Reviewed,
UniProtKB/Swiss-Prot Q9JHI5 (IVD_MOUSE)
Last modified
November 3, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Isovaleryl-CoA dehydrogenase, mitochondrial Short name=IVD EC=1.3.99.10 | ||
| 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 | 424 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 3-methylbutanoyl-CoA + acceptor = 3-methylbut-2-enoyl-CoA + reduced acceptor. |
| Cofactor | FAD. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Post-translational modification | Acetylation of Lys-76 is observed in liver mitochondria from fasted mice but not from fed mice. |
| Sequence similarities | Belongs to the acyl-CoA dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro isovaleryl-CoA dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 30 | 30 | Mitochondrion By similarity | ||||||
| Chain | 31 – 424 | 394 | Isovaleryl-CoA dehydrogenase, mitochondrial | PRO_0000000532 | |||||
Sites | |||||||||
| Active site | 284 | 1 | Proton acceptor By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 76 | 1 | N6-acetyllysine Ref.5 | ||||||
Experimental info | |||||||||
| Sequence conflict | 29 | 1 | R → G in BAB23751. Ref.2 | ||||||
| Sequence conflict | 41 | 1 | N → K in BAB30859. Ref.2 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Cloning of genomic and cDNA for mouse isovaleryl-CoA dehydrogenase (IVD) and evolutionary comparison to other known IVDs." Willard J.M., Reinard T., Mohsen A.W., Vockley J. Gene 270:253-257(2001) [PubMed: 11404023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: 129/Ola. |
| [2] | "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. Tissue: Liver. |
| [3] | "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]. Strain: FVB/N. Tissue: Kidney and Salivary gland. |
| [4] | Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 57-76; 154-178; 212-221; 231-239; 273-285; 339-346; 400-411 AND 418-424, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain. |
| [5] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-76, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF225989 mRNA. Translation: AAF35888.1. AF226043 AF226042 Genomic DNA. Translation: AAF67667.1. AK005024 mRNA. Translation: BAB23751.1. AK017660 mRNA. Translation: BAB30859.1. BC018325 mRNA. Translation: AAH18325.1. BC027198 mRNA. Translation: AAH27198.1. | |
| IPI | IPI00471246. |
| RefSeq | NP_062800.1. |
| UniGene | Mm.6635 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1IVH based on UniProtKB P26440. |
| SMR | Q9JHI5. Positions 36-422. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9JHI5. |
PTM databases | |
| PhosphoSite | Q9JHI5. |
2-D gel databases | |
| REPRODUCTION-2DPAGE | Q9JHI5. |
Proteomic databases | |
| PRIDE | Q9JHI5. |
Genome annotation databases | |
| Ensembl | ENSMUST00000028807; ENSMUSP00000028807; ENSMUSG00000027332; Mus musculus. [Genome view] |
| GeneID | 56357. |
| KEGG | mmu:56357. |
| NMPDR | fig|10090.3.peg.6671. |
| UCSC | uc008lsv.1. mouse. |
Organism-specific databases | |
| CTD | 56357. |
| MGI | MGI:1929242. Ivd. |
Phylogenomic databases | |
| HOGENOM | Q9JHI5. |
| HOVERGEN | Q9JHI5. |
| OMA | KHAREDD. |
Enzyme and pathway databases | |
| BRENDA | 1.3.99.10. 244. |
Gene expression databases | |
| ArrayExpress | Q9JHI5. |
| Bgee | Q9JHI5. |
| CleanEx | MM_IVD. |
| Genevestigator | Q9JHI5. |
| GermOnline | ENSMUSG00000027332. Mus musculus. |
Family and domain databases | |
| InterPro | IPR006089. Acyl-CoA_DH_CS. IPR006092. Acyl-CoA_DH_N. IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view] |
| Gene3D | G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit. |
| Pfam | PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view] |
| PROSITE | PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 312370. |
| SOURCE | Search... |
Entry information
| Entry name | IVD_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9JHI5 Secondary accession number(s): Q9CYI3, Q9DBD7 | ||||||||
| Entry history |
| ||||||||
| 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


