Reviewed,
UniProtKB/Swiss-Prot P79274 (ACADL_PIG)
Last modified
September 1, 2009.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Long-chain specific acyl-CoA dehydrogenase, mitochondrial Short name=LCAD EC=1.3.99.13 | ||
| Gene names |
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| Organism | Sus scrofa (Pig) | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 430 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)
| Catalytic activity | Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor. |
| Cofactor | FAD. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Miscellaneous | A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues. |
| Sequence similarities | Belongs to the acyl-CoA dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid metabolism Lipid metabolism |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred 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 long-chain-acyl-CoA dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | Suzuki H., Hamasima N., Kimura M., Yasue H. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| D89478 mRNA. Translation: BAA13965.1. | |
| RefSeq | NP_999062.1. |
| UniGene | Ssc.14530 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1IVH based on UniProtKB P26440. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 396931. |
| KEGG | ssc:396931. |
Organism-specific databases | |
| CTD | 396931. |
Phylogenomic databases | |
| HOVERGEN | P79274. |
Enzyme and pathway databases | |
| BRENDA | 1.3.99.13. 249. |
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... |
Entry information
| Entry name | ACADL_PIG | ||||||||
| Accession | Primary (citable) accession number: P79274 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


