BLVRB_BOVIN
ID BLVRB_BOVIN Reviewed; 206 AA.
AC P52556; Q3T0T4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
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=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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-58 AND 118-127, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=7937764; DOI=10.1073/pnas.91.20.9322;
RA Quandt K.S., Hultquist D.E.;
RT "Flavin reductase: sequence of cDNA from bovine liver and tissue
RT distribution.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9322-9326(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-37; 121-137 AND 146-169.
RC TISSUE=Erythrocyte;
RX PubMed=2069570; DOI=10.1016/0006-291x(91)91816-u;
RA Quandt K.S., Xu F., Chen P., Hultquist D.E.;
RT "Evidence that the protein components of bovine erythrocyte green heme
RT binding protein and flavin reductase are identical.";
RL Biochem. Biophys. Res. Commun. 178:315-321(1991).
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}.
CC -!- TISSUE SPECIFICITY: At least expressed in the liver and erythrocyte.
CC -!- MASS SPECTROMETRY: Mass=21994; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7937764};
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DR EMBL; L35045; AAC37323.1; -; mRNA.
DR EMBL; BC102269; AAI02270.1; -; mRNA.
DR PIR; S68597; S68597.
DR RefSeq; NP_776676.1; NM_174251.1.
DR AlphaFoldDB; P52556; -.
DR SMR; P52556; -.
DR STRING; 9913.ENSBTAP00000013889; -.
DR PaxDb; P52556; -.
DR PeptideAtlas; P52556; -.
DR PRIDE; P52556; -.
DR Ensembl; ENSBTAT00000013889; ENSBTAP00000013889; ENSBTAG00000010508.
DR GeneID; 281650; -.
DR KEGG; bta:281650; -.
DR CTD; 645; -.
DR VEuPathDB; HostDB:ENSBTAG00000010508; -.
DR VGNC; VGNC:26511; BLVRB.
DR eggNOG; ENOG502RY9R; Eukaryota.
DR GeneTree; ENSGT00390000014810; -.
DR HOGENOM; CLU_025711_2_0_1; -.
DR InParanoid; P52556; -.
DR OMA; EQPEHYG; -.
DR OrthoDB; 1166292at2759; -.
DR TreeFam; TF324063; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000010508; Expressed in digestive system secreted substance and 106 other tissues.
DR ExpressionAtlas; P52556; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2069570"
FT CHAIN 2..206
FT /note="Flavin reductase (NADPH)"
FT /id="PRO_0000064947"
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; 22132 MW; 79A679FED289E32C CRC64;
MVVKKIALFG ATGNTGLTTL AQAVQAGYEV TVLVRDPSRL PSEGPQPAHV VVGDVRQPAD
VDKTVAGQDA VIVLLGTRND LSPTTVMSEG AQNIVAAMKA HGVDKVVACT SAFLLWDPSK
VPPRLQDVTD DHIRMHKVLQ QSGLKYVAVM PPHIGDHPLT GAYTVTLDGR GPSRVISKHD
LGHFMLHCLT TDKYDGHTTY PSHVYE
