BLVRB_MOUSE
ID BLVRB_MOUSE Reviewed; 206 AA.
AC Q923D2;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Flavin reductase (NADPH);
DE Short=FR;
DE EC=1.5.1.30 {ECO:0000250|UniProtKB:P30043};
DE AltName: Full=Biliverdin reductase B;
DE Short=BVR-B;
DE EC=1.3.1.24 {ECO:0000250|UniProtKB:P30043};
DE AltName: Full=Biliverdin-IX beta-reductase;
DE AltName: Full=NADPH-dependent diaphorase;
DE AltName: Full=NADPH-flavin reductase;
DE Short=FLR;
GN Name=Blvrb;
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 [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [2]
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: 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:0000250|UniProtKB:P30043}.
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:0000250|UniProtKB:P30043};
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:0000250|UniProtKB:P30043};
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:0000250|UniProtKB:P30043};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P30043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30043}.
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DR EMBL; BC006617; AAH06617.1; -; mRNA.
DR EMBL; BC027279; AAH27279.1; -; mRNA.
DR CCDS; CCDS39848.1; -.
DR RefSeq; NP_659172.1; NM_144923.3.
DR AlphaFoldDB; Q923D2; -.
DR SMR; Q923D2; -.
DR BioGRID; 231349; 1.
DR STRING; 10090.ENSMUSP00000043092; -.
DR iPTMnet; Q923D2; -.
DR PhosphoSitePlus; Q923D2; -.
DR SwissPalm; Q923D2; -.
DR CPTAC; non-CPTAC-3896; -.
DR EPD; Q923D2; -.
DR jPOST; Q923D2; -.
DR MaxQB; Q923D2; -.
DR PaxDb; Q923D2; -.
DR PRIDE; Q923D2; -.
DR ProteomicsDB; 265306; -.
DR Antibodypedia; 30531; 349 antibodies from 34 providers.
DR DNASU; 233016; -.
DR Ensembl; ENSMUST00000037399; ENSMUSP00000043092; ENSMUSG00000040466.
DR GeneID; 233016; -.
DR KEGG; mmu:233016; -.
DR UCSC; uc009fwd.1; mouse.
DR CTD; 645; -.
DR MGI; MGI:2385271; Blvrb.
DR VEuPathDB; HostDB:ENSMUSG00000040466; -.
DR eggNOG; ENOG502RY9R; Eukaryota.
DR GeneTree; ENSGT00390000014810; -.
DR HOGENOM; CLU_025711_2_0_1; -.
DR InParanoid; Q923D2; -.
DR OMA; EQPEHYG; -.
DR OrthoDB; 1166292at2759; -.
DR PhylomeDB; Q923D2; -.
DR TreeFam; TF324063; -.
DR Reactome; R-MMU-189483; Heme degradation.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 233016; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q923D2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q923D2; protein.
DR Bgee; ENSMUSG00000040466; Expressed in fetal liver hematopoietic progenitor cell and 191 other tissues.
DR ExpressionAtlas; Q923D2; baseline and differential.
DR Genevisible; Q923D2; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0106276; F:biliberdin reductase NAD+ activity; IEA:UniProtKB-EC.
DR GO; GO:0004074; F:biliverdin reductase (NAD(P)+) activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0042167; P:heme catabolic process; ISS: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 Cytoplasm; NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..206
FT /note="Flavin reductase (NADPH)"
FT /id="PRO_0000064949"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 54..55
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 75..78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30043"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30043"
SQ SEQUENCE 206 AA; 22197 MW; EDAEE91F5F39F629 CRC64;
MTVKKIAIFG ATGRTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPQPAHV VVGDVRQAAD
VDKTVAGQEA VIVLLGTGND LSPTTVMSEG TRNIVTAMKA HGVDKVVACT SAFLLWDPTK
VPPRLQDVTD DHIRMHKILQ ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD
LGHFMLRCLT TNEYDGHTTY PSHQYD
