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Reviewed, UniProtKB/Swiss-Prot Q9CY64 (BIEA_MOUSE)

Last modified January 19, 2010. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Biliverdin reductase A
      Short name=BVR A
    EC=1.3.1.24
Alternative name(s):
    Biliverdin-IX alpha-reductase
Gene names
Name: Blvra
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Pathway

Porphyrin metabolism; protoheme degradation.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Sequence similarities

Belongs to the gfo/idh/mocA family. Biliverdin reductase subfamily.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
NADP
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
Gene Ontology (GO)
   Biological processheme catabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbiliverdin reductase activity

Inferred from direct assay. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22 By similarity
PRO_0000010854
Chain3 – 295293Biliverdin reductase A
PRO_0000010855

Regions

Nucleotide binding15 – 206NAD or NADP By similarity
Nucleotide binding76 – 794NAD or NADP By similarity
Compositional bias11 – 166Poly-Val

Sites

Metal binding2791Zinc Potential
Metal binding2801Zinc Potential
Metal binding2911Zinc Potential
Metal binding2921Zinc Potential
Binding site971NAD or NADP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1731Phosphothreonine By similarity
Modified residue1771Phosphoserine By similarity
Modified residue2291Phosphoserine By similarity
Modified residue2361Phosphoserine By similarity
Modified residue2471N6-acetyllysine By similarity
Modified residue2521N6-acetyllysine By similarity

Experimental info

Sequence conflict271L → S in AAH52146. Ref.2
Sequence conflict2951Q → QWGGSFRYL in BAB21950. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9CY64-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F2E1682BD77032A4

FASTA29533,525
        10         20         30         40         50         60 
MSTEPKRKFG VVVVGVGRAG SVRIRDLKDP HSSAFLNLIG YVSRRELGSL DNVRQISLED 

        70         80         90        100        110        120 
ALRSQEVDVA YICTESSSHE DYIRQFLQAG KHVLVEYPMA LSFAAAQELW ELAAQKGRVL 

       130        140        150        160        170        180 
HEEHIELLME EFEFLKREVA GKELLKGSLR FTASPLEEEK FGFPAFSGIS RLTWLVSLFG 

       190        200        210        220        230        240 
ELSLISATME NRKEDQYMKM TVQLETQNKS PLSWIEEKGP GLKRNRHISI HFKSGSLEEV 

       250        260        270        280        290 
PNVGVNKNIF LKDQDIFIQK LLGQVSAEDL AAEKKRILHC LELASDIQRL CHRKQ

« Hide

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References

[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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK002231 mRNA. Translation: BAB21950.1.
AK010847 mRNA. Translation: BAB27219.1.
AK172620 mRNA. Translation: BAE43098.1.
BC052146 mRNA. Translation: AAH52146.1.
IPIIPI00330627.
RefSeqNP_080954.4.
UniGeneMm.22028

3D structure databases

SMRQ9CY64. Positions 1-292.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9CY64.

PTM databases

PhosphoSiteQ9CY64.

Proteomic databases

PRIDEQ9CY64.

Genome annotation databases

EnsemblENSMUST00000002064; ENSMUSP00000002064; ENSMUSG00000001999; Mus musculus. [Genome view]
GeneID109778.
KEGGmmu:109778.
NMPDRfig|10090.3.peg.6848.
UCSCuc008meq.1. mouse.

Organism-specific databases

CTD109778.
MGIMGI:88170. Blvra.

Phylogenomic databases

HOGENOMHBG717259.
HOVERGENQ9CY64.
InParanoidQ9CY64.
OMAEERKEDQ.
OrthoDBEOG9T4GDM.
PhylomeDBQ9CY64.

Enzyme and pathway databases

BRENDA1.3.1.24. 244.

Gene expression databases

ArrayExpressQ9CY64.
BgeeQ9CY64.
CleanExMM_BLVRA.
GenevestigatorQ9CY64.
GermOnlineENSMUSG00000001999. Mus musculus.

Family and domain databases

InterProIPR017094. Biliverdin_Rdtase_A.
IPR015249. Biliverdin_Rdtase_cat.
IPR016040. NAD(P)-bd_dom.
IPR000683. Oxidoreductase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF09166. Biliv-reduc_cat. 1 hit.
PF01408. GFO_IDH_MocA. 1 hit.
[Graphical view]
PIRSFPIRSF037032. Biliverdin_reductase_A. 1 hit.
ProDomPD040165. Biliverdin_Rdtase_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other Resources

NextBio362743.
SOURCESearch...

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Entry information

Entry nameBIEA_MOUSE
AccessionPrimary (citable) accession number: Q9CY64
Secondary accession number(s): Q3T9C6, Q80WR6, Q9DD21
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2001
Last modified: January 19, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents