Reviewed,
UniProtKB/Swiss-Prot Q9WVK3 (PECR_RAT)
Last modified
October 13, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Peroxisomal trans-2-enoyl-CoA reductase EC=1.3.1.38 Alternative name(s): RLF98 Peroxisomal 2,4-dienoyl-CoA reductase PX-2,4-DCR1 | ||
| 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 | 303 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity By similarity. |
| Catalytic activity | Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH. |
| Pathway | |
| Subunit structure | Interacts with PEX5, probably required to target it into peroxisomes By similarity. |
| Subcellular location | Peroxisome By similarity. |
| Tissue specificity | Highly expressed in liver and kidney. Weakly expressed in other tissues. Ref.1 |
| Induction | Up-regulated by fasting. Ref.1 |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Cellular component | Peroxisome |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB peroxisomeInferred from direct assay. Source: HGNC |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro trans-2-enoyl-CoA reductase (NADPH) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 303 | 303 | Peroxisomal trans-2-enoyl-CoA reductase | PRO_0000054743 | |||||
Regions | |||||||||
| Nucleotide binding | 23 – 47 | 25 | NADP By similarity | ||||||
| Motif | 301 – 303 | 3 | Microbody targeting signal By similarity | ||||||
Sites | |||||||||
| Active site | 179 | 1 | Proton acceptor By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 179 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and characterization of a new fasting-inducible short-chain dehydrogenase/reductase from rat liver." Zhang J., Underwood L.E. Biochim. Biophys. Acta 1435:184-190(1999) [PubMed: 10561551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Strain: Sprague-Dawley. Tissue: Liver. |
| [2] | "Mitochondria and peroxisomes contain distinct isoforms of 2,4-dienoyl CoA reductase that interact with an Hsp70 member: isolation and characterisation of a cDNA encoding rat peroxisomal 2,4-dienoyl CoA reductase." Naylor D.J., Koivurantac K.T., Stines A.P., Hiltunen J.K., Hoogenraad N.J., Hoj P.B. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. 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]. Tissue: Pituitary. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF099742 mRNA. Translation: AAD38447.1. AF021854 mRNA. Translation: AAF14047.1. BC060546 mRNA. Translation: AAH60546.1. | |
| IPI | IPI00326195. |
| RefSeq | NP_579833.1. |
| UniGene | Rn.163081 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AE1 based on UniProtKB P50162. |
| SMR | Q9WVK3. Positions 7-303. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q9WVK3. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000021512; ENSRNOP00000021512; ENSRNOG00000015809; Rattus norvegicus. [Genome view] |
| GeneID | 113956. |
| KEGG | rno:113956. |
Organism-specific databases | |
| CTD | 113956. |
| RGD | 70925. Pecr. |
Phylogenomic databases | |
| HOVERGEN | Q9WVK3. |
Enzyme and pathway databases | |
| BRENDA | 1.3.1.38. 248. |
Gene expression databases | |
| ArrayExpress | Q9WVK3. |
| Genevestigator | Q9WVK3. |
| GermOnline | ENSRNOG00000015809. 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. |
| PANTHER | PTHR19410. ADH_short_C2. 1 hit. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. |
| PROSITE | PS00061. ADH_SHORT. False negative. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 618083. |
Entry information
| Entry name | PECR_RAT | ||||||||
| Accession | Primary (citable) accession number: Q9WVK3 | ||||||||
| Entry history |
| ||||||||
| 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


