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Protein

Biliverdin reductase A

Gene

Blvra

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.By similarity

Catalytic activityi

Bilirubin + NAD(P)+ = biliverdin + NAD(P)H.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi: protoheme degradation

This protein is involved in the pathway protoheme degradation, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway protoheme degradation and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971NAD or NADP; via carbonyl oxygenBy similarity
Metal bindingi279 – 2791ZincSequence analysis
Metal bindingi280 – 2801ZincSequence analysis
Metal bindingi291 – 2911ZincSequence analysis
Metal bindingi292 – 2921ZincSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 206NAD or NADPBy similarity
Nucleotide bindingi76 – 794NAD or NADPBy similarity

GO - Molecular functioni

  • biliverdin reductase activity Source: MGI
  • nucleotide binding Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-189483. Heme degradation.
UniPathwayiUPA00684.

Names & Taxonomyi

Protein namesi
Recommended name:
Biliverdin reductase A (EC:1.3.1.24)
Short name:
BVR A
Alternative name(s):
Biliverdin-IX alpha-reductase
Gene namesi
Name:Blvra
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:88170. Blvra.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22By similarityPRO_0000010854
Chaini3 – 295293Biliverdin reductase APRO_0000010855Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541PhosphoserineCombined sources
Modified residuei173 – 1731PhosphothreonineBy similarity
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei229 – 2291PhosphoserineBy similarity
Modified residuei247 – 2471N6-acetyllysineBy similarity
Modified residuei252 – 2521N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CY64.
MaxQBiQ9CY64.
PaxDbiQ9CY64.
PRIDEiQ9CY64.

PTM databases

iPTMnetiQ9CY64.
PhosphoSiteiQ9CY64.

Expressioni

Gene expression databases

BgeeiQ9CY64.
CleanExiMM_BLVRA.
ExpressionAtlasiQ9CY64. baseline and differential.
GenevisibleiQ9CY64. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ9CY64. 2 interactions.
MINTiMINT-1854695.
STRINGi10090.ENSMUSP00000002064.

Structurei

3D structure databases

ProteinModelPortaliQ9CY64.
SMRiQ9CY64. Positions 8-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 166Poly-Val

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IH7U. Eukaryota.
ENOG4111FZX. LUCA.
GeneTreeiENSGT00390000011072.
HOGENOMiHOG000231884.
HOVERGENiHBG003218.
InParanoidiQ9CY64.
KOiK00214.
OMAiHVAFICT.
OrthoDBiEOG78WKS5.
PhylomeDBiQ9CY64.
TreeFamiTF342889.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR017094. Biliverdin_Rdtase_A.
IPR015249. Biliverdin_Rdtase_cat.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF09166. Biliv-reduc_cat. 1 hit.
PF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
PIRSFiPIRSF037032. Biliverdin_reductase_A. 1 hit.
ProDomiPD040165. Biliverdin_Rdtase_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CY64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTEPKRKFG VVVVGVGRAG SVRIRDLKDP HSSAFLNLIG YVSRRELGSL
60 70 80 90 100
DNVRQISLED ALRSQEVDVA YICTESSSHE DYIRQFLQAG KHVLVEYPMA
110 120 130 140 150
LSFAAAQELW ELAAQKGRVL HEEHIELLME EFEFLKREVA GKELLKGSLR
160 170 180 190 200
FTASPLEEEK FGFPAFSGIS RLTWLVSLFG ELSLISATME NRKEDQYMKM
210 220 230 240 250
TVQLETQNKS PLSWIEEKGP GLKRNRHISI HFKSGSLEEV PNVGVNKNIF
260 270 280 290
LKDQDIFIQK LLGQVSAEDL AAEKKRILHC LELASDIQRL CHRKQ
Length:295
Mass (Da):33,525
Last modified:June 1, 2001 - v1
Checksum:iF2E1682BD77032A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271L → S in AAH52146 (PubMed:15489334).Curated
Sequence conflicti295 – 2951Q → QWGGSFRYL in BAB21950 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002231 mRNA. Translation: BAB21950.1.
AK010847 mRNA. Translation: BAB27219.1.
AK172620 mRNA. Translation: BAE43098.1.
BC052146 mRNA. Translation: AAH52146.1.
CCDSiCCDS16692.1.
RefSeqiNP_080954.4. NM_026678.4.
XP_006498634.1. XM_006498571.2.
XP_006498635.1. XM_006498572.2.
UniGeneiMm.22028.

Genome annotation databases

EnsembliENSMUST00000002064; ENSMUSP00000002064; ENSMUSG00000001999.
GeneIDi109778.
KEGGimmu:109778.
UCSCiuc008meq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002231 mRNA. Translation: BAB21950.1.
AK010847 mRNA. Translation: BAB27219.1.
AK172620 mRNA. Translation: BAE43098.1.
BC052146 mRNA. Translation: AAH52146.1.
CCDSiCCDS16692.1.
RefSeqiNP_080954.4. NM_026678.4.
XP_006498634.1. XM_006498571.2.
XP_006498635.1. XM_006498572.2.
UniGeneiMm.22028.

3D structure databases

ProteinModelPortaliQ9CY64.
SMRiQ9CY64. Positions 8-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CY64. 2 interactions.
MINTiMINT-1854695.
STRINGi10090.ENSMUSP00000002064.

PTM databases

iPTMnetiQ9CY64.
PhosphoSiteiQ9CY64.

Proteomic databases

EPDiQ9CY64.
MaxQBiQ9CY64.
PaxDbiQ9CY64.
PRIDEiQ9CY64.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002064; ENSMUSP00000002064; ENSMUSG00000001999.
GeneIDi109778.
KEGGimmu:109778.
UCSCiuc008meq.1. mouse.

Organism-specific databases

CTDi644.
MGIiMGI:88170. Blvra.

Phylogenomic databases

eggNOGiENOG410IH7U. Eukaryota.
ENOG4111FZX. LUCA.
GeneTreeiENSGT00390000011072.
HOGENOMiHOG000231884.
HOVERGENiHBG003218.
InParanoidiQ9CY64.
KOiK00214.
OMAiHVAFICT.
OrthoDBiEOG78WKS5.
PhylomeDBiQ9CY64.
TreeFamiTF342889.

Enzyme and pathway databases

UniPathwayiUPA00684.
ReactomeiR-MMU-189483. Heme degradation.

Miscellaneous databases

NextBioi362743.
PROiQ9CY64.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CY64.
CleanExiMM_BLVRA.
ExpressionAtlasiQ9CY64. baseline and differential.
GenevisibleiQ9CY64. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR017094. Biliverdin_Rdtase_A.
IPR015249. Biliverdin_Rdtase_cat.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
PfamiPF09166. Biliv-reduc_cat. 1 hit.
PF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
PIRSFiPIRSF037032. Biliverdin_reductase_A. 1 hit.
ProDomiPD040165. Biliverdin_Rdtase_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryonic liver, Kidney and Spleen.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiBIEA_MOUSE
AccessioniPrimary (citable) accession number: Q9CY64
Secondary accession number(s): Q3T9C6, Q80WR6, Q9DD21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7). NADPH, however, is the probable reactant in biological systems (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.