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Protein

L-lactate dehydrogenase A chain

Gene

Ldha

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-lactate + NAD+ = pyruvate + NADH.

Pathwayi: pyruvate fermentation to lactate

This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate.
Proteins known to be involved in this subpathway in this organism are:
  1. L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhb), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase B chain (Ldhb), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldhal6b), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase A chain (Ldha), L-lactate dehydrogenase (Ldhb), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase C chain (Ldhc), L-lactate dehydrogenase (Ldhc)
This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate, the pathway pyruvate fermentation to lactate and in Fermentation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991NADBy similarity
Binding sitei106 – 1061SubstrateBy similarity
Binding sitei138 – 1381NAD or substrateBy similarity
Binding sitei169 – 1691SubstrateBy similarity
Active sitei193 – 1931Proton acceptorBy similarity
Binding sitei248 – 2481SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 5729NADBy similarityAdd
BLAST

GO - Molecular functioni

  • lactate dehydrogenase activity Source: MGI
  • L-lactate dehydrogenase activity Source: MGI

GO - Biological processi

  • cellular response to extracellular stimulus Source: MGI
  • glucose catabolic process to lactate via pyruvate Source: MGI
  • lactate biosynthetic process from pyruvate Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiR-MMU-70268. Pyruvate metabolism.
UniPathwayiUPA00554; UER00611.

Names & Taxonomyi

Protein namesi
Recommended name:
L-lactate dehydrogenase A chain (EC:1.1.1.27)
Short name:
LDH-A
Alternative name(s):
LDH muscle subunit
Short name:
LDH-M
Gene namesi
Name:Ldha
Synonyms:Ldh-1, Ldh1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:96759. Ldha.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
  • sperm fibrous sheath Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 332331L-lactate dehydrogenase A chainPRO_0000168414Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei5 – 51N6-acetyllysine; alternateCombined sources
Modified residuei5 – 51N6-succinyllysine; alternateCombined sources
Modified residuei14 – 141N6-acetyllysineBy similarity
Modified residuei57 – 571N6-acetyllysineBy similarity
Modified residuei81 – 811N6-acetyllysineCombined sources
Modified residuei118 – 1181N6-acetyllysine; alternateCombined sources
Modified residuei118 – 1181N6-succinyllysine; alternateCombined sources
Modified residuei126 – 1261N6-acetyllysineCombined sources
Modified residuei224 – 2241N6-acetyllysineCombined sources
Modified residuei232 – 2321N6-acetyllysineCombined sources
Modified residuei239 – 2391PhosphotyrosineCombined sources
Modified residuei243 – 2431N6-acetyllysineCombined sources
Modified residuei309 – 3091PhosphothreonineBy similarity
Modified residuei318 – 3181N6-acetyllysine; alternateCombined sources
Modified residuei318 – 3181N6-succinyllysine; alternateCombined sources
Modified residuei322 – 3221PhosphothreonineBy similarity

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP06151.
PaxDbiP06151.
PRIDEiP06151.
TopDownProteomicsiP06151.

2D gel databases

REPRODUCTION-2DPAGEP06151.
SWISS-2DPAGEP06151.
UCD-2DPAGEP06151.

PTM databases

iPTMnetiP06151.
PhosphoSiteiP06151.
SwissPalmiP06151.

Expressioni

Gene expression databases

BgeeiP06151.
CleanExiMM_LDHA.
ExpressionAtlasiP06151. baseline and differential.
GenevisibleiP06151. MM.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
HnrnpdQ606682EBI-444940,EBI-299932

Protein-protein interaction databases

BioGridi201127. 8 interactions.
IntActiP06151. 21 interactions.
MINTiMINT-1612559.
STRINGi10090.ENSMUSP00000103267.

Structurei

3D structure databases

ProteinModelPortaliP06151.
SMRiP06151. Positions 4-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. LDH family.Curated

Phylogenomic databases

eggNOGiKOG1495. Eukaryota.
COG0039. LUCA.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP06151.
PhylomeDBiP06151.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. 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]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06151-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLKDQLIV NLLKEEQAPQ NKITVVGVGA VGMACAISIL MKDLADELAL
60 70 80 90 100
VDVMEDKLKG EMMDLQHGSL FLKTPKIVSS KDYCVTANSK LVIITAGARQ
110 120 130 140 150
QEGESRLNLV QRNVNIFKFI IPNIVKYSPH CKLLIVSNPV DILTYVAWKI
160 170 180 190 200
SGFPKNRVIG SGCNLDSARF RYLMGERLGV HALSCHGWVL GEHGDSSVPV
210 220 230 240 250
WSGVNVAGVS LKSLNPELGT DADKEQWKEV HKQVVDSAYE VIKLKGYTSW
260 270 280 290 300
AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGINEDVFLS VPCILGQNGI
310 320 330
SDVVKVTLTP EEEARLKKSA DTLWGIQKEL QF
Length:332
Mass (Da):36,499
Last modified:January 23, 2007 - v3
Checksum:i5AEB41E1E0B95100
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111N → I (PubMed:3996406).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00309 Genomic DNA. Translation: CAA68410.1.
X02520
, X02521, X02522, X02523, X02524, X02525, X02526 Genomic DNA. Translation: CAA26360.1.
U13687 mRNA. Translation: AAA21466.1.
X03753 Genomic DNA. Translation: CAA27387.1.
M17516 mRNA. Translation: AAA39424.1.
CCDSiCCDS21289.1.
PIRiA25205. DEMSLM.
I48240.
RefSeqiNP_034829.1. NM_010699.2.
UniGeneiMm.29324.

Genome annotation databases

EnsembliENSMUST00000048209; ENSMUSP00000036386; ENSMUSG00000063229.
GeneIDi16828.
UCSCiuc009gzm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00309 Genomic DNA. Translation: CAA68410.1.
X02520
, X02521, X02522, X02523, X02524, X02525, X02526 Genomic DNA. Translation: CAA26360.1.
U13687 mRNA. Translation: AAA21466.1.
X03753 Genomic DNA. Translation: CAA27387.1.
M17516 mRNA. Translation: AAA39424.1.
CCDSiCCDS21289.1.
PIRiA25205. DEMSLM.
I48240.
RefSeqiNP_034829.1. NM_010699.2.
UniGeneiMm.29324.

3D structure databases

ProteinModelPortaliP06151.
SMRiP06151. Positions 4-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201127. 8 interactions.
IntActiP06151. 21 interactions.
MINTiMINT-1612559.
STRINGi10090.ENSMUSP00000103267.

PTM databases

iPTMnetiP06151.
PhosphoSiteiP06151.
SwissPalmiP06151.

2D gel databases

REPRODUCTION-2DPAGEP06151.
SWISS-2DPAGEP06151.
UCD-2DPAGEP06151.

Proteomic databases

EPDiP06151.
PaxDbiP06151.
PRIDEiP06151.
TopDownProteomicsiP06151.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048209; ENSMUSP00000036386; ENSMUSG00000063229.
GeneIDi16828.
UCSCiuc009gzm.2. mouse.

Organism-specific databases

CTDi3939.
MGIiMGI:96759. Ldha.

Phylogenomic databases

eggNOGiKOG1495. Eukaryota.
COG0039. LUCA.
HOGENOMiHOG000213793.
HOVERGENiHBG000462.
InParanoidiP06151.
PhylomeDBiP06151.

Enzyme and pathway databases

UniPathwayiUPA00554; UER00611.
ReactomeiR-MMU-70268. Pyruvate metabolism.

Miscellaneous databases

ChiTaRSiLdha. mouse.
NextBioi290734.
PROiP06151.
SOURCEiSearch...

Gene expression databases

BgeeiP06151.
CleanExiMM_LDHA.
ExpressionAtlasiP06151. baseline and differential.
GenevisibleiP06151. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00488. Lactate_dehydrog.
InterProiIPR001557. 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]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
PROSITEiPS00064. L_LDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of the mouse lactate dehydrogenase-A functional gene: comparison of the exon-intron organization of dehydrogenase genes."
    Fukasawa K.M., Li S.S.-L.
    Genetics 116:99-105(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/10.
    Tissue: Liver.
  2. "Protein structure and gene organization of mouse lactate dehydrogenase-A isozyme."
    Li S.S.-L., Tiano H.F., Fukasawa K.M., Yagi K., Shimizu M., Sharief F.S., Nakashima Y., Pan Y.E.
    Eur. J. Biochem. 149:215-225(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Lactate dehydrogenase-A mRNAs in mouse testis and somatic tissues containing different 5' noncoding sequences."
    Hiraoka Y., Li S.S.-L.
    J. Genet. Mol. Biol. 1:1-6(1990)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DBA/2J.
  4. "Nucleotide sequence of the putative regulatory region of mouse lactate dehydrogenase-A gene."
    Fukasawa K.M., Li S.S.-L.
    Biochem. J. 235:435-439(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
  5. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-14; 23-73; 82-99; 107-126; 133-149; 158-169; 172-177; 213-228; 233-243; 246-265; 269-315 AND 319-328, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J and OF1.
    Tissue: Brain and Hippocampus.
  6. "Isolation and characterization of a cDNA and a pseudogene for mouse lactate dehydrogenase-A isozyme."
    Akai K., Yagi K., Tiano H.F., Pan Y.-C.E., Shimizu M., Fong K., Jungmann R.A., Li S.S.-L.
    Int. J. Biochem. 17:645-648(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 202-332.
  7. Cited for: ISGYLATION.
  8. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-5; LYS-81; LYS-118; LYS-126; LYS-224; LYS-232; LYS-243 AND LYS-318, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-118 AND LYS-318, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiLDHA_MOUSE
AccessioniPrimary (citable) accession number: P06151
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 13, 2016
This is version 166 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.