Galectin-7 (LGALS7B)
The protein contains 136 amino acids for an estimated molecular weight of 15075 Da.
Could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release. (updated: Jan. 7, 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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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Biological Process
Apoptotic process
Heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules
Negative regulation of CD4-positive, alpha-beta T cell proliferation
Negative regulation of gene expression
Negative regulation of interferon-gamma production
Positive regulation of gene expression
Positive regulation of interleukin-10 production
Positive regulation of interleukin-6 production
The reference OMIM entry for this protein is 600615
Lectin, galactoside-binding, soluble, 7; lgals7
Galectin 7; gal7
DESCRIPTION
Galectins belong to a family of related beta-galactoside-binding lectins, also referred to as S-type or S-Lac lectins. Members of this family have been implicated in a variety of functions, including growth regulation, cell adhesion, migration, neoplastic transformation, and immune responses. In addition to galectin-7, the family includes galectin-1 (LGALS1; 150570), also known as galaptin, a homodimer with subunit molecular mass of 14,500, which is abundant in smooth and skeletal muscle, although it is also found in many other cell types; galectin-2 (LGALS2; 150571), a homodimer with a subunit molecular mass of 14,650 originally described in a hepatoma; galectin-3 (LGALS3; 153619), also known as MAC2, that is abundant in activated macrophages and epithelial cells; and galectin-4 (LGALS4; 602518), a monomer with a molecular mass of 36,300 containing 2 carboxyhydrate-binding domains within a single polypeptide chain.CLONING
In the course of a systematic search for keratinocyte proteins whose levels are differentially regulated in transformed cells and which may play a role in the maintenance of the normal phenotype, Madsen et al. (1995) cloned a novel member of the galectin family, designated galectin-7. This is an abundant keratinocyte protein whose expression is abrogated in SV40 transformed keratinocytes. It is a monomeric beta-galactoside-binding protein with a very narrow tissue distribution. The galectin-7 corresponds to IEF (isoelectric focusing) 17 as determined by 2-dimensional gel electrophoresis analysis of proteins expressed by transiently transfected COS-1 cells. The protein was found mainly in stratified squamous epithelium. The antigen localized to basal keratinocytes, although it was also found, albeit at lower levels, in the suprabasal layers where it concentrated to areas of cell-to-cell contact. The cellular localization and its striking down-regulation in cultured keratinocytes imply a role in cell-cell and/or cell-matrix interactions necessary for normal growth control.GENE FUNCTION
Cao et al. (2003) reported the role of the carbohydrate-binding protein, galectin-7, in reepithelialization of corneal wounds. They found that expression of galectin-7 was markedly upregulated in corneal epithelium after injury and that exogenous galectin-7 stimulated reepithelialization of corneal wounds. The stimulatory effect of galectin-7 on corneal epithelial wound closure was specifically inhibited by beta-lactose, a competing sugar, but unaffected by sucrose, an irrelevant disaccharide.MAPPING
By Southern blotting of human/rodent cell hybrids, Madsen et al. (1995) mapped the galectin-7 gene to chromosome 19.ANIMAL MODEL
Using models of corneal wound healing, Cao et al. (2002) found that reepithelialization of wounds was significantly slower in Gal3-null mice compared with wildtype mice, and the difference was not due to a reduced epithelial cell proliferation rate. Gene expression analysis using cDNA microarrays revealed that healing corneas of Gal3-null mice had reduced levels of Gal7. Exogenous application of Gal7, but not Gal3, accelerated reepithelialization of wounds in Gal3-null mice. Both Gal3 and Gal7 accelerated corneal wound healing in wildtype mice. Cao et al. (2002) concluded that both GAL3 and GAL7 play a role in reepithelialization of corneal wounds. ... 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 25, 2017: Additional information
No protein expression data in P. Mayeux work for LGALS7B
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600615 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed