Q64591 (DECR_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 85.
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: 2,4-dienoyl-CoA reductase, mitochondrial EC=1.3.1.34 Alternative name(s): 2,4-dienoyl-CoA reductase [NADPH] Short name=4-enoyl-CoA reductase [NADPH] | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 335 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)
| Function | Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. |
| Catalytic activity | Trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 2,4-dienoyl-CoA reductase (NADPH) activity Traceable author statement Ref.1. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 34 | 34 | Mitochondrion Ref.1 | ||||||
| Chain | 35 – 335 | 301 | 2,4-dienoyl-CoA reductase, mitochondrial | PRO_0000031967 | |||||
Regions | |||||||||
| Nucleotide binding | 62 – 94 | 33 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 199 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 157 | 1 | Substrate By similarity | ||||||
| Binding site | 214 | 1 | NADP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 106 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 110 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 11 | 1 | G → R in AAH59120. Ref.2 | ||||||
| Sequence conflict | 23 | 1 | R → K in BAA00446. Ref.1 | ||||||
| Sequence conflict | 79 | 1 | L → R in BAA00446. Ref.1 | ||||||
| Sequence conflict | 162 | 1 | K → R in BAA00446. Ref.1 | ||||||
| Sequence conflict | 190 | 1 | A → V in BAA00446. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "cDNA cloning of rat liver 2,4-dienoyl-CoA reductase." Hirose A., Kamijo K., Osumi T., Hashimoto T., Mizugaki M. Biochim. Biophys. Acta 1049:346-349(1990) [PubMed: 2383590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-53. Tissue: Liver. |
| [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: Pituitary. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D00569 mRNA. Translation: BAA00446.1. BC059120 mRNA. Translation: AAH59120.1. |
| IPI | IPI00213659. |
| PIR | S11021. |
| RefSeq | NP_476545.2. NM_057197.2. |
| UniGene | Rn.2854. |
3D structure databases | |
| ProteinModelPortal | Q64591. |
| SMR | Q64591. Positions 37-328. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q64591. 1 interaction. |
| STRING | Q64591. |
Proteomic databases | |
| PRIDE | Q64591. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 117543. |
| KEGG | rno:117543. |
| UCSC | BC059120. rat. |
Organism-specific databases | |
| CTD | 1666. |
| RGD | 70999. Decr1. |
Phylogenomic databases | |
| eggNOG | roNOG15274. |
| GeneTree | ENSGT00600000084005. |
| HOVERGEN | HBG005465. |
| InParanoid | Q64591. |
| OrthoDB | EOG4C2HB7. |
| PhylomeDB | Q64591. |
Gene expression databases | |
| ArrayExpress | Q64591. |
| Genevestigator | Q64591. |
| GermOnline | ENSRNOG00000008236. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K13236. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. |
| PROSITE | PS00061. ADH_SHORT. False negative. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 620365. |
Entry information
| Entry name | DECR_RAT | ||||||||
| Accession | Primary (citable) accession number: Q64591 Secondary accession number(s): Q6PCV4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with