| LGALS13 | |||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||
| Aliases | LGALS13 , GAL13, PLAC8, PP13, galectin 13 | ||||||||||||||||||||||||
| External IDs | OMIM: 608717 HomoloGene: 49329 GeneCards: LGALS13 | ||||||||||||||||||||||||
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| Orthologs | |||||||||||||||||||||||||
| Species | Human | Mouse | |||||||||||||||||||||||
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| Location (UCSC) | Chr 19: 39.6 – 39.61 Mb | n/a | |||||||||||||||||||||||
| PubMed search | [2] | n/a | |||||||||||||||||||||||
| Wikidata | |||||||||||||||||||||||||
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Placental protein 13 (PP13) is a protein that in humans is encoded by the LGALS13 gene. [3] [4]
It is composed of two identical subunits which are held together by disulfide bonds. The monomer of this protein has structural similarity to several members of the beta-galactoside-binding S-type lectin family, but it could not bind beta-galactoside. This is because the ligand binding site is lack of key residue for binding beta-galactoside. [5] It is a galectin-like protein. The ligand of this protein is still unknown.
PP13 levels that are low in the first trimester of pregnancy confers a higher risk for developing pre-eclampsia later in pregnancy. [6]
Eosinophil major basic protein, often shortened to major basic protein is encoded in humans by the PRG2 gene.
Endoglin (ENG) is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex. It is also commonly referred to as CD105, END, FLJ41744, HHT1, ORW and ORW1. It has a crucial role in angiogenesis, therefore, making it an important protein for tumor growth, survival and metastasis of cancer cells to other locations in the body.
Galectins are a class of proteins that bind specifically to β-galactoside sugars, such as N-acetyllactosamine, which can be bound to proteins by either N-linked or O-linked glycosylation. They are also termed S-type lectins due to their dependency on disulphide bonds for stability and carbohydrate binding. There have been 15 galectins discovered in mammals, encoded by the LGALS genes, which are numbered in a consecutive manner. Only galectin-1, -2, -3, -4, -7, -8, -9, -10 and -12 have been identified in humans. Galectin-5 and -6 are found in rodents, whereas galectin-11, -14 and -15 are uniquely found in sheep and goats. Members of the galectin family have also been discovered in other mammals, birds, amphibians, fish, nematodes, sponges, and some fungi. Unlike the majority of lectins they are not membrane bound, but soluble proteins with both intra- and extracellular functions. They have distinct but overlapping distributions but found primarily in the cytosol, nucleus, extracellular matrix or in circulation. Although many galectins must be secreted, they do not have a typical signal peptide required for classical secretion. The mechanism and reason for this non-classical secretion pathway is unknown.
Protein disulfide-isomerase A3 (PDIA3), also known as glucose-regulated protein, 58-kD (GRP58), is an isomerase enzyme. This protein localizes to the endoplasmic reticulum (ER) and interacts with lectin chaperones calreticulin and calnexin (CNX) to modulate folding of newly synthesized glycoproteins. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.
The interleukin 4 receptor is a type I cytokine receptor. IL4R is its human gene.
Galectin-1 is a protein that in humans is encoded by the LGALS1 gene.
Insulin-like growth factor-binding protein 1 (IBP-1) also known as placental protein 12 (PP12) is a protein that in humans is encoded by the IGFBP1 gene.
Human placental protein-14 (PP-14), also known as glycodelin, progestogen-associated endometrial protein (PAEP) or pregnancy-associated endometrial alpha-2 globulin is a glycoprotein that inhibits cell immune function and plays an essential role in the pregnancy process. In humans is encoded by the PAEP gene.
Galectin-3-binding protein is a protein that in humans is encoded by the LGALS3BP gene.
Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.
Eosinophil lysophospholipase is an enzyme that in humans is encoded by the CLC gene.
Galectin-8 is a protein of the galectin family that in humans is encoded by the LGALS8 gene.
Galectin-9 was first time isolated from mouse embryonic kidney in 1997 as a 36 kDa beta-galactoside lectin protein. Human galectin-9 is encoded by the LGALS9 gene.
Tachykinin-3 is a protein that in humans is encoded by the TAC3 gene.
Galectin-2 is a protein that in humans is encoded by the LGALS2 gene.
Galectin-7 is a protein that in humans is encoded by the LGALS7 gene.
Galectin-4 is a protein that in humans is encoded by the LGALS4 gene.
Galectin-3 is a protein that in humans is encoded by the LGALS3 gene. Galectin-3 is a member of the lectin family, of which 14 mammalian galectins have been identified.
In molecular biology, the galactose binding lectin domain is a protein domain. It is found in many proteins including the lectin purified from sea urchin eggs, SUEL. This lectin exists as a disulfide-linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity. The sea urchin egg lectin (SUEL) forms a new class of lectins. Although SUEL was first isolated as a D-galactoside binding lectin, it was later shown that it binds to L-rhamnose preferentially. L-rhamnose and D-galactose share the same hydroxyl group orientation at C2 and C4 of the pyranose ring structure.
Intelectins are lectins expressed in humans and other chordates. Humans express two types of intelectins encoded by ITLN1 and ITLN2 genes respectively. Several intelectins bind microbe-specific carbohydrate residues. Therefore, intelectins have been proposed to function as immune lectins. Even though intelectins contain fibrinogen-like domain found in the ficolins family of immune lectins, there is significant structural divergence. Thus, intelectins may not function through the same lectin-complement pathway. Most intelectins are still poorly characterized and they may have diverse biological roles. Human intelectin-1 (hIntL-1) has also been shown to bind lactoferrin, but the functional consequence has yet to be elucidated. Additionally, hIntL-1 is a major component of asthmatic mucus and may be involved in insulin physiology as well.
