BLVRB_HUMAN
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 03-AUG-2022, entry version 203.
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 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 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 AlphaFoldDB; P30043; -.
DR SMR; P30043; -.
DR BioGRID; 107114; 28.
DR IntAct; P30043; 20.
DR STRING; 9606.ENSP00000263368; -.
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 iPTMnet; P30043; -.
DR MetOSite; P30043; -.
DR PhosphoSitePlus; P30043; -.
DR BioMuta; BLVRB; -.
DR DMDM; 1706870; -.
DR DOSAC-COBS-2DPAGE; P30043; -.
DR REPRODUCTION-2DPAGE; IPI00783862; -.
DR SWISS-2DPAGE; P30043; -.
DR UCD-2DPAGE; P30043; -.
DR EPD; P30043; -.
DR jPOST; P30043; -.
DR MassIVE; P30043; -.
DR PaxDb; P30043; -.
DR PeptideAtlas; P30043; -.
DR PRIDE; P30043; -.
DR ProteomicsDB; 54623; -.
DR TopDownProteomics; P30043; -.
DR Antibodypedia; 30531; 349 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 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; VYTEIRP; -.
DR OrthoDB; 1166292at2759; -.
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; 13 hits in 1089 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 200 other tissues.
DR ExpressionAtlas; P30043; baseline and differential.
DR Genevisible; P30043; HS.
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: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:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0042167; P:heme catabolic process; IDA:UniProtKB.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF13460; NAD_binding_10; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
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
