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 25-NOV-2008, entry version 54. DE RecName: Full=Flavin reductase; DE Short=FR; DE EC=1.5.1.30; DE AltName: Full=NADPH-dependent diaphorase; DE AltName: Full=NADPH-flavin reductase; DE Short=FLR; DE AltName: Full=Biliverdin reductase B; DE Short=BVR-B; DE EC=1.3.1.24; DE AltName: Full=Biliverdin-IX beta-reductase; DE AltName: Full=Green heme-binding protein; DE Short=GHBP; GN Name=BLVRB; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-58 AND 118-127, AND RP MASS SPECTROMETRY. RC TISSUE=Liver; RX MEDLINE=95023903; PubMed=7937764; 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 MEDLINE=91298967; 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: Catalyzes electron transfer from reduced pyridine CC nucleotides to flavins as well as methylene blue, pyrroloquinoline CC quinone, riboflavin, or methemoglobin. Possible role in protecting CC cells from oxidative damage or in regulating iron metabolism. In CC the liver, converts biliverdin to bilirubin. CC -!- CATALYTIC ACTIVITY: Reduced riboflavin + NADP(+) = riboflavin + CC NADPH. CC -!- CATALYTIC ACTIVITY: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H. CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- TISSUE SPECIFICITY: At least expressed in the liver and CC erythrocyte. CC -!- MASS SPECTROMETRY: Mass=21994; Method=Electrospray; Range=2-206; CC Source=PubMed:7937764; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L35045; AAC37323.1; -; mRNA. DR EMBL; BC102269; AAI02270.1; -; mRNA. DR PIR; S68597; S68597. DR RefSeq; NP_776676.1; -. DR UniGene; Bt.4093; -. DR HSSP; P30043; 1HDO. DR SMR; P52556; 1-205. DR Ensembl; ENSBTAG00000010508; Bos taurus. DR GeneID; 281650; -. DR KEGG; bta:281650; -. DR HOVERGEN; P52556; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004074; F:biliverdin reductase activity; IEA:EC. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0042602; F:flavin reductase activity; IEA:EC. DR GO; GO:0044237; P:cellular metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01370; Epimerase; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Multifunctional enzyme; NADP; KW Oxidoreductase. FT INIT_MET 1 1 Removed. FT CHAIN 2 206 Flavin reductase. FT /FTId=PRO_0000064947. FT NP_BIND 5 36 NAD or NADP (Potential). 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 //