Protein capable of counteracting the damaging effects of oxidation, e.g. by trapping free radicals generated during the metabolic burst and possibly inhibiting ageing. Scavengers of highly reactive and harmful oxygen species
Protein involved in hypersensitive response, a complex and early defense response that causes necrosis and cell death to restrict the growth of a pathogen. Local and systemic biochemical changes include generation of active oxygen species (oxidative burst), cell death, overproduction of lignin-related materials, and the induction of certain proteins such as pathogen related (PR) proteins
Protein originating from a species thought to be extinct, i.e. from a species for which no known surviving specimens are known to exist. Eg Dodo, Mammoth or Neanderthal
Protein involved in respiratory chain. In aerobic respiration electrons are transferred from metabolites to molecular oxygen through a series of redox reactions mediated by an electron transport chain The resulting free energy is used for the formation of ATP and NAD. In anaerobic respiration analogous reactions take place with an inorganic compound other than oxygen as ultimate electron acceptor
Protein involved in the synthesis of cysteine, the amino acid with the highly reactive sulfhydryl group (-SH). It is derived from the amino acids methionine and serine. Cysteine plays a special role in shaping some proteins by forming disulfide bonds. In enzymes the unique reactivity of this group is frequently exploited at the catalytic site
Protein involved in the self-incompatibility system, which is to say the inability of pollen grains to fertilize flowers of the same plant or a close relative. This mechanism ensures out-breeding in certain plant species
Protein involved in fruiting body formation or expressed in fruiting bodies, any specialized reproductive structure that produces spores or gametes in fungi, slime molds, algae, etc. Fruiting bodies are distinct in size, shape and coloration for each species
Protein involved in the biosynthesis of prostaglandins. Prostaglandins are fatty acids composed of 20 carbons with a substituted cyclopentane ring. There are four major classes of prostaglandin, which differ in the position of the double bonds and/or the oxygen substituents on the ring: PGA, PGB, PGE, and PGF. They are found in many mammalian tissues
Protein involved in a biochemical reaction with prostaglandins Prostaglandins are fatty acids composed of 20 carbons with a substituted cyclopentane ring. There are four major classes of prostaglandin, which differ in the position of the double bonds and/or the oxygen substituents on the ring: PGA, PGB, PGE, and PGF. They are found in many mammalian tissues
Protein involved in the biosynthetic pathway leading from pantothenate to coenzyme A (CoA). CoA has two halves in phosphodiester linkage: a 3',5'-ADP residue, and 4-phosphopantetheine. The phosphopantetheine moiety is itself composed of three structural entities: a branched chain dihydroxy acid in amide linkage to a beta-alanyl residue, which is in turn linked to a cysteamide containing the reactive thiol Coenzyme A functions as a carrier of acetyl and acyl groups and is essential for numerous biosynthetic, energy-yielding, and degradative metabolic pathways. Acetyl-CoA is the common cellular currency for acetyl transfers
Protein involved in the synthesis of ubiquinone which involves the conversion of chorismate into 4-hydroxy-benzoate, to which is added six to ten isoprene units to form polyprenyl phenol. The addition of a further oxygen atom at C3, followed by the transfer of three methyl groups from S-adenosine methionine gives rise to ubiquinol, which is further reduced to ubiquinone (6-polyprenyl-2,3-dimethoxy-5-methyl- 1,4-benzoquinone)
Protein interacting with bacteriochlorophyll, a photosynthetic pigment found in non-oxygenic photosynthetic bacteria. It is a magnesium- porphyrin complex esterified to a long hydrophobic terpenoid side chain (the alcohol phytol). It differs from chlorophyll of oxygenic organisms in the substituents around the tetrapyrrole nucleus of the molecule, and in the absorption spectra. Different bacteria have different species of bacteriochlorophyll
Protein induced in several plant species when they are infected by viruses, viroids, fungi or bacteria. The occurrence of these proteins is not pathogen-specific, but determined by the type of reaction of the host plant. They form a protective barrier against pathogens by collecting at infection sites and act to decrease susceptibility of plants. They may have anti-fungal or anti-bacterial activity
Protein which interferes with the function of chloride channels which are membrane proteins forming a channel in a biological membrane selectively permeable to chloride ions. Chloride channels include voltage-gated chloride channels (ClC), ionotropic GABA receptors (ligand-gated ion channels activated by GABA) and CFTR ion channels (ABC transporter-class ion channels). Toxins that target these channels are found in venom of several species including scorpions and snakes
Protein which is part of a reference proteome. Reference proteomes are a subset of proteomes that have been selected either manually or algorithmically according to a number of criteria to provide a broad coverage of the tree of life and a representative cross-section of the taxonomic diversity found within UniProtKB, as well as the proteomes of well-studied model organisms and other species of interest for biomedical research
Protein containing at least one heme, an iron atom coordinated to a protoporphyrin IX. In myoglobin and hemoglobin, one of the coordination positions of iron is occupied by oxygen or other ligands, such as carbon monoxide. Hemes are also found in cytochromes of the electron-transport chain where they bind electrons, in reducing peroxides (catalases and peroxidases), and act as terminal components in multienzyme systems involved in hydroxylation. Cytochrome c is the only common heme protein in which the heme is covalently bound
Protein located in or on the magnetosome, a membrane-bound bacterial organelle that envelops crystals of magnetic iron minerals in magnetotactic bacteria. Magnetosomes form linear chains that align along the cellular motility axis at midcell and function in bacterial navigation along the Earth's magnetic field. They are formed by invagination of the cell inner membrane; in some species they remain connected to the inner membrane, in others they pinch off to form independent intracellular vesicles
Protein involved in the synthesis of ascorbate, the ionized form of ascorbic acid (vitamin C). Ascorbic acid is derived from glucose via the uronic acid pathway. This water-soluble vitamin is essential for the synthesis of bone, cartilage and dentine. It is required in the diet of primates and some other species that cannot synthesize L- ascorbic acid because of their deficiency in L-gulono-gamma-lactone oxidase, a key enzyme for the biosynthesis of this vitamin
Protein which, if defective, causes congenital absolute erythrocytosis, a disorder characterized by expansion of the erythrocyte compartment in the peripheral blood. Total red cell mass is increased in the absence of a reduction of plasma volume Erythrocytoses are usually divided into primary and secondary forms Primary erythrocytoses are due to defects in the erythroid progenitors and are characterized by low erythropoietin levels. Secondary erythrocytoses can be due to defects in hypoxia sensing, or to conditions that cause low tissue oxygen tension with consequent increase in erythropoietin secretion
Protein involved in virulence, the degree of pathogenicity within a group or species of microorganisms or viruses, as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host. In some cases, the virulence factor can be borne by another organism in symbiosis with the one whose virulence is increased. Some prokaryotic viruses/proviruses for example bear exotoxins that increase the virulence of their host. A well-known bacterial exotoxin encoded by a provirus is the diphtheria toxin
Protein involved in a system responding to environmental changes characterized usually by a sensor kinase in the cell membrane that phosphorylates itself in response to a signal and a response regulator to which the phosphoryl group is transferred. The responder is typically a DNA-binding protein that regulates transcription. Several of these systems are quite complex, involving many proteins in a signaling cascade or contributing to several responses simultaneously They are involved in a variety processes such as chemotaxis, osmoregulation, magnesium transport, pH tolerance, sporulation, or response of virulent species to host cell's environments
Protein which, if defective, causes amyloidosis, a vast group of diseases defined by the accumulation of amyloid in tissues Amyloidoses are classified according to clinical signs, biochemical type of amyloid protein involved, and the extent of amyloid deposition (generalized or localized). Most amyloidoses are multisystemic diseases affecting several organs or systems. Mainly affected organs are the kidneys, heart, gastrointestinal tract, liver, skin, peripheral nerves and eyes, but any organ can be affected. The most frequent forms are primary amyloidosis, also known as light-chain immunoglobulin amyloidosis (AL), reactive or inflammatory amyloidosis, also known as acquired amyloidosis (AA), and transthyretin amyloidosis (ATTR). Localized amyloidosis affecting the brain is characteristic of Alzheimer's disease, trisomy 21, and prion diseases (transmissible spongiform encephalitis, Creutzfeldt-Jakob disease, Gerstmann- Straussler-Scheinker syndrome, fatal familial insomnia). In prion diseases the amyloid precursor is the prion protein
Protein related to the vacuole of a cell. The precise form and function of vacuoles may vary between phyla. Plant vacuoles are among the best characterized. They are generally large fluid-filled compartments in the cytoplasm, bounded by a membrane called the tonoplast; individual vacuoles can fuse to form larger species Examples include the lytic vacuole, the storage vacuole and the lutoid. One important function of plant vacuoles is the maintenance of hydrostatic pressure. Other eukaryotes employ vacuoles for a variety of purposes, including storage (as in the yeast lysosome/vacuole), secretion and phagocytosis. In Protozoa, contractile vacuoles can be used to discharge water from the cytoplasm to the external environment
Protein involved in a light-dependent process to convert 2-phospho- glycolate (2-PG) into 3-phospho-D-glycerate (3-PG), where oxygen is consumed and carbon dioxide released. It takes place in plants and cyanobacteria during the light period, since in the presence of O(2) their type of Rubisco can catalyze the oxidative fragmentation of ribulose 1,5-biphosphate to 3-PG and 2-PG. 2-PG inhibits the Calvin cycle enzyme triose-phosphate isomerase, and so must be eliminated quickly. In plants 2-PG is recycled to 3-PG via reactions in peroxisomes, mitochondria as well as chloroplasts. For every 2 molecules of 2-PG, one molecule of 3-PG is formed and one molecule of CO(2) is lost. In cyanobacteria it seems there are two mechanisms to deal with 2-PG; a path similar to that described for plants and the bacterial-like glycerate pathway
Protein which interacts with quinones. Quinones are aromatic dicarbonyl compounds, where the two carbonyl groups are usually in the para position. Most naturally occuring quinones contain a long isoprenoid side chain, and are divided in two major structural groups, the naphtoquinones and benzoquinones; the number of isoprene units depends on the organism. These highly hydrophobic molecules are mainly involved in electron transport, as electron carriers in redox reactions. For example, ubiquinone (coenzyme Q) and menaquinone (vitamin K2) are essential components of the respiratory electron transport chain. Plastoquinone, found in chloroplasts and in cyanobacteria, functions as one of the carrier molecules of the electron transport chain in photosynthesis. Phylloquinone (vitamin K1) is the major form of vitamin K found in plants. Chlorobiumquinone, demethylmenaquinone, alpha-tocopherolquinone, rhodoquinone, epoxyubiquinone and caldariellaquinone are other quinones found in several species
Protein which is part of an anion channel found in the plasma membrane and in intracellular membranes. These channels are permeable for various anions, such as iodide, bromide, but also for nitrates, phosphates and even negatively charged amino acids. They are called chloride channels, because chloride is the most abundant anion and the predominant permeating species in all organisms. They have been classified according to their gating mechanisms, which may depend on changes in the transmembrane electric field (voltage-dependent/gated chloride channels, e.g. ClC family), on a protein kinase/nucleotide mediated mechanism (CFTR), an increase in intracellular calcium (calcium activated chloride channels, e.g. CaCC), cell swelling (volume-regulated anion channels, e.g. VRAC) or binding of a ligand, e.g. glycine or - aminobutyric acid (GABA) activated channels. In contrast with cation channels, they are not involved in the initiation or spread of excitation, but in the regulation of excitability in nerve and muscle. They also participate in many housekeeping processes, such as volume regulation, pH regulation in organelles, electrogenesis and control of synaptic activity. The chloride channels are crucial for transepithelial transport and the control of water flow, and often provide unexpected permeation pathways for a large variety of anions
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