Reviewed,
UniProtKB/Swiss-Prot Q9BY49 (PECR_HUMAN)
Last modified
January 19, 2010.
Version 79.
History...
Clusters with 100%,
90%,
50% identity |
Documents (7) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peroxisomal trans-2-enoyl-CoA reductase EC=1.3.1.38 Alternative name(s): TERP HPDHase pVI-ARL 2,4-dienoyl-CoA reductase-related protein Short name=DCR-RP | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 303 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity. |
| Catalytic activity | Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH. Ref.1 |
| Pathway | |
| Subunit structure | Interacts with PEX5, probably required to target it into peroxisomes. Ref.2 |
| Subcellular location | |
| Induction | Not induced by IR. Ref.9 |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fatty acid biosynthesis Lipid synthesis |
| Cellular component | Peroxisome |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW regulation of apoptosisInferred from electronic annotation. Source: InterPro |
| Cellular component | peroxisome Ref.1 Non-traceable author statement. Source: ProtInc |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro trans-2-enoyl-CoA reductase (NADPH) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9BY49-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q9BY49-2) The sequence of this isoform differs from the canonical sequence as follows: 1-146: Missing. |
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_0000054740 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 23 – 47 | 25 | NADP By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Motif | 301 – 303 | 3 | Microbody targeting signal | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 179 | 1 | Proton acceptor By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 179 | 1 | Phosphotyrosine Ref.10 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 146 | 146 | Missing in isoform 2. | VSP_013260 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 149 | 1 | E → K: dbSNP rs1429148. | VAR_021535 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 297 | 1 | F → L: dbSNP rs9288513. | VAR_021536 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 303 | 1 | Missing: Abolishes localization to peroxisomes. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 22 | 1 | I → F in CAB89810. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 129 | 1 | E → R in CAB89810. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 135 | 1 | T → S in CAB89810. Ref.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 248 | 1 | S → P in CAG33426. Ref.5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 13 – 18 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 20 – 24 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 25 – 27 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 29 – 40 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 44 – 50 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 52 – 64 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 74 – 78 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 84 – 98 | 15 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 103 – 106 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 116 – 118 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 121 – 131 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 133 – 145 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 147 – 150 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 152 – 157 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 169 – 188 | 20 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 190 – 192 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 194 – 201 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 208 – 210 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 214 – 221 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 224 – 227 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 237 – 247 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 249 – 251 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 258 – 262 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 265 – 267 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 288 – 302 | 15 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs." Das A.K., Uhler M.D., Hajra A.K. J. Biol. Chem. 275:24333-24340(2000) [PubMed: 10811639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY. |
| [2] | "Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology." Amery L., Mannaerts G.P., Subramani S., Van Veldhoven P.P., Fransen M. Comb. Chem. High Throughput Screen. 4:545-552(2001) [PubMed: 11669066] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PEX5, MUTAGENESIS OF LEU-303. |
| [3] | "A novel gene expressed in human liver non-tumor tissues." Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Liver. |
| [4] | "Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver." Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Fetal liver. |
| [5] | "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). |
| [6] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon. |
| [7] | "Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [8] | "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] (ISOFORM 1). Tissue: Placenta. |
| [9] | "Ku86 autoantigen related protein-1 transcription initiates from a CpG island and is induced by p53 through a nearby p53 response element." Braastad C.D., Leguia M., Hendrickson E.A. Nucleic Acids Res. 30:1713-1724(2002) [PubMed: 11937624] [Abstract] Cited for: INDUCTION. |
| [10] | "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J.Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-179, MASS SPECTROMETRY. |
| [11] | "Crystal structure of perixomal trans 2-enoyl CoA reductase (PECRA)." Structural genomics consortium (SGC) Submitted (MAY-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADENINE AND PHOSPHATE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AF232009 mRNA. Translation: AAF69798.1. Different initiation. AJ250303 mRNA. Translation: CAB89810.1. AF212234 mRNA. Translation: AAK14920.1. AF119841 mRNA. Translation: AAF69595.1. CR457145 mRNA. Translation: CAG33426.1. AK315795 mRNA. Translation: BAG38139.1. AC010686 Genomic DNA. Translation: AAY14657.1. BC002529 mRNA. Translation: AAH02529.1. | ||||||||||||
| IPI | IPI00554710. IPI00744627. | ||||||||||||
| RefSeq | NP_060911.2. | ||||||||||||
| UniGene | Hs.281680 | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | Q9BY49. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q9BY49. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q9BY49. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000265322; ENSP00000265322; ENSG00000115425; Homo sapiens. [Genome view] | ||||||||||||
| GeneID | 55825. | ||||||||||||
| KEGG | hsa:55825. | ||||||||||||
| UCSC | uc002vfr.1. human. uc002vft.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 55825. | ||||||||||||
| GeneCards | GC02M216611. | ||||||||||||
| H-InvDB | HIX0002806. | ||||||||||||
| HGNC | HGNC:18281. PECR. | ||||||||||||
| HPA | HPA021593. HPA022539. | ||||||||||||
| MIM | 605843. gene. | ||||||||||||
| PharmGKB | PA134967510. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | prNOG07392. | ||||||||||||
| HOVERGEN | Q9BY49. | ||||||||||||
| InParanoid | Q9BY49. | ||||||||||||
| OMA | ARVIPIQ. | ||||||||||||
| PhylomeDB | Q9BY49. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 1.3.1.38. 247. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q9BY49. | ||||||||||||
| Bgee | Q9BY49. | ||||||||||||
| CleanEx | HS_PECR. | ||||||||||||
| Genevestigator | Q9BY49. | ||||||||||||
| GermOnline | ENSG00000115425. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR000712. Bcl2_BH. 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. | ||||||||||||
| SMART | SM00337. BCL. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS00061. ADH_SHORT. False negative. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| DrugBank | DB00173. Adenine. | ||||||||||||
| NextBio | 61022. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | PECR_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9BY49 Secondary accession number(s): B2RE42 Q9P1A4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 2 Human chromosome 2: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


