L-lactate dehydrogenase A chain (LDHA)
The protein contains 332 amino acids for an estimated molecular weight of 36689 Da.
No function (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs5030621 | |
| dbSNP:rs748436361 | |
| dbSNP:rs200093825 |
Biological Process
Cellular carbohydrate metabolic process
Cellular metabolic process
Cellular response to extracellular stimulus
Glycolytic process
Lactate metabolic process
NAD metabolic process
Positive regulation of apoptotic process
Post-embryonic animal organ development
Pyruvate metabolic process
Response to cAMP
Response to drug
Response to estrogen
Response to glucose
Response to hydrogen peroxide
Response to hypoxia
Response to nutrient
Small molecule metabolic process
Substantia nigra development
Cellular Component
Cytosol
Extracellular exosome
Membrane
Mitochondrion
Nucleus
Sperm fibrous sheath
The reference OMIM entry for this protein is 150000
Lactate dehydrogenase a; ldha
Ldh, subunit m
DESCRIPTION
The LDHA gene encodes the A subunit of lactate dehydrogenase (EC 1.1.1.27), an enzyme that catalyzes the interconversion of lactate and pyruvate. The A subunit is expressed in skeletal muscle. Other isoforms include LDHB (150100), expressed in cardiac muscle, and LDHC (150150), expressed in testes (Tsujibo et al., 1985; Chung et al., 1985).CLONING
Tsujibo et al. (1985) isolated cDNA clones corresponding to the human LDHA gene from a human fibroblast cDNA library. The predicted 332-amino acid sequence had a molecular mass of 36.7 kD and showed 92% homology to the porcine Ldha polypeptide. A nonfunctional pseudogene was also isolated.GENE STRUCTURE
Chung et al. (1985) determined that the LDHA gene contains 7 exons and spans about 12 kb.MAPPING
Studies using human-mouse somatic cell hybrids indicated that the LDHA and LDHB loci are not linked (Nabholz et al., 1969). By study of cell hybrids, LDHA was assigned to the short arm of chromosome 11 by Francke and Busby (1975). By the study of cells from 4 persons with different interstitial deletions of 11p, Francke et al. (1977) assigned the LDHA locus to 11p1203-11p1208. At HGM8, controversy arose over the mapping of LDHA (see Grzeschik and Kazazian, 1985). HGM8 reported the location as 11p14-p12. Lebo et al. (1985) and Lewis et al. (1985) placed the locus at a more distal position. Yang-Feng et al. (1986) did in situ hybridization studies in cell lines from 2 persons with apparently balanced translocations involving 11p13. Their findings excluded LDHA from any region proximal to 11p13 and localized the gene to 11p15-p14. Scrable et al. (1990) demonstrated that LDHA is located in band 11p15.4.GENE FUNCTION
Centrosomal proteins (e.g., 117139, 117140, 117141, 117143) have been studied mainly with anticentrosome serum. Using a spontaneously arising rabbit anticentrosome serum with strong human specificity, Gosti et al. (1987) identified specific antigens in isolated centrosomes which reacted with several noncentrosomal proteins, notably, lactate dehydrogenase. Anderson and Kovacik (1981) identified an unusual isozyme of lactate dehydrogenase, which they designated lactate dehydrogenase K (LDHK), in cells transformed by the Kirsten murine sarcoma virus. They examined 16 different human carcinomas and found that 11 had LDHK activity 10- to 500-fold over the level in adjoining nontumor tissue. Li et al. (1988) determined that this cancer-associated lactate dehydrogenase is a tyrosylphosphorylated form of LDHA. The protein was found to be complexed with 21-kD, 30-kD, and 56-kD proteins.MOLECULAR GENETICS
Nance et al. (1963) observed a genetically determined variant LDH in the red cells of 4 members of 2 generations of a Brazilian family. The mutation involved the A subunit. This was the first instance in which practical considerations permitted demonstration of the variant in multiple relatives. Unlike the findings of Shaw and Barto (1963) in Peromyscus and of Boyer et al. (1963) in man, the findings in the Brazilian family did not suggest random association between the products of the mutant and wildtype alleles. LDH variants, involving either the A or the B subunit, seem to be unusually frequent in India (Das et al., 1970). - Glycogen Storage Disease XI In a patient with LDHA deficiency, or glycogen storage disease XI (GSD11; 612933), reported by Maekawa et al. (1986), Maekawa et al. (1990) found homozygosity for a 2 ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 150000 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed