Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial precursor

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P08461 (ODP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

Dlat

Organism

Rattus norvegicus (Rat) [Reference proteome]

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, and thereby links the glycolytic pathway to the tricarboxylic cycle.
Catalytic activity	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently.
Subunit structure	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.
Subcellular location	Mitochondrion matrix.
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	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Lipoyl Repeat Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay PubMed 7487891. Source: RGD glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW sleep Inferred from expression pattern PubMed 16923172. Source: RGD tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 7487891 PubMed 8431428. Source: RGD pyruvate dehydrogenase complex Inferred from direct assay PubMed 7487891. Source: RGD
Molecular_function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from direct assay PubMed 7487891. Source: RGD nucleotide binding Traceable author statement Ref.2. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 77

Mitochondrion Ref.2

Chain

78 – 632

555

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

PRO_0000162298

Regions

Domain

83 – 157

Lipoyl-binding 1

Domain

209 – 283

Lipoyl-binding 2

Region

344 – 375

E3- and/or E1-component binding domain Potential

Region

456 – 632

177

Catalytic By similarity

Region

600 – 611

CoA-binding By similarity

Sites

Active site

605

Potential

Active site

609

Potential

Amino acid modifications

Modified residue

249

N6-lipoyllysine

Modified residue

451

N6-acetyllysine By similarity

Experimental info

Sequence conflict

150 – 152

VGS → IGC in BAA01504. Ref.2

Sequence conflict

163 – 164

DI → GP in BAA20956. Ref.3

Sequence conflict

163 – 164

DI → GP in AAA41813. Ref.3

Sequence conflict

601 – 632

LSCDH…VTMLL → HSAVIIELWMEQLEPSGLL in BAA20956. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P08461 [UniParc].

Last modified December 12, 2006. Version 3.
Checksum: 3F0EDBD44D93EB68
Show »

FASTA

632

67,166

        10         20         30         40         50         60 
MWRVCARRVQ SAVPRAGFRA RWATLKGPRT GPAAVRCGSG IPSYGVRSLC GWSYGSATVP 

        70         80         90        100        110        120 
RNRILQQLLG SPSRRSYSLP PHQKVPLPSL SPTMQAGTIA RWEKKEGEKI SEGDLIAEVE 

       130        140        150        160        170        180 
TDKATVGFES LEECYMAKIL VPEGTRDVPV GSIICITVEK PQDIEAFKNY TLDSATAATQ 

       190        200        210        220        230        240 
AAPAPAAAPA AAPAAPSASA PGSSYPVHMQ IVLPALSPTM TMGTVQRWEK KVGEKLSEGD 

       250        260        270        280        290        300 
LLAEIETDKA TIGFEVQEEG YLAKILVPEG TRDVPLGTPL CIIVEKQEDI AAFADYRPTE 

       310        320        330        340        350        360 
VTSLKPQAPP PVPPPVAAVP PIPQPLAPTP SAAPAGPKGR VFVSPLAKKL AAEKGIDLTQ 

       370        380        390        400        410        420 
VKGTGPEGRI IKKDIDSFVP TKAAPAAAAA APPGPRVAPT PAGVFIDIPI SNIRRVIAQR 

       430        440        450        460        470        480 
LMQSKQTIPH YYLSVDVNMG EVLLVRKELN KMLEGKGKIS VNDFIIKASA LACLKVPEAN 

       490        500        510        520        530        540 
SSWMDTVIRQ NHVVDVSVAV STPAGLITPI VFNAHIKGLE TIASDVVSLA SKAREGKLQP 

       550        560        570        580        590        600 
HEFQGGTFTI SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG FDVASVMSVT 

       610        620        630 
LSCDHRVVDG AVGAQWLAEF KKYLEKPVTM LL

« Hide

References

	« Hide 'large scale' referencesShow '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] [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. 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, 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_031025.1.
UniGene	Rn.15413.
3D structure databases
ProteinModelPortal	P08461.
SMR	P08461. Positions 83-173, 204-305, 394-632.
ModBase	Search...
Protein-protein interaction databases
IntAct	P08461. 1 interaction.
STRING	10116.ENSRNOP00000032890.
PTM databases
PhosphoSite	P08461.
2D gel databases
World-2DPAGE	0004:P08461.
Proteomic databases
PaxDb	P08461.
PRIDE	P08461.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000032152; ENSRNOP00000032890; ENSRNOG00000009994.
GeneID	81654.
KEGG	rno:81654.
UCSC	RGD:619859. rat.
Organism-specific databases
CTD	1737.
RGD	619859. Dlat.
Phylogenomic databases
eggNOG	COG0508.
GeneTree	ENSGT00560000077144.
HOGENOM	HOG000281566.
HOVERGEN	HBG005063.
InParanoid	P08461.
KO	K00627.
OMA	GTICISN.
OrthoDB	EOG412M54.
Gene expression databases
Genevestigator	P08461.
GermOnline	ENSRNOG00000009994. Rattus norvegicus.
Family and domain databases
Gene3D	3.30.559.10. 1 hit. 4.10.320.10. 1 hit.
InterPro	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]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 2 hits. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF47005. E3_bd. 1 hit. SSF51230. Hybrid_motif. 2 hits.
TIGRFAMs	TIGR01349. PDHac_trf_mito. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 2 hits. PS00189. LIPOYL. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	615200.

Entry information

Entry name

ODP2_RAT

Accession

Primary (citable) accession number: P08461
Secondary accession number(s): Q3B7V7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	December 12, 2006
Last modified:	April 3, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents