Reviewed,
UniProtKB/Swiss-Prot P08461 (ODP2_RAT)
Last modified
November 3, 2009.
Version 100.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial EC=2.3.1.12 Alternative name(s): Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex PDC-E2 Short name=E2 70 kDa mitochondrial autoantigen of primary biliary cirrhosis Short name=PBC | ||
| 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 | 632 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 | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). |
| Catalytic activity | Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. |
| Cofactor | Binds 1 lipoyl cofactor covalently. |
| Subunit structure | 20 to 30 alpha(2)-beta2 tetramers of E1 + 6 homodimers of E3 + 60 copies of E2. |
| Subcellular location | |
| Tissue specificity | Expressed in flagella of epididymal sperm. Ref.5 |
| Involvement in disease | Primary biliary cirrhosis (PBC) is an autoimmune disease characterized by inflammatory obliteration of intra-hepatic bile duct, leading to liver cell damage and cirrhosis. The E2 component of pyruvate dehydrogenase complex is the autoantigen for PBC. |
| Sequence similarities | Belongs to the 2-oxoacid dehydrogenase family. Contains 2 lipoyl-binding domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Domain | Lipoyl Repeat Transit peptide |
| Molecular function | Acyltransferase Transferase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay. Source: RGD glycolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell pyruvate dehydrogenase complex Ref.2Inferred from direct assay. Source: RGD |
| Molecular function | dihydrolipoyllysine-residue acetyltransferase activity Ref.2 Inferred from direct assay. Source: RGD lipoic acid bindingInferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Ref.2Traceable author statement. Source: RGD protein 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 – 77 | 77 | Mitochondrion Ref.2 | ||||||
| Chain | 78 – 632 | 555 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial | PRO_0000162298 | |||||
Regions | |||||||||
| Domain | 83 – 157 | 75 | Lipoyl-binding 1 | ||||||
| Domain | 209 – 283 | 75 | Lipoyl-binding 2 | ||||||
| Region | 344 – 375 | 32 | E3- and/or E1-component binding domain Potential | ||||||
| Region | 456 – 632 | 177 | Catalytic By similarity | ||||||
| Region | 600 – 611 | 12 | CoA-binding By similarity | ||||||
Sites | |||||||||
| Active site | 605 | 1 | Potential | ||||||
| Active site | 609 | 1 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 249 | 1 | N6-lipoyllysine | ||||||
| Modified residue | 451 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 150 – 152 | 3 | VGS → IGC in BAA01504. Ref.2 | ||||||
| Sequence conflict | 163 – 164 | 2 | DI → GP in BAA20956. Ref.3 | ||||||
| Sequence conflict | 163 – 164 | 2 | DI → GP in AAA41813. Ref.3 | ||||||
| Sequence conflict | 601 – 632 | 32 | LSCDH…VTMLL → HSAVIIELWMEQLEPSGLL in BAA20956. Ref.3 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "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: Testis. |
| [2] | "Molecular cloning of dihydrolipoamide acetyltransferase of the rat pyruvate dehydrogenase complex: sequence comparison and evolutionary relationship to other dihydrolipoamide acyltransferases." Matuda S., Nakano K., Ohta S., Shimura M., Yamanaka T., Nakagawa S., Titani K., Miyata T. Biochim. Biophys. Acta 1131:114-118(1992) [PubMed: 1581353] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-632, PROTEIN SEQUENCE OF 78-91. Tissue: Heart. |
| [3] | "Identification and specificity of a cDNA encoding the 70 kd mitochondrial antigen recognized in primary biliary cirrhosis." Gershwin M.E., McKay I.R., Sturgess A., Coppel R.L. J. Immunol. 138:3525-3531(1987) [PubMed: 3571977] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-632. Tissue: Liver. |
| [4] | Lubec G., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 397-414, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus. |
| [5] | "Identification of novel immunodominant epididymal sperm proteins using combinatorial approach." Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V. Reproduction 138:81-93(2009) [PubMed: 19423663] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| BC107440 mRNA. Translation: AAI07441.1. D10655 mRNA. Translation: BAA01504.1. D00092 mRNA. Translation: BAA20956.1. M16075 mRNA. Translation: AAA41813.1. | |
| IPI | IPI00231714. |
| PIR | S21766. |
| RefSeq | NP_112287.1. |
| UniGene | Rn.15413 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FYC based on UniProtKB P10515. |
| SMR | P08461. Positions 83-173, 204-296. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P08461. |
Proteomic databases | |
| PRIDE | P08461. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000032152; ENSRNOP00000032890; ENSRNOG00000009994; Rattus norvegicus. [Genome view] |
| GeneID | 81654. |
| KEGG | rno:81654. |
| NMPDR | fig|10116.3.peg.28575. |
| UCSC | NM_031025. rat. |
Organism-specific databases | |
| CTD | 81654. |
| RGD | 619859. Dlat. |
Phylogenomic databases | |
| HOVERGEN | P08461. |
| OMA | ISNLGMN. |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.12. 248. |
Gene expression databases | |
| ArrayExpress | P08461. |
| Genevestigator | P08461. |
| GermOnline | ENSRNOG00000009994. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR006257. AcTrfase_Pyrv_DH_cplx_L. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view] |
| Gene3D | G3DSA:4.10.320.10. E3_bd. 1 hit. |
| Pfam | PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 2 hits. PF02817. E3_binding. 1 hit. [Graphical view] |
| ProDom | PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01349. PDHac_trf_mito. 1 hit. |
| PROSITE | PS50968. BIOTINYL_LIPOYL. 2 hits. PS00189. LIPOYL. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 615200. |
Entry information
| Entry name | ODP2_RAT | ||||||||
| Accession | Primary (citable) accession number: P08461 Secondary accession number(s): Q3B7V7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


