB.
DR   CDD; cd05244; BVR-B_like_SDR_a; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43355; FLAVIN REDUCTASE (NADPH); 1.
DR   PANTHER; PTHR43355:SF10; FLAVIN REDUCTASE (NADPH); 1.
DR   Pfam; PF13460; NAD_binding_10; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SWISS-2DPAGE; P30043; -.
DR   UCD-2DPAGE; P30043; -.
DR   Genevisible; P30043; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1286669,
FT                   ECO:0000269|PubMed:7929092, ECO:0000269|PubMed:8117274,
FT                   ECO:0000269|PubMed:8280170, ECO:0000269|PubMed:8313871"
FT   CHAIN           2..206
FT                   /note="Flavin reductase (NADPH)"
FT                   /id="PRO_0000064948"
FT   BINDING         10..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         54..55
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         75..78
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         132
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         153
FT                   /ligand="substrate"
FT   BINDING         154
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         46
FT                   /note="R -> Q (in dbSNP:rs11547746)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_019168"
FT   MUTAGEN         153
FT                   /note="H->A: Reduced affinity for biliverdin."
FT                   /evidence="ECO:0000269|PubMed:18241201"
FT   CONFLICT        16
FT                   /note="G -> C (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   HELIX           14..25
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          29..35
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          48..53
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   HELIX           58..65
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   HELIX           86..101
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:1HE2"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   HELIX           126..141
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          144..149
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   HELIX           178..187
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:1HE2"
FT   TURN            193..196
FT                   /evidence="ECO:0007829|PDB:1HDO"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:1HDO"
SQ   SEQUENCE   206 AA;  22119 MW;  3057E6D69A9F9F9F CRC64;
     MAVKKIAIFG ATGQTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPRPAHV VVGDVLQAAD
     VDKTVAGQDA VIVLLGTRND LSPTTVMSEG ARNIVAAMKA HGVDKVVACT SAFLLWDPTK
     VPPRLQAVTD DHIRMHKVLR ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD
     LGHFMLRCLT TDEYDGHSTY PSHQYQ
//