ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P30043


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name BLVRB_HUMAN
Primary accession number P30043
Secondary accession numbers A6NKD8 P32078 P53005 Q32LZ2
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 83)
Name and origin of the protein
Protein name Flavin reductase
Synonyms FR
EC 1.5.1.30
NADPH-dependent diaphorase
NADPH-flavin reductase
FLR
Biliverdin reductase B
BVR-B
EC 1.3.1.24
Biliverdin-IX beta-reductase
Green heme-binding protein
GHBP
Gene name
Name: BLVRB
Synonyms: FLR
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-34; 63-87 AND 98-206.
TISSUE=Erythrocyte, and Reticulocyte;
DOI=10.1006/bbrc.1994.1165; PubMed=8117274 [NCBI, ExPASy, EBI, Israel, Japan]
Chikuba K., Yubisui T., Shirabe K., Takeshita M.;
"Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase.";
Biochem. Biophys. Res. Commun. 198:1170-1176(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8799475 [NCBI, ExPASy, EBI, Israel, Japan]
Komuro A., Tobe T., Hashimoto K., Nakano Y., Yamaguchi T., Nakajima H., Tomita M.;
"Molecular cloning and expression of human liver biliverdin-IXbeta reductase.";
Biol. Pharm. Bull. 19:796-804(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-46.
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-205.
TISSUE=Liver;
DOI=10.1006/bbrc.1993.2649; PubMed=8280170 [NCBI, ExPASy, EBI, Israel, Japan]
Yamaguchi T., Komuro A., Nakano Y., Tomita M., Nakajima H.;
"Complete amino acid sequence of biliverdin-IX beta reductase from human liver.";
Biochem. Biophys. Res. Commun. 197:1518-1523(1993).
[8]
PROTEIN SEQUENCE OF 2-21.
TISSUE=Liver;
PubMed=7929092 [NCBI, ExPASy, EBI, Israel, Japan]
Yamaguchi T., Komoda Y., Nakajima H.;
"Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization.";
J. Biol. Chem. 269:24343-24348(1994).
[9]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Liver;
PubMed=1286669 [NCBI, ExPASy, EBI, Israel, Japan]
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[10]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Erythrocyte;
PubMed=8313871 [NCBI, ExPASy, EBI, Israel, Japan]
Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., Balant L., Hochstrasser D.F.;
"Plasma and red blood cell protein maps: update 1993.";
Electrophoresis 14:1223-1231(1993).
[11]
PROTEIN SEQUENCE OF 64-78 AND 146-170, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[12]
IDENTITY OF FR AND BVR-B.
PubMed=8687377 [NCBI, ExPASy, EBI, Israel, Japan]
Shalloe F., Elliott G., Ennis O., Mantle T.J.;
"Evidence that biliverdin-IX beta reductase and flavin reductase are identical.";
Biochem. J. 316:385-387(1996).
[13]
X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS).
DOI=10.1038/84948; PubMed=11224564 [NCBI, ExPASy, EBI, Israel, Japan]
Pereira P.J., Macedo-Ribeiro S., Parraga A., Perez-Luque R., Cunningham O., Darcy K., Mantle T.J., Coll M.;
"Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme.";
Nat. Struct. Biol. 8:215-220(2001).
Comments
  • FUNCTION: Catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. Possible role in protecting cells from oxidative damage or in regulating iron metabolism. In the liver, converts biliverdin to bilirubin.
  • CATALYTIC ACTIVITY: Reduced riboflavin + NADP+ = riboflavin + NADPH.
  • CATALYTIC ACTIVITY: Bilirubin + NAD(P)+ = biliverdin + NAD(P)H.
  • SUBUNIT: Monomer.
  • SUBCELLULAR LOCATION: Cytoplasm (Potential).
  • TISSUE SPECIFICITY: Predominantly expressed in liver and erythrocytes. At lower levels in heart, lung, adrenal gland and cerebrum.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D26308; BAA05370.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D32143; BAA06874.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY340485; AAP88933.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC010271; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CH471126; EAW56969.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC109371; AAI09372.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC2070; JC2070.
RefSeq NP_000704.1; -.
UniGene Hs.515785
3D structure databases
PDB
1HDO; X-ray; 1.15 A; A=1-206.[ExPASy / RCSB / EBI]
1HE2; X-ray; 1.20 A; A=1-206.[ExPASy / RCSB / EBI]
1HE3; X-ray; 1.40 A; A=1-206.[ExPASy / RCSB / EBI]
1HE4; X-ray; 1.40 A; A=1-206.[ExPASy / RCSB / EBI]
1HE5; X-ray; 1.50 A; A=1-206.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HDO; -.
1HE2; -.
1HE3; -.
1HE4; -.
1HE5; -.
ModBase P30043.
Polymorphism databases
NIEHS-SNPs BLVRB.
2D gel databases
SWISS-2DPAGE P30043; -.
DOSAC-COBS-2DPAGE P30043; -.
REPRODUCTION-2DPAGE IPI00783862; -.
Organism-specific databases
H-InvDB HIX0040129; -.
HGNC HGNC:1063; BLVRB.
GenAtlas BLVRB.
MIM 600941; gene. [NCBI / EBI]
PharmGKB PA25374; -.
GeneCards P30043.
Gene expression databases
ArrayExpress P30043; -.
CleanEx HS_BLVRB; -.
GermOnline ENSG00000090013; Homo sapiens.
Ontologies
GO
GO:0004074; Molecular function: biliverdin reductase activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001509; Epimerase_deHydtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01370; Epimerase; 1.
Pfam graphical view of domain structure.
BLOCKS P30043.
Genome annotation databases
Ensembl ENSG00000090013; Homo sapiens. [Contig view]
GeneID 645; -.
KEGG hsa:645; -.
Phylogenomic databases
HOVERGEN P30043; -.
Other
DrugBank DB00157; NADH.
DB00140; Riboflavin.
LinkHub P30043; -.
SOURCE BLVRB; Homo sapiens.
ProtoNet P30043.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Multifunctional enzyme; NADP; Oxidoreductase; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   206  205     Flavin reductase. PRO_0000064948
NP_BIND   5    36  32     NAD or NADP (Potential). 
VARIANT   46    46  1     R -> Q. VAR_019168 [3D]
CONFLICT   16    16        G -> C (in Ref. 8; AA sequence). 
STRAND   5    10  6      
HELIX   14    25  12      
STRAND   29    35  7      
HELIX   37    39  3      
STRAND   42    44  3      
STRAND   48    53  6      
HELIX   58    65  8      
STRAND   69    73  5      
HELIX   86   101  16      
STRAND   105   109  5      
HELIX   112   114  3      
HELIX   123   125  3      
HELIX   126   141  16      
STRAND   144   149  6      
STRAND   152   155  4      
STRAND   164   169  6      
STRAND   174   177  4      
HELIX   178   187  10      
TURN   193   196  4      
STRAND   198   202  5      
Sequence information
Length: 206 AA [This is the length of the unprocessed precursor] Molecular weight: 22119 Da [This is the MW of the unprocessed precursor] CRC64: 3057E6D69A9F9F9F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVKKIAIFG ATGQTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPRPAHV VVGDVLQAAD 

        70         80         90        100        110        120 
VDKTVAGQDA VIVLLGTRND LSPTTVMSEG ARNIVAAMKA HGVDKVVACT SAFLLWDPTK 

       130        140        150        160        170        180 
VPPRLQAVTD DHIRMHKVLR ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD 

       190        200 
LGHFMLRCLT TDEYDGHSTY PSHQYQ 

P30043 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!