BPIFA2
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BPIFA2
BPI fold containing family A, member 2 (BPIFA2), also known as Parotid Secretory Protein (PSP), is a protein that in humans is encoded by the ''BPIFA2'' gene. The ''BPIFA2'' gene sequence predicts multiple transcripts ( splice variants); 2 mRNA variants have been well characterized. The resulting BPIFA2 is a secreted protein, expressed at very high levels in the parotid (salivary) gland; at high levels in oropharyneal mucosa, including tongue; and at moderate levels many other tissue types and glands including mammary gland, testis, lung, bladder, blood, prostate, adrenal gland, kidney, and pancreas. Superfamily BPIFA2 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/CETP family. The BPI fold creates apolar binding pockets that can interact with hydr ...
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Lipid-binding Serum Glycoprotein
In molecular biology, the lipid-binding serum glycoproteins family, also known as the BPI/LBP/Plunc family or LBP/BPI/CETP family represents a family which includes mammalian lipid-binding serum glycoproteins and/or proteins containing a structural motif known as the ''BPI fold''. Members of this family include: *Bactericidal permeability-increasing protein (BPI) * Lipopolysaccharide-binding protein (LBP) *Cholesteryl ester transfer protein (CETP) * Phospholipid transfer protein (PLTP) * Palate, lung and nasal epithelium carcinoma-associated protein (PLUNC) Structure These proteins consist of N- and C-terminal domains, which share a similar two-layer alpha/beta structure, but show little sequence identity to each other. These domains were first described as being arranged in a "boomerang" shape that creates the BPI fold. The fold contains apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains of lipopolysacch ...
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BPIFA1
BPI fold containing family A, member 1 (BPIFA1), also known as Palate, lung, and nasal epithelium clone (PLUNC), is a protein that in humans is encoded by the ''BPIFA1'' gene. It was also formerly known as "Secretory protein in upper respiratory tracts" (SPURT). The ''BPIFA1'' gene sequence predicts 4 transcripts ( splice variants); 3 mRNA variants have been well characterized. The resulting BPIFA1 is a secreted protein, expressed at very high levels in mucosa of the airways (olfactory and respiratory and epithelium) and salivary glands; at high levels in oropharyneal epithelium, including tongue and tonsils; and at moderate levels many other tissue types and glands including pituitary, testis, lung, bladder, blood, prostate, pancreas, levels in the digestive tract (tongue, stomach, intestinal epithelium) and pancreas. The protein can be detected on the apical side of epithelial cells and in airway surface liquid, nasal mucus, and sputum. Superfamily BPIFA1 is a member of a B ...
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BPIFB9P
Vomeromodulin is a non-human protein also known as BPI fold containing family B, member 9 (BPIFB9) in the rat encoded by the ''Bpifb9/RYF3'' gene, and as BPI fold containing family B, member 9A (BPIFB9A) encoded by the ''Bpifb9a'' gene in the mouse. This protein has been characterized in mammals such as rodents, carnivores, even-toed ungulates, insectivores, bats, lagomorphs, and shrews but is apparently absent in primates and other vertebrates such as birds, reptiles, and amphibians. Its function is associated with detection of chemical odorant pheromone molecules. In humans no protein is expressed and it is present only as a pseudogene ''BPIFB9P''. The pseudogene was named based on its functional ortholog found in the other species. Superfamily Vomeromodulin/BPIFB9/BPIFB9A is a member of the BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" ...
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BPIFB5P
BPI fold containing family B, member 5 is a non-human protein encoded by the ''Bpifb5'' gene, also known as ''Lplunc5.'' The BPIFB5 protein and ''Bpifb5'' gene have been characterized in mammals such as rodents (mouse, rat) and even-toed ungulates (pig, cow) but are apparently lacking in primates and other vertebrates such as birds, reptiles, and amphibians. The protein in rodents is expressed at moderately high levels in Mucous membrane, mucosa of the airways (respiratory and olfactory epithelium) and at moderate levels in salivary glands, esophagus, and gonads (ovary, testis); in even-toed ungulates expression is high in testis, moderate in brain and striated muscle, and low in kidney. In humans no protein is expressed and it is present only as a pseudogene ''BPIFB5P''. The pseudogene was named based on its functional ortholog found in the other species. Superfamily BPIFB5 is a member of the BPI fold protein superfamily defined by the presence of the bactericidal/permeabil ...
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BPIFB6
BPI fold containing family B, member 6 (BPIFB6), also known as bactericidal/permeability-increasing protein-like 3 (BPIL3), is a protein that in humans is encoded by the ''BPIFB6'' gene, also known as ''BPIL3'' and ''LPLUNC6''. It is expressed at high levels in hypertrophic tonsils, at relatively moderate levels in oronasal epithelium including nasal mucosa, tongue, and salivary gland, as well as esophageal mucosa at lesser levels. Orthologs are present in many vertebrate species including mammals, birds, reptiles, and amphibians. Superfamily BPIFB6 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/ CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains ...
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BPIFB3
BPI fold containing family B, member 3 (BPIFB3) is a protein that in humans is encoded by the ''BPIFB3'' gene. Two variants have been detected in humans. Superfamily BPIFB3 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/ CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains of lipopolysaccharide found on Gram-negative bacteria, but members of this family may have many other functions. Genes for the BPI/LBP/PLUNC superfamily are found in all vertebrate species, including distant homologs in non-vertebrate species such as insects, mollusks, and roundworms. Within that broad grouping is the BPIF gene family whose members encode the BPI fold structur ...
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BPIFB2
BPI fold-containing family B, member 2, (BPIFB2) also known as bactericidal/permeability-increasing protein-like 1, (BPI-like 1) is a protein that in humans is encoded by the ''BPIFB2'' gene. Superfamily BPIFB2 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/ CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains of lipopolysaccharide found on Gram-negative bacteria, but members of this family may have many other functions. Genes for the BPI/LBP/PLUNC superfamily are found in all vertebrate species, including distant homologs in non-vertebrate species such as insects, mollusks, and roundworms. Within that broad grouping is the BPIF gene family whose m ...
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BPIFB1
BPI fold containing family B, member 1 (BPIFB1) is a protein that in humans is encoded by the ''BPIFB1'' gene. BPIFB1 is a secreted protein, expressed at very high levels in mucosa of the airways (respiratory and olfactory epithelium) and salivary glands, and at moderate levels in the digestive tract (tongue, stomach, intestinal epithelium) and pancreas. Superfamily BPIFB1 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic molecules, such as the acyl carbon chains of lipopolysaccharide found on Gram-negative bacteria, but members of this family may have many other functions. Genes for the BPI/LBP/PLUNC superfamily are found in all vertebrate sp ...
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BPIFA4P
BPI fold containing family A, member 4 (BPIFA4) is a non-human protein encoded by the ''Bpifa4'' gene in monkey and cow. It is also known as Latherin in horse, encoded by the ''Lath/Bpifa4'' gene but somewhat divergent from the other species. Latherin/BPIFA4 is a secreted protein found in saliva and sweat. In humans, no protein is normally expressed and BPIFB5P is present only as a pseudogene ''BPIFB5P''. However, it has appeared as a secreted product in breast cancer cell lines, previously named BASE (''b''reast cancer ''a''nd ''s''alivary gland ''e''xpression) protein. Superfamily BPIFA3 is a member of a BPI fold protein superfamily defined by the presence of the bactericidal/permeability-increasing protein fold (BPI fold) which is formed by two similar domains in a "boomerang" shape. This superfamily is also known as the BPI/LBP/PLUNC family or the BPI/ LPB/ CETP family. The BPI fold creates apolar binding pockets that can interact with hydrophobic and amphipathic mole ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ...
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Human Proteins
Humans (''Homo sapiens'') are the most abundant and widespread species of primate, characterized by bipedalism and exceptional cognitive skills due to a large and complex brain. This has enabled the development of advanced tools, culture, and language. Humans are highly social and tend to live in complex social structures composed of many cooperating and competing groups, from families and kinship networks to political states. Social interactions between humans have established a wide variety of values, social norms, and rituals, which bolster human society. Its intelligence and its desire to understand and influence the environment and to explain and manipulate phenomena have motivated humanity's development of science, philosophy, mythology, religion, and other fields of study. Although some scientists equate the term ''humans'' with all members of the genus ''Homo'', in common usage, it generally refers to ''Homo sapiens'', the only extant member. Anatomically modern huma ...
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Knockout Mouse
A knockout mouse, or knock-out mouse, is a genetically modified mouse (''Mus musculus'') in which researchers have inactivated, or "knocked out", an existing gene by replacing it or disrupting it with an artificial piece of DNA. They are important animal models for studying the role of genes which have been sequenced but whose functions have not been determined. By causing a specific gene to be inactive in the mouse, and observing any differences from normal behaviour or physiology, researchers can infer its probable function. Mice are currently the laboratory animal species most closely related to humans for which the knockout technique can easily be applied. They are widely used in knockout experiments, especially those investigating genetic questions that relate to human physiology. Gene knockout in rats is much harder and has only been possible since 2003. The first recorded knockout mouse was created by Mario R. Capecchi, Martin Evans, and Oliver Smithies in 1989, for whi ...
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