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P08461

- ODP2_RAT

UniProt

P08461 - ODP2_RAT

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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

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
Complete GO annotation...

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. mitochondrion Source: RGD
  2. pyruvate dehydrogenase complex Source: RGD
Complete GO annotation...

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.
GeneTreeiENSGT00760000119281.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWRVCARRVQ SAVPRAGFRA RWATLKGPRT GPAAVRCGSG IPSYGVRSLC
60 70 80 90 100
GWSYGSATVP RNRILQQLLG SPSRRSYSLP PHQKVPLPSL SPTMQAGTIA
110 120 130 140 150
RWEKKEGEKI SEGDLIAEVE TDKATVGFES LEECYMAKIL VPEGTRDVPV
160 170 180 190 200
GSIICITVEK PQDIEAFKNY TLDSATAATQ AAPAPAAAPA AAPAAPSASA
210 220 230 240 250
PGSSYPVHMQ IVLPALSPTM TMGTVQRWEK KVGEKLSEGD LLAEIETDKA
260 270 280 290 300
TIGFEVQEEG YLAKILVPEG TRDVPLGTPL CIIVEKQEDI AAFADYRPTE
310 320 330 340 350
VTSLKPQAPP PVPPPVAAVP PIPQPLAPTP SAAPAGPKGR VFVSPLAKKL
360 370 380 390 400
AAEKGIDLTQ VKGTGPEGRI IKKDIDSFVP TKAAPAAAAA APPGPRVAPT
410 420 430 440 450
PAGVFIDIPI SNIRRVIAQR LMQSKQTIPH YYLSVDVNMG EVLLVRKELN
460 470 480 490 500
KMLEGKGKIS VNDFIIKASA LACLKVPEAN SSWMDTVIRQ NHVVDVSVAV
510 520 530 540 550
STPAGLITPI VFNAHIKGLE TIASDVVSLA SKAREGKLQP HEFQGGTFTI
560 570 580 590 600
SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG FDVASVMSVT
610 620 630
LSCDHRVVDG AVGAQWLAEF KKYLEKPVTM LL
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 ENSGT00760000119281.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 138 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