Intercellular adhesion molecule 4 (ICAM4)
The protein contains 271 amino acids for an estimated molecular weight of 29265 Da.
ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM4 is also a ligand for alpha-4/beta-1 and alpha-V integrins. (updated: March 4, 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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| Variant | Description |
|---|---|
| LW(B) | |
| dbSNP:rs36023325 |
Biological Process
Cell adhesion
Cell-cell adhesion
Extracellular matrix organization
Regulation of immune response
Single organismal cell-cell adhesion
The reference OMIM entry for this protein is 111250
Blood group system, landsteiner-wiener; lw
Landsteiner-wiener blood group system
A number sign (#) is used with this entry because LW blood group antigens reside on a protein encoded by the ICAM4 gene (614088) on chromosome 19p13.3.
DESCRIPTION
The LW blood group antigens reside on a 42-kD red cell intercellular adhesion molecule designated ICAM4 (Bailly et al., 1994; Bailly et al., 1995).MAPPING
Sistonen (1984) showed that the LW locus is closely linked to C3 (120700) and Lutheran (111200) on chromosome 19. The maximum lod score was 3.61 at theta = 0.00 for LW:C3 and 3.67 at theta = 0.05 for LW:Lu. The data suggested that the Lewis blood group locus is situated outside the C3-LW region. Using a C3 DNA probe, Lewis et al. (1987) found no recombinants between LW and C3 (maximum lod score = 4.216 at theta = 0.00). No recombinants were found in 16 female meioses. Combined with the data of Sistonen (1984), the recombination fraction between LW and C3 was estimated to be 0.09 in females (maximum lod score = 3.773). Lewis et al. (1988) established close linkage between LW and LDLR (606945); maximum lod = 8.43 at theta = 0.00. They concluded that LDLR, C3, and LW constitute a tightly linked gene cluster. Their findings supported a 19p13.2-cen position for LW. The LW locus was assigned to 19p13.3 by isotopic in situ hybridization (Hermand et al., 1995).MOLECULAR GENETICS
- LW(a)/LW(b) Polymorphism Hermand et al. (1995) demonstrated that the molecular basis for the LW(a)/LW(b) polymorphism is a single-basepair change (308A-G) in the ICAM4 gene that correlates with a PvuII restriction site and results in a gln70-to-arg (Q70R) amino acid substitution (614088.0001). COS-7 cells transfected with LW(a) or LW(b) cDNAs reacted with human anti-LW(a) and anti-LW(b) sera, respectively, as well as with a murine monoclonal anti-LW(ab) antibody, as shown by flow cytometry analysis. Study by Southern blot analysis indicated that the LW locus is composed of a single gene that is not grossly rearranged in the rare LW(a-b-) individuals or in Rh-null individuals deficient for LW antigens. RFLP analysis using PvuII indicated that these variants were homozygous for a phenotypically silent LW(a) allele in all cases. - LW(a-b-) Phenotype Individuals with the rare LW(a-b-) phenotype lack LW antigens and LW protein expression on red blood cells. Some of these individuals express normal Rh antigens, but others also lack Rh and Rh-associated antigens and proteins. Using Southern blot analysis, Hermand et al. (1995) showed that the ICAM4 gene was not grossly rearranged in an individual with the LW(a-b-) phenotype or in individuals with the Rh-null phenotype, who also lack LW antigens. RFLP analysis using PvuII indicated that the LW(a-b-) individual and 3 Rh-null individuals were homozygous for a phenotypically silent LW(a) allele. In an individual with the LW(a-b-) phenotype who carried a normal Rh phenotype, Hermand et al. (1996) identified a 10-bp deletion in exon 1 of the ICAM4 gene (614088.0002) that generated a premature stop codon, resulting in a truncated protein without the transmembrane and cytoplasmic domains. Heterogeneity was indicated by the fact that no detectable abnormality of the LW gene or transcript could be detected in another LW(a-b-) individual.HISTORY
LW stands for Landsteiner and Wiener, the researchers who first discovered the LW blood group with antibody raised in guinea pigs injected with the cells of rhesus monkeys. It was originally thought to be identical to the anti-D first ... 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 111250 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed