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P04642 (LDHA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-lactate dehydrogenase A chain

Short name=LDH-A
EC=1.1.1.27
Alternative name(s):
LDH muscle subunit
Short name=LDH-M
Gene names
Name:Ldha
Synonyms:Ldh-1, Ldh1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-lactate + NAD+ = pyruvate + NADH. HAMAP-Rule MF_00488

Pathway

Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. HAMAP-Rule MF_00488

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00488.

Post-translational modification

ISGylated By similarity. HAMAP-Rule MF_00488

Sequence similarities

Belongs to the LDH/MDH superfamily. LDH family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNAD metabolic process

Inferred from direct assay PubMed 17447164. Source: RGD

cellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

lactate metabolic process

Inferred from direct assay PubMed 17447164. Source: RGD

positive regulation of apoptotic process

Inferred from direct assay PubMed 9465046. Source: RGD

post-embryonic organ development

Inferred from expression pattern PubMed 6849973. Source: RGD

response to cAMP

Inferred from expression pattern PubMed 6300127. Source: RGD

response to drug

Inferred from expression pattern PubMed 11176097. Source: RGD

response to estrogen

Inferred from expression pattern PubMed 17010207. Source: RGD

response to glucose

Inferred from expression pattern PubMed 11457846. Source: RGD

response to hydrogen peroxide

Inferred from expression pattern PubMed 16154111. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 12678657. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 15110778. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 7758843. Source: RGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-lactate dehydrogenase activity

Inferred from direct assay PubMed 17447164. Source: RGD

NAD binding

Inferred from direct assay PubMed 17447164. Source: RGD

identical protein binding

Inferred from direct assay PubMed 7138505. Source: RGD

kinase binding

Inferred from physical interaction PubMed 17572440. Source: RGD

lactate dehydrogenase activity

Inferred from direct assay PubMed 7138505. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 332331L-lactate dehydrogenase A chain HAMAP-Rule MF_00488
PRO_0000168419

Regions

Nucleotide binding29 – 5729NAD By similarity

Sites

Active site1931Proton acceptor By similarity
Binding site991NAD By similarity
Binding site1061Substrate By similarity
Binding site1381NAD or substrate By similarity
Binding site1691Substrate By similarity
Binding site2481Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue51N6-acetyllysine; alternate By similarity
Modified residue51N6-succinyllysine; alternate By similarity
Modified residue141N6-acetyllysine By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue811N6-acetyllysine By similarity
Modified residue1181N6-acetyllysine; alternate By similarity
Modified residue1181N6-succinyllysine; alternate By similarity
Modified residue1261N6-acetyllysine By similarity
Modified residue2241N6-acetyllysine By similarity
Modified residue2321N6-acetyllysine By similarity
Modified residue2391Phosphotyrosine By similarity
Modified residue2431N6-acetyllysine By similarity
Modified residue3181N6-acetyllysine; alternate By similarity
Modified residue3181N6-succinyllysine; alternate By similarity

Experimental info

Sequence conflict184 – 1918SCHGWVLG → ADLGEVV AA sequence Ref.4
Sequence conflict3241W → G in AAA41508. Ref.5
Sequence conflict3261I → T in AAA41508. Ref.5

Secondary structure

........................................................ 332
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04642 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 5E432659D032A4D3

FASTA33236,451
        10         20         30         40         50         60 
MAALKDQLIV NLLKEEQVPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG 

        70         80         90        100        110        120 
EMMDLQHGSL FLKTPKIVSS KDYSVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI 

       130        140        150        160        170        180 
IPNVVKYSPQ CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV 

       190        200        210        220        230        240 
HPLSCHGWVL GEHGDSSVPV WSGVNVAGVS LKSLNPQLGT DADKEQWKDV HKQVVDSAYE 

       250        260        270        280        290        300 
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI 

       310        320        330 
SDVVKVTLTP DEEARLKKSA DTLWGIQKEL QF 

« Hide

References

« Hide 'large scale' references
[1]"Epidermal growth factor or serum stimulation of rat fibroblasts induces an elevation in mRNA levels for lactate dehydrogenase and other glycolytic enzymes."
Matrisian L.M., Rautmann G., Magun B.E., Breathnach R.
Nucleic Acids Res. 13:711-726(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: Lung.
[3]Bienvenut W.V., von Kriegsheim A.F., Kolch W.
Submitted (JUN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14; 43-57; 91-99; 107-112; 119-126; 233-243; 306-315 AND 319-328, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fibroblast and Pheochromocytoma.
[4]"Identification of a nucleic acid helix-destabilizing protein from rat liver as lactate dehydrogenase-5."
Williams K.R., Reddigari S., Patel G.L.
Proc. Natl. Acad. Sci. U.S.A. 82:5260-5264(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 82-99; 127-132; 156-157; 170-190; 234-245; 306-315 AND 319-328.
[5]"Characterization of the folding structure of 3'-end of lactate dehydrogenase A-mRNA isolated from hormone stimulated rat C-6 glioma cell culture."
Bae S.C., Lee S.K.
J. Microbiol. 25:94-102(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 274-332.
Tissue: Liver.
[6]Lubec G., Chen W.-Q.
Submitted (SEP-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 319-328, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01964 mRNA. Translation: CAA26000.1.
BC084698 mRNA. Translation: AAH84698.1.
M54926 mRNA. Translation: AAA41508.1.
PIRA23083.
RefSeqNP_058721.1. NM_017025.1.
UniGeneRn.107896.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AJ1X-ray1.87A/B/C/D2-332[»]
4AJ2X-ray1.75A/B/C/D2-332[»]
4AJ4X-ray1.90A/B/C/D1-332[»]
4AJEX-ray2.35A/B/C/D2-332[»]
4AJHX-ray1.93A/B/C/D2-332[»]
4AJIX-ray1.93A/B/C/D2-332[»]
4AJJX-ray1.75A/B/C/D2-332[»]
4AJKX-ray2.03A/B/C/D2-332[»]
4AJLX-ray1.77A/B/C/D2-332[»]
4AJNX-ray2.10A/B/C/D2-332[»]
4AJOX-ray1.96A/B/C/D2-332[»]
4AL4X-ray1.78A/B/C/D2-332[»]
ProteinModelPortalP04642.
SMRP04642. Positions 2-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246686. 3 interactions.
IntActP04642. 5 interactions.
MINTMINT-4568905.

Chemistry

BindingDBP04642.
ChEMBLCHEMBL2176824.

PTM databases

PhosphoSiteP04642.

Proteomic databases

PaxDbP04642.
PRIDEP04642.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000017468; ENSRNOP00000017468; ENSRNOG00000013009.
GeneID24533.
KEGGrno:24533.

Organism-specific databases

CTD3939.
RGD2996. Ldha.

Phylogenomic databases

eggNOGCOG0039.
GeneTreeENSGT00550000074541.
HOGENOMHOG000213793.
HOVERGENHBG000462.
InParanoidP04642.
KOK00016.
OMAYTQTSIL.
OrthoDBEOG7X0VH3.
PhylomeDBP04642.
TreeFamTF314963.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11604.
UniPathwayUPA00554; UER00611.

Gene expression databases

GenevestigatorP04642.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_00488. Lactate_dehydrog.
InterProIPR001557. L-lactate/malate_DH.
IPR011304. L-lactate_DH.
IPR018177. L-lactate_DH_AS.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSPR00086. LLDHDRGNASE.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01771. L-LDH-NAD. 1 hit.
PROSITEPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603598.

Entry information

Entry nameLDHA_RAT
AccessionPrimary (citable) accession number: P04642
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways