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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Gene

Dlat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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 N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei605Sequence analysis1
Active sitei609Sequence analysis1

GO - Molecular functioni

  • dihydrolipoyllysine-residue acetyltransferase activity Source: RGD
  • identical protein binding Source: RGD
  • nucleotide binding Source: RGD
  • pyruvate dehydrogenase (NAD+) activity Source: Ensembl

GO - Biological processi

  • acetyl-CoA biosynthetic process from pyruvate Source: RGD
  • glucose metabolic process Source: UniProtKB-KW
  • sleep Source: RGD
  • tricarboxylic acid cycle Source: UniProtKB-KW

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processCarbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiR-RNO-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-RNO-389661 Glyoxylate metabolism and glycine degradation
R-RNO-5362517 Signaling by Retinoic Acid
R-RNO-70268 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi619859 Dlat

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 77Mitochondrion1 PublicationAdd BLAST77
ChainiPRO_000016229878 – 632Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrialAdd BLAST555

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei91PhosphoserineBy similarity1
Modified residuei123N6-lipoyllysinePROSITE-ProRule annotation1 Publication1
Modified residuei249N6-lipoyllysinePROSITE-ProRule annotation1 Publication1
Modified residuei451N6-acetyllysineBy similarity1
Modified residuei458N6-succinyllysineBy similarity1
Modified residuei532N6-succinyllysineBy similarity1

Post-translational modificationi

Delipoylated at Lys-123 and Lys-249 by SIRT4, delipoylation decreases the PHD complex activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP08461
PRIDEiP08461

2D gel databases

World-2DPAGEi0004:P08461

PTM databases

iPTMnetiP08461
PhosphoSitePlusiP08461

Expressioni

Tissue specificityi

Expressed in flagella of epididymal sperm.1 Publication

Gene expression databases

BgeeiENSRNOG00000009994

Interactioni

Subunit structurei

Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDH1A and PDHB, 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. Interacts with SIRT4. Interacts with PDHB.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP08461 1 interactor.
STRINGi10116.ENSRNOP00000032890

Structurei

3D structure databases

ProteinModelPortaliP08461
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 158Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST77
Domaini208 – 284Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST77
Domaini342 – 379Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni456 – 632CatalyticBy similarityAdd BLAST177
Regioni600 – 611CoA-bindingBy similarityAdd BLAST12

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG0557 Eukaryota
COG0508 LUCA
GeneTreeiENSGT00890000139393
HOGENOMiHOG000281566
HOVERGENiHBG005063
InParanoidiP08461
KOiK00627
OMAiTMEFESF
OrthoDBiEOG091G0CAV
PhylomeDBiP08461
TreeFamiTF106145

Family and domain databases

Gene3Di3.30.559.101 hit
4.10.320.101 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR006257 LAT1
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 2 hits
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 2 hits
TIGRFAMsiTIGR01349 PDHac_trf_mito, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 2 hits
PS00189 LIPOYL, 2 hits
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

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

P08461-1 [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)DescriptionActionsGraphical viewLength
Sequence conflicti150 – 152VGS → IGC in BAA01504 (PubMed:1581353).Curated3
Sequence conflicti163 – 164DI → GP in BAA20956 (PubMed:3571977).Curated2
Sequence conflicti163 – 164DI → GP in AAA41813 (PubMed:3571977).Curated2
Sequence conflicti601 – 632LSCDH…VTMLL → HSAVIIELWMEQLEPSGLL in BAA20956 (PubMed:3571977).CuratedAdd BLAST32

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiODP2_RAT
AccessioniPrimary (citable) accession number: P08461
Secondary accession number(s): Q3B7V7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: December 12, 2006
Last modified: March 28, 2018
This is version 168 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome