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P08461

- ODP2_RAT

UniProt

P08461 - ODP2_RAT

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

Dlat

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (12 Dec 2006)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.

    Catalytic activityi

    Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei605 – 6051Sequence Analysis
    Active sitei609 – 6091Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: RGD
    2. nucleotide binding Source: RGD

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: RGD
    2. glucose metabolic process Source: UniProtKB-KW
    3. sleep Source: RGD
    4. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

    Enzyme and pathway databases

    ReactomeiREACT_203088. Pyruvate metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
    Alternative name(s):
    70 kDa mitochondrial autoantigen of primary biliary cirrhosis
    Short name:
    PBC
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
    Pyruvate dehydrogenase complex component E2
    Short name:
    PDC-E2
    Short name:
    PDCE2
    Gene namesi
    Name:Dlat
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi619859. Dlat.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: RGD
    3. pyruvate dehydrogenase complex Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    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.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7777Mitochondrion1 PublicationAdd
    BLAST
    Chaini78 – 632555Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialPRO_0000162298Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei123 – 1231N6-lipoyllysine1 Publication
    Modified residuei249 – 2491N6-lipoyllysine1 Publication
    Modified residuei451 – 4511N6-acetyllysineBy similarity
    Modified residuei458 – 4581N6-succinyllysineBy similarity
    Modified residuei532 – 5321N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP08461.
    PRIDEiP08461.

    2D gel databases

    World-2DPAGE0004:P08461.

    PTM databases

    PhosphoSiteiP08461.

    Expressioni

    Tissue specificityi

    Expressed in flagella of epididymal sperm.1 Publication

    Gene expression databases

    GenevestigatoriP08461.

    Interactioni

    Subunit structurei

    Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Interacts with PDK2 and PDK3 By similarity.By similarity

    Protein-protein interaction databases

    IntActiP08461. 1 interaction.
    STRINGi10116.ENSRNOP00000032890.

    Structurei

    3D structure databases

    ProteinModelPortaliP08461.
    SMRiP08461. Positions 83-173, 204-305, 394-632.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini83 – 15775Lipoyl-binding 1Add
    BLAST
    Domaini209 – 28375Lipoyl-binding 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni344 – 37532E3- and/or E1-component binding domainSequence AnalysisAdd
    BLAST
    Regioni456 – 632177CatalyticBy similarityAdd
    BLAST
    Regioni600 – 61112CoA-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 2 lipoyl-binding domains.Curated

    Keywords - Domaini

    Lipoyl, Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    GeneTreeiENSGT00740000115255.
    HOGENOMiHOG000281566.
    HOVERGENiHBG005063.
    InParanoidiP08461.
    KOiK00627.
    OMAiPISNIRK.
    OrthoDBiEOG7K3TKW.
    PhylomeDBiP08461.
    TreeFamiTF106145.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08461-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWRVCARRVQ SAVPRAGFRA RWATLKGPRT GPAAVRCGSG IPSYGVRSLC    50
    GWSYGSATVP RNRILQQLLG SPSRRSYSLP PHQKVPLPSL SPTMQAGTIA 100
    RWEKKEGEKI SEGDLIAEVE TDKATVGFES LEECYMAKIL VPEGTRDVPV 150
    GSIICITVEK PQDIEAFKNY TLDSATAATQ AAPAPAAAPA AAPAAPSASA 200
    PGSSYPVHMQ IVLPALSPTM TMGTVQRWEK KVGEKLSEGD LLAEIETDKA 250
    TIGFEVQEEG YLAKILVPEG TRDVPLGTPL CIIVEKQEDI AAFADYRPTE 300
    VTSLKPQAPP PVPPPVAAVP PIPQPLAPTP SAAPAGPKGR VFVSPLAKKL 350
    AAEKGIDLTQ VKGTGPEGRI IKKDIDSFVP TKAAPAAAAA APPGPRVAPT 400
    PAGVFIDIPI SNIRRVIAQR LMQSKQTIPH YYLSVDVNMG EVLLVRKELN 450
    KMLEGKGKIS VNDFIIKASA LACLKVPEAN SSWMDTVIRQ NHVVDVSVAV 500
    STPAGLITPI VFNAHIKGLE TIASDVVSLA SKAREGKLQP HEFQGGTFTI 550
    SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG FDVASVMSVT 600
    LSCDHRVVDG AVGAQWLAEF KKYLEKPVTM LL 632
    Length:632
    Mass (Da):67,166
    Last modified:December 12, 2006 - v3
    Checksum:i3F0EDBD44D93EB68
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti150 – 1523VGS → IGC in BAA01504. (PubMed:1581353)Curated
    Sequence conflicti163 – 1642DI → GP in BAA20956. (PubMed:3571977)Curated
    Sequence conflicti163 – 1642DI → GP in AAA41813. (PubMed:3571977)Curated
    Sequence conflicti601 – 63232LSCDH…VTMLL → HSAVIIELWMEQLEPSGLL in BAA20956. (PubMed:3571977)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC107440 mRNA. Translation: AAI07441.1.
    D10655 mRNA. Translation: BAA01504.1.
    D00092 mRNA. Translation: BAA20956.1.
    M16075 mRNA. Translation: AAA41813.1.
    PIRiS21766.
    RefSeqiNP_112287.1. NM_031025.1.
    UniGeneiRn.15413.

    Genome annotation databases

    EnsembliENSRNOT00000032152; ENSRNOP00000032890; ENSRNOG00000009994.
    GeneIDi81654.
    KEGGirno:81654.
    UCSCiRGD:619859. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC107440 mRNA. Translation: AAI07441.1 .
    D10655 mRNA. Translation: BAA01504.1 .
    D00092 mRNA. Translation: BAA20956.1 .
    M16075 mRNA. Translation: AAA41813.1 .
    PIRi S21766.
    RefSeqi NP_112287.1. NM_031025.1.
    UniGenei Rn.15413.

    3D structure databases

    ProteinModelPortali P08461.
    SMRi P08461. Positions 83-173, 204-305, 394-632.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08461. 1 interaction.
    STRINGi 10116.ENSRNOP00000032890.

    PTM databases

    PhosphoSitei P08461.

    2D gel databases

    World-2DPAGE 0004:P08461.

    Proteomic databases

    PaxDbi P08461.
    PRIDEi P08461.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000032152 ; ENSRNOP00000032890 ; ENSRNOG00000009994 .
    GeneIDi 81654.
    KEGGi rno:81654.
    UCSCi RGD:619859. rat.

    Organism-specific databases

    CTDi 1737.
    RGDi 619859. Dlat.

    Phylogenomic databases

    eggNOGi COG0508.
    GeneTreei ENSGT00740000115255.
    HOGENOMi HOG000281566.
    HOVERGENi HBG005063.
    InParanoidi P08461.
    KOi K00627.
    OMAi PISNIRK.
    OrthoDBi EOG7K3TKW.
    PhylomeDBi P08461.
    TreeFami TF106145.

    Enzyme and pathway databases

    Reactomei REACT_203088. Pyruvate metabolism.

    Miscellaneous databases

    NextBioi 615200.
    PROi P08461.

    Gene expression databases

    Genevestigatori P08461.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR006257. LAT1.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 2 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 2 hits.
    TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 2 hits.
    PS00189. LIPOYL. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-632, PROTEIN SEQUENCE OF 78-91, LIPOYLATION AT LYS-123 AND LYS-249.
      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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiODP2_RAT
    AccessioniPrimary (citable) accession number: P08461
    Secondary accession number(s): Q3B7V7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3