Reviewed,
UniProtKB/Swiss-Prot Q9CY64 (BIEA_MOUSE)
Last modified
January 19, 2010.
Version 65.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Biliverdin reductase A Short name=BVR A EC=1.3.1.24 Alternative name(s): Biliverdin-IX alpha-reductase | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 295 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
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 | |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding NAD NADP Zinc |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | heme catabolic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | biliverdin reductase activity Inferred from direct assay. Source: MGI zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Propeptide | 1 – 2 | 2 | By similarity | PRO_0000010854 | |||||
| Chain | 3 – 295 | 293 | Biliverdin reductase A | PRO_0000010855 | |||||
Regions | |||||||||
| Nucleotide binding | 15 – 20 | 6 | NAD or NADP By similarity | ||||||
| Nucleotide binding | 76 – 79 | 4 | NAD or NADP By similarity | ||||||
| Compositional bias | 11 – 16 | 6 | Poly-Val | ||||||
Sites | |||||||||
| Metal binding | 279 | 1 | Zinc Potential | ||||||
| Metal binding | 280 | 1 | Zinc Potential | ||||||
| Metal binding | 291 | 1 | Zinc Potential | ||||||
| Metal binding | 292 | 1 | Zinc Potential | ||||||
| Binding site | 97 | 1 | NAD or NADP; via carbonyl oxygen By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
| Modified residue | 173 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 177 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 229 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 236 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 247 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 252 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 27 | 1 | L → S in AAH52146. Ref.2 | ||||||
| Sequence conflict | 295 | 1 | Q → QWGGSFRYL in BAB21950. Ref.1 | ||||||
Sequences
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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. 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. |
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. |
| IPI | IPI00330627. |
| RefSeq | NP_080954.4. |
| UniGene | Mm.22028 |
3D structure databases | |
| SMR | Q9CY64. Positions 1-292. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9CY64. |
PTM databases | |
| PhosphoSite | Q9CY64. |
Proteomic databases | |
| PRIDE | Q9CY64. |
Genome annotation databases | |
| Ensembl | ENSMUST00000002064; ENSMUSP00000002064; ENSMUSG00000001999; Mus musculus. [Genome view] |
| GeneID | 109778. |
| KEGG | mmu:109778. |
| NMPDR | fig|10090.3.peg.6848. |
| UCSC | uc008meq.1. mouse. |
Organism-specific databases | |
| CTD | 109778. |
| MGI | MGI:88170. Blvra. |
Phylogenomic databases | |
| HOGENOM | HBG717259. |
| HOVERGEN | Q9CY64. |
| InParanoid | Q9CY64. |
| OMA | EERKEDQ. |
| OrthoDB | EOG9T4GDM. |
| PhylomeDB | Q9CY64. |
Enzyme and pathway databases | |
| BRENDA | 1.3.1.24. 244. |
Gene expression databases | |
| ArrayExpress | Q9CY64. |
| Bgee | Q9CY64. |
| CleanEx | MM_BLVRA. |
| Genevestigator | Q9CY64. |
| GermOnline | ENSMUSG00000001999. Mus musculus. |
Family and domain databases | |
| InterPro | IPR017094. Biliverdin_Rdtase_A. IPR015249. Biliverdin_Rdtase_cat. IPR016040. NAD(P)-bd_dom. IPR000683. Oxidoreductase_N. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF09166. Biliv-reduc_cat. 1 hit. PF01408. GFO_IDH_MocA. 1 hit. [Graphical view] |
| PIRSF | PIRSF037032. Biliverdin_reductase_A. 1 hit. |
| ProDom | PD040165. Biliverdin_Rdtase_cat. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 362743. |
| SOURCE | Search... |
Entry information
| Entry name | BIEA_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9CY64 Secondary accession number(s): Q3T9C6, Q80WR6, Q9DD21 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
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 |

Clusters with


