Q9D7B6 (ACAD8_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 88.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Isobutyryl-CoA dehydrogenase, mitochondrial EC=1.3.99.- Alternative name(s): Acyl-CoA dehydrogenase family member 8 Short name=ACAD-8 | ||
| 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 › Mus |
Protein attributes
| Sequence length | 413 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 | Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism By similarity. |
| Catalytic activity | Isobutyryl-CoA + ETF = methylacrylyl-CoA + reduced ETF. |
| Cofactor | FAD By similarity. |
| Pathway | |
| Subunit structure | Homotetramer, formed by a dimer of dimers. Subunit of the large multiprotein complex ARC/DRIP By similarity. |
| Subcellular location | Mitochondrion By similarity. |
| Sequence similarities | Belongs to the acyl-CoA dehydrogenase family. |
| Sequence caution | The sequence BAC26664.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Branched-chain amino acid catabolism |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | branched chain family amino acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from direct assay. Source: MGI |
| Molecular function | acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 20 | 20 | Mitochondrion Potential | ||||||
| Chain | 21 – 413 | 393 | Isobutyryl-CoA dehydrogenase, mitochondrial | PRO_0000000523 | |||||
Regions | |||||||||
| Nucleotide binding | 155 – 165 | 11 | FAD By similarity | ||||||
| Nucleotide binding | 156 – 165 | 10 | FAD By similarity | ||||||
| Nucleotide binding | 189 – 191 | 3 | FAD By similarity | ||||||
| Nucleotide binding | 310 – 311 | 2 | FAD; shared with dimeric partner By similarity | ||||||
| Nucleotide binding | 369 – 375 | 7 | FAD By similarity | ||||||
| Nucleotide binding | 398 – 400 | 3 | FAD By similarity | ||||||
| Region | 272 – 275 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 396 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 165 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 300 | 1 | FAD By similarity | ||||||
| Binding site | 300 | 1 | FAD; shared with dimeric partner By similarity | ||||||
| Binding site | 397 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 408 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 207 | 1 | G → E in BAB26255. Ref.1 | ||||||
| Sequence conflict | 207 | 1 | G → E in BAB31764. Ref.1 | ||||||
| Sequence conflict | 207 | 1 | G → E in BAC26664. Ref.1 | ||||||
| Sequence conflict | 207 | 1 | G → E in BAC34521. Ref.1 | ||||||
| Sequence conflict | 207 | 1 | G → E in BAC36757. Ref.1 | ||||||
| Sequence conflict | 254 | 1 | A → P in BAC34521. Ref.1 | ||||||
| Sequence conflict | 413 | 1 | D → RLAPKLESLAWSLCAAGISL DAPMGCSVQVNHEVDQRAEL F in BAB31764. 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. Tissue: Embryo, Pituitary, Skin, Testis and Tongue. |
| [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]. Strain: FVB/N. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK009379 mRNA. Translation: BAB26255.2. AK019502 mRNA. Translation: BAB31764.1. AK029897 mRNA. Translation: BAC26664.1. Different initiation. AK051091 mRNA. Translation: BAC34521.1. AK077335 mRNA. Translation: BAC36757.1. BC037644 mRNA. Translation: AAH37644.1. |
| IPI | IPI00274222. |
| RefSeq | NP_080138.2. NM_025862.2. |
| UniGene | Mm.289244. |
3D structure databases | |
| ProteinModelPortal | Q9D7B6. |
| SMR | Q9D7B6. Positions 30-413. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9D7B6. |
PTM databases | |
| PhosphoSite | Q9D7B6. |
Proteomic databases | |
| PRIDE | Q9D7B6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000060513; ENSMUSP00000054370; ENSMUSG00000031969. |
| GeneID | 66948. |
| KEGG | mmu:66948. |
Organism-specific databases | |
| CTD | 27034. |
| MGI | MGI:1914198. Acad8. |
Phylogenomic databases | |
| eggNOG | roNOG14457. |
| GeneTree | ENSGT00590000082821. |
| HOVERGEN | HBG000224. |
Gene expression databases | |
| ArrayExpress | Q9D7B6. |
| Bgee | Q9D7B6. |
| CleanEx | MM_ACAD8. |
| Genevestigator | Q9D7B6. |
| GermOnline | ENSMUSG00000031969. 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_cen-dom. IPR009075. AcylCo_DH/oxidase_C. IPR013786. AcylCoA_DH/ox_N. IPR009100. AcylCoA_DH/oxidase. [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. |
| KO | K11538. |
| Pfam | PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view] |
| SUPFAM | SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 1 hit. |
| PROSITE | PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 323096. |
| SOURCE | Search... |
Entry information
| Entry name | ACAD8_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9D7B6 Secondary accession number(s): Q8BK36 Q9D2L8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
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