Glycophorin-A (GYPA)
The protein contains 150 amino acids for an estimated molecular weight of 16331 Da.
Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). (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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- 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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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Biological Process
Leukocyte migration
Obsolete cytoskeletal anchoring at plasma membrane
Regulation of response to osmotic stress
The reference OMIM entry for this protein is 111300
Blood group--mn locus; mn glycophorin a, included; gpa, included
Gypa, included
On the basis of studies in the family of a child with a translocation chromosome, German et al. (1968) suggested that the MN locus is either in the middle of chromosome 2 or near the distal end of the long arm of chromosome 4. Using 'banding techniques,' German and Chaganti (1973) restudied the translocation they reported in 1968 and concluded that MN can be tentatively assigned to the area of band q14 in the proximal portion of the long arm of chromosome 2. Weitkamp et al. (1972) presented data suggesting that the MN locus and the beta hemoglobin locus (141900) are linked. (This has, of course, been disproved.) Barbosa et al. (1975) excluded a recombination fraction of less than 0.30 for MN and Hb beta. The results supported a lower recombination fraction for males. Linkage with the Alzheimer locus (104300) and with colonic polyposis (175100) has been suspected. Recombination data suggested that the MN and acid phosphatase (ACP1; 171500) loci are far apart (Weitkamp et al., 1975). Cook et al. (1978) excluded MNSs from chromosome 9 by exclusion mapping that incorporated data both from families with chromosome markers and from linkage studies with firmly assigned markers. MNSs was subsequently assigned to chromosome 4. In a further study of the propositus of the 2q;4q translocation family, German et al. (1979) showed by banding that the breaks had occurred at 2q14 and 4q29 and that a minute segment had been lost at the site of break. Whether the loss was from chromosome 2 or 4 was not certain because both have several short bands at these sites and only one band was missing in the proband. The proband lacked blood type 's' (GPB; 111740) which he should have received from his 'ss' father, had signs of a modified red cell membrane, and had developmental abnormalities. Since the abnormalities of phenotype appeared at the same time as the chromosomal abnormality, German et al. (1979) suggested that deletion was the basis of all the changes. Since Weitkamp (1978) reported observations indicating strongly that MNSs is not near 2q14, German et al. (1979) concluded that it must be in a band near 4q29. Cook et al. (1980) favored 4q28 over 4q31. For males, Bias and Meyers (1979) found a maximal lod score of 3.99 at theta 0.18 for linkage of Stoltzfus (111800) and MNS. Acid phosphatase and Kidd both gave lods of 0.32 with Stoltzfus at a male-theta of 0.20. Linkage of Gc and MNSs at recombination frequencies of less than 25% in males and 30% in females was excluded by Weitkamp (1978). For MN versus Gc, Falk et al. (1979) found a male lod score of 3.75 at a recombination fraction of 0.30. In females the maximal lod score was 0.34 at a recombination fraction of 0.42. From analysis of MNSs blood groups in families with chromosome 4 rearrangements, both deletion analysis and family linkage study, Cook et al. (1981) concluded that the MNSs 'locus' lies in the region 4q28-q31. Blumenfeld and Adamany (1978) found that the MM blood group polypeptide differs from the NN polypeptide in two amino acids, these being serine and glycine in MM and leucine and glutamic acid in NN. The MN individual shows all four amino acids. The two major sialoglycoproteins of the human red cell membrane, alpha and delta (glycophorins A and B), carry the MNSs antigenic specificities. They have identical amino acid sequences for the first 26 residues from the amino terminus. Alpha expresses M or N blood group activity; delta carries only blood group N activity. Furthermore, the asp ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
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
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for GYPA
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 111300 was added.
Sept. 16, 2015: Protein entry updated
Automatic update: model status changed