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https://en.wikipedia.org/wiki/C5AR2 | C5a anaphylatoxin chemotactic receptor 2 is a protein that in humans is encoded by the C5AR2 gene. It's a complement component G protein-coupled receptor, of class A (rhodopsin-like).
Function
The anaphylatoxins C3a, C4a, and C5a are cationic fragments generated during the complement cascade that participate in host defense. In the case of inappropriate complement activation, anaphylatoxins may be involved in autoimmunity and sepsis. C5a2 is coexpressed with the C5a receptor, (C5a1, C5aR, C5R1, CD88), on polymorphonuclear neutrophils and may modulate C5a1 activity.
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/P2RY10 | Putative P2Y purinoceptor 10 is a protein that, in humans, is encoded by the P2RY10 gene.
Function
The protein encoded by this gene belongs to the family of G-protein coupled receptors that is preferentially activated by adenosine and uridine nucleotides. Two alternatively spliced transcript variants encoding the same protein isoform have been found for this gene.
See also
P2Y receptor
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR171 | Probable G-protein coupled receptor 171 is a protein that in humans is encoded by the GPR171 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR132 | G protein coupled receptor 132, also termed G2A, is classified as a member of the proton sensing G protein coupled receptor (GPR) subfamily. Like other members of this subfamily, i.e. GPR4, GPR68 (OGR1), and GPR65 (TDAG8), G2A is a G protein coupled receptor that resides in the cell surface membrane, senses changes in extracellular pH, and can alter cellular function as a consequence of these changes. Subsequently, G2A was suggested to be a receptor for lysophosphatidylcholine (LPC). However, the roles of G2A as a pH-sensor or LPC receptor are disputed. Rather, current studies suggest that it is a receptor for certain metabolites of the polyunsaturated fatty acid, linoleic acid.
The G2A gene
G2A in humans is encoded by the GPR132 gene. The G2A gene is located on chromosome 14q32.3 codes for two alternative splice variants, the original one, G2A-a, and G2A-b, that consist of 380 and 371 amino acids, respectively; the two receptor variants, when expressed in Chinese hamster ovary cells, gave very similar results when analyzed for functionality. G2A-a and G2A-b mRNA are expressed at similar levels in blood leukocytes ( macrophages, dendritic cells, neutrophils [PMN], mast cells, T lymphocytes and B lymphocytes at the highest levels followed by lower levels in spleen, lung and heart tissues; both variants are expressed at similar levels, and are almost equally induced by DNA synthesis inhibitors (hydroxyurea and cytosine arabinoside) or a differentiation inducer (all-tran |
https://en.wikipedia.org/wiki/Relaxin/insulin-like%20family%20peptide%20receptor%203 | Relaxin/insulin-like family peptide receptor 3, also known as RXFP3, is a human G-protein coupled receptor.
See also
Relaxin receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/CCRL1 | C-C chemokine receptor type 11 is a protein that in humans is encoded by the CCRL1 gene.
The protein encoded by this gene is a member of the G protein-coupled receptor family, and is a receptor for C-C type chemokines. This receptor has been shown to bind dendritic cell- and T cell-activated chemokines including CCL19/ELC, CCL21/SLC, and CCL25/TECK. Alternatively spliced transcript variants encoding the same protein have been described.
References
Further reading
External links
Chemokine receptors |
https://en.wikipedia.org/wiki/S1PR5 | Sphingosine-1-phosphate receptor 5 also known as S1PR5 is a human gene which encodes a G protein-coupled receptor which binds the lipid signaling molecule sphingosine 1-phosphate (S1P). Hence this receptor is also known as S1P5.
Agonists
A-971432
Sphingosine 1-phosphate receptor agonists: a patent review (2010-2012)
See also
Lysophospholipid receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/P2RY13 | P2Y purinoceptor 13 is a protein that in humans is encoded by the P2RY13 gene.
The product of this gene, P2Y13, belongs to the family of G-protein coupled receptors. This family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. This receptor is activated by ADP. Two transcript variants encoding the same protein have been identified for this gene.
See also
P2Y receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR84 | Probable G-protein coupled receptor 84 is a protein that in humans is encoded by the GPR84 gene.
Discovery
GPR84 (EX33) was described practically in the same time by two groups. One was the group of Timo Wittenberger in the Zentrum fur Molekulare Neurobiologie, Hamburg, Germany (Wittenberg T. et al.) and the other was the group of Gabor Jarai in Novartis Horsham Research Centre, Horsham, United Kingdom. In their papers they described the sequence and expression profile of five new members of GPC receptor family. One among them was GPR84 which represents a unique GPCR sub-family so far.
Gene
Hgpr84 locates to chromosome 12q13.13, and its coding sequence is not interrupted by introns.
Protein
The human and the murine GPR84 ORFs both encode proteins of 396 amino acid residues length with 85% identity and are therefore considered as orthologs. The hgpr84 was found by Northern blot analysis as a transcript of about 1.5 kb in brain, heart, muscle, colon, thymus, spleen, kidney, liver, intestine, placenta, lung, and leukocytes. In addition, a 1.2 kb transcript in heart and a strong band at 1.3 kb in muscle were detected. A Northern blot from different brain regions revealed strongest expression of the 1.5 kb transcript in the medulla and the spinal cord. Somewhat less transcript was found in the substantia nigra, thalamus, and the corpus callosum. The 1.5 kb band was also visible in other brain regions, but at very low levels. EST clones corresponding to hgpr84 were from B |
https://en.wikipedia.org/wiki/GPR87 | Probable G-protein coupled receptor 87 is a protein that in humans is encoded by the GPR87 gene.
G protein-coupled receptors play a role in cell communication. They are characterized by an extracellular N terminus, 7 transmembrane regions, and an intracellular C terminus.[supplied by OMIM]
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR173 | Probable G-protein coupled receptor 173 is a protein that in humans is encoded by the GPR173 gene.
See also
SREB
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/LGR4 | Leucine-rich repeat-containing G-protein coupled receptor 4 is a protein that in humans is encoded by the LGR4 gene. LGR4 is known to have a role in the development of the male reproductive tract, eyelids, hair and bone.
Mutations in this gene have been associated to osteoporosis (doi:10.1038/nature12124).
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Leukotriene%20B4%20receptor%202 | {{DISPLAYTITLE:Leukotriene B4 receptor 2}}
Leukotriene B4 receptor 2, also known as BLT2, BLT2 receptor, and BLTR2, is an Integral membrane protein that is encoded by the LTB4R2 gene in humans and the Ltbr2 gene in mice.
Discovered several years after the leukotriene B4 receptor 1 (BLT1), BLT2 receptor binds leukotriene B4 (LTB4) with far lower affinity than the BLT1 receptor does and therefore has been termed the low affinity LTB4 receptor. Sometime after its initial discovery, the BLT2 receptor was shown to bind and become activated by several other arachidonic acid metabolites, one of which, 12-hydroxyheptadecatrienoic acid (12-HHT), has 10- to 100-fold higher affinity for it than does LTB4; 12-HHT fails to bind or activate BLT1 receptors. While BLT2 receptors have some actions similar to BLT1 receptors, they have other actions which clearly oppose those of BLT1 in regulating inflammation and allergic responses; BLT2 receptors also have actions that extend beyond those of BLT1 receptors. Laboratory, animal, and other pre-clinical studies suggest that BLT2 receptors may be involved not only in inflammation and allergy but also in human cancer.
Function
BLT2 is a Cell surface receptor that functions by recognizing, binding, and mediating responses to a particular set of messenger molecules or ligands. These messenger ligands are any one of a range of structurally different arachidonic acid metabolites made and released by nearby cells to act as paracrine signals for |
https://en.wikipedia.org/wiki/SUCNR1 | Succinate receptor 1 is a protein that in humans is encoded by the SUCNR1 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/ACKR3 | Atypical chemokine receptor 3 also known as C-X-C chemokine receptor type 7 (CXCR-7) and G-protein coupled receptor 159 (GPR159) is a protein that in humans is encoded by the ACKR3 gene.
This gene encodes a G protein-coupled receptor family member. It belongs to the chemokine receptor family of GPCRs. Within this family, ACKR3 is classified as a class A GPCR. This GPCR protein was earlier thought to be a receptor for vasoactive intestinal peptide (VIP) and was considered to be an orphan receptor. It is now classified as a chemokine receptor able to bind the chemokines CXCL12/SDF-1 and CXCL11. The protein is also a coreceptor for human immunodeficiency viruses (HIV). Translocations involving this gene and HMGA2 on chromosome 12 have been observed in lipomas. Alternatively spliced transcript variants encoding the same protein isoform have been found for this gene. Whereas some reports claim that the receptor induces signaling following ligand binding, recent findings in zebrafish suggest that CXCR7 functions primarily by sequestering the chemokine CXCL12.
Another study has provided evidence that ligand binding to CXCR7 activates MAP kinases through Beta-arrestins, and thus has functions beyond ligand sequestration.
ACKR3 has also been shown to sequester endogenous opioid peptides, and is thought to modulate their activity. Inhibition of ACKR3 by ligands such as the peptide LIH383 (FGGFMRRK-NH2) increases opioid peptide activity and produces analgesic and antidepressant effec |
https://en.wikipedia.org/wiki/LPAR5 | Lysophosphatidic acid receptor 5 also known as LPA5 is a protein that in humans is encoded by the LPAR5 gene. LPA5 is a G protein-coupled receptor that binds the lipid signaling molecule lysophosphatidic acid (LPA).
See also
Lysophospholipid receptor
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/VN1R1 | Vomeronasal type-1 receptor 1 is a protein that in humans is encoded by the VN1R1 gene.
Function
Pheromones are chemical signals that elicit specific behavioral responses and physiologic alterations in recipients of the same species. The protein encoded by this gene is similar to pheromone receptors and is primarily localized to the olfactory mucosa. An alternate splice variant of this gene is thought to exist, but its full length nature has not been determined.
Ligands
Decanal
Hedione
Iso E Super
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR126 | G protein-coupled receptor 126 also known as VIGR and DREG is a protein encoded by the ADGRG6 gene. GPR126 is a member of the adhesion GPCR family.
Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
GPR126 is all widely expressed on stromal cells. The N-terminal fragment of GPR126 contains C1r-C1s, Uegf and Bmp1 (CUB), and PTX-like modules.
Ligand
GPR126 was shown to bind collagen IV and laminin-211 promoting cyclic adenosine monophosphate (cAMP) to mediate myelination.
Signaling
Upon lipopolysaccharide (LPS) or thrombin stimulation, expression of GPR126 is induced by MAP kinases in endothelial cells. During angiogenesis, GPR126 promotes protein kinase A (PKA)–cAMP-activated signaling in endothelial cells. Forced GPR126 expression in COS-7 cells enhances cAMP levels by coupling to heterotrimeric Gαs/i proteins.
Function
GPR126 has been identified in genomic regions associated with adult height, more specially trunk height, pulmonary function and adolescent idiopathic scoliosis. In the vertebrate nervous system, many axons are surrounded by a myelin sheath to conduct action potentials rapidly and efficiently. Applying a genetic screen in zebrafish mutants, Talbot’s group demonstrated that GPR126 affects the development of myelinated axons. GPR126 drives the differentiation of Schwann cells through inducing cA |
https://en.wikipedia.org/wiki/Ion%20trapping | In cell biology, ion trapping is the build-up of a higher concentration of a chemical across a cell membrane due to the pKa value of the chemical and difference of pH across the cell membrane. This results in basic chemicals accumulating in acidic bodily fluids such as the cytosol, and acidic chemicals accumulating in basic fluids.
Mechanism
Many cells have other mechanisms to pump a molecule inside or outside the cell against the concentration gradient, but these processes are active ones, meaning that they require enzymes and consume cellular energy. In contrast, ion trapping does not require any enzyme or energy. It is similar to osmosis in that they both involve the semipermeable nature of the cell membrane.
Cells have a more acidic pH inside the cell than outside (gastric mucosal cells being an exception). Therefore, basic drugs (like bupivacaine, pyrimethamine) are more charged inside the cell than outside. The cell membrane is permeable to non-ionized (fat-soluble) molecules; ionized (water-soluble) molecules cannot cross it easily. Once a non-charged molecule of a basic chemical crosses the cell membrane to enter the cell, it becomes charged due to gaining a hydrogen ion because of the lower pH inside the cell, and thus becomes unable to cross back. Because transmembrane equilibrium must be maintained, another unionized molecule must diffuse into the cell to repeat the process. Thus its concentration inside the cell increases many times that of the outside. The non- |
https://en.wikipedia.org/wiki/GPR158 | Probable G-protein coupled receptor 158 (GPR158), also known as the metabotropic glycine receptor (mGlyR), is a protein that in humans is encoded by the GPR158 gene.
Function
This protein is an orphan class C GPCR. It is highly expressed in the brain, where it binds to RGS7, an inhibitor of Gi/o-coupled GPCR signaling, localizing it to the plasma membrane.
It is expressed at lower levels in other organs and shows an unusual subcellular localization pattern, being found at both the plasma membrane and in the nucleus.
Clinical significance
Role in mood regulation
GPR158 in the medial prefrontal cortex (mPFC) has been shown to regulate stress-induced depression in a mouse model of depression and has been found to be upregulated in post-mortem tissue samples from humans with major depressive disorder (MDD).
Role in prostate cancer
The GPR158 gene is an androgen-regulated gene that stimulates cell proliferation in prostate cancer cell lines, and it is linked to neuroendocrine differentiation.
References
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR107 | Protein GPR107 is a protein that in humans is encoded by the GPR107 gene.
References
Further reading |
https://en.wikipedia.org/wiki/Relaxin/insulin-like%20family%20peptide%20receptor%201 | Relaxin/insulin-like family peptide receptor 1, also known as RXFP1, is a human G protein coupled receptor that is one of the relaxin receptors. It is a rhodopsin-like GPCR which is unusual in this class as it contains a large extracellular binding and signalling domain. Some reports suggest that RXFP1 forms homodimers, however the most recent evidence indicates that relaxin binds a non-homodimer of RXFP1.
See also
Relaxin family peptide hormones
Insulin/IGF/Relaxin family
Relaxin
Relaxin-3
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Neuropeptide%20FF%20receptor%201 | Neuropeptide FF receptor 1, also known as NPFF1 is a human protein, encoded by the NPFFR1 gene.
See also
Neuropeptide FF receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Horst%20H.%20Berger | Horst H. Berger (born March 30, 1933) is a German electrical engineer noted for his contributions to semiconductor technologies for integrated circuits.
Berger was born in Liegnitz (Legnica), Lower Silesia, and received the Vordiplom. from the Technische Hochschule of Dresden, then worked at the IBM Laboratories in Böblingen. Afterwards he became a researcher and teacher at the Technical University of Berlin.
Together with Siegfried K. Wiedmann, Berger received the 1977 IEEE Morris N. Liebmann Memorial Award "for the invention and exploration of the Merged Transistor Logic, MTL".
Selected works
H. H. Berger and S. K. Wiedmann, "Merged-Transistor Logic (MTL) – A Low-Cost Bipolar Logic Concept", IEEE Journal of Solid-State Circuits, vol. SC-7, No. 5, Oct. 1972, pp. 340–346.
References
Fruchtbare Quelle: Horst Berger wurde 70 (German)
Contributors, IEEE Journal of Solid-State Circuits, Volume 7, Issue 5, pages 435–440. October 1972.
1933 births
Living people
People from Legnica
German electrical engineers
IBM employees
People from the Province of Lower Silesia
Academic staff of the Technical University of Berlin
Computer hardware engineers
Semiconductor technology |
https://en.wikipedia.org/wiki/GPR135 | Probable G-protein coupled receptor 135 is a protein that in humans is encoded by the GPR135 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Channel-conductance-controlling%20ATPase | In enzymology, a channel-conductance-controlling ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (channel-conductance-controlling).
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.6.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Chloroplast%20protein-transporting%20ATPase | In enzymology, a chloroplast protein-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (chloroplast protein-importing).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DCTP%20diphosphatase | In enzymology, a dCTP diphosphatase () is an enzyme that catalyzes the chemical reaction
dCTP + H2O dCMP + diphosphate
Thus, the two substrates of this enzyme are dCTP and H2O, whereas its two products are dCMP and diphosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is dCTP nucleotidohydrolase. Other names in common use include deoxycytidine-triphosphatase, dCTPase, dCTP pyrophosphatase, deoxycytidine triphosphatase, deoxy-CTPase, and dCTPase. This enzyme participates in pyrimidine metabolism.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diphosphoinositol-polyphosphate%20diphosphatase | In enzymology, a diphosphoinositol-polyphosphate diphosphatase () is an enzyme that catalyzes the chemical reaction
diphospho-myo-inositol polyphosphate + H2O myo-inositol polyphosphate + phosphate
Thus, the two substrates of this enzyme are diphospho-myo-inositol polyphosphate and H2O, whereas its two products are myo-inositol polyphosphate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is diphospho-myo-inositol-polyphosphate diphosphohydrolase. Other names in common use include diphosphoinositol-polyphosphate phosphohydrolase, and DIPP.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 3.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Cl-transporting%20ATPase | In enzymology, a Cl-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + Cl−out ADP + phosphate + Cl−in
The 3 substrates of this enzyme are ATP, H2O, and Cl−, whereas its 3 products are ADP, phosphate, and Cl−.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Cl−-importing). Other names in common use include Cl−-translocating ATPase, and Cl−-motive ATPase.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dolichyldiphosphatase | In enzymology, a dolichyldiphosphatase () is an enzyme that catalyzes the chemical reaction
dolichyl diphosphate + H2O dolichyl phosphate + phosphate
Thus, the two substrates of this enzyme are dolichyl diphosphate and H2O, whereas its two products are dolichyl phosphate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is dolichyl-diphosphate phosphohydrolase. Other names in common use include dolichol diphosphatase, dolichyl pyrophosphatase, dolichyl pyrophosphate phosphatase, dolichyl diphosphate phosphohydrolase, and Dol-P-P phosphohydrolase. This enzyme participates in n-glycan biosynthesis.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DUTP%20diphosphatase | In Enzymology, a dUTP diphosphatase () is an enzyme that catalyzes the chemical reaction
dUTP + H2O dUMP + diphosphate
Thus, the two substrates of this enzyme are dUTP and H2O, whereas its two products are dUMP and diphosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is dUTP nucleotidohydrolase. Other names in common use include deoxyuridine-triphosphatase, dUTPase, dUTP pyrophosphatase, desoxyuridine 5'-triphosphate nucleotidohydrolase, and desoxyuridine 5'-triphosphatase. This enzyme participates in pyrimidine metabolism.
This enzyme has a dual function: on one hand, it removes dUTP from the deoxynucleotide pool, which reduces the probability of this base being incorporated into DNA by DNA polymerases, while on the other hand, it produces the dTTP precursor dUMP. Lack or inhibition of dUTPase action leads to harmful perturbations in the nucleotide pool resulting in increased uracil content of DNA that activates a hyperactive futile cycle of DNA repair.
Structural studies
As of late 2007, 48 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
There are at least two structurally distinct families of dUTPases. The crystal structure of human dUTPase reveals that each subunit of the dUTPase trimer folds into an ei |
https://en.wikipedia.org/wiki/GPR157 | Probable G-protein coupled receptor 157 is a protein that in humans is encoded by the GPR157 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Endopolyphosphatase | In enzymology, an endopolyphosphatase () is an enzyme that catalyzes the chemical reaction
polyphosphate + n H2O (n+1) oligophosphate
Thus, the two substrates of this enzyme are polyphosphate and H2O, whereas its product is oligophosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is polyphosphate polyphosphohydrolase. Other names in common use include polyphosphate depolymerase, metaphosphatase, polyphosphatase, and polymetaphosphatase.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Exopolyphosphatase | Exopolyphosphatase (PPX) is a phosphatase enzyme which catalyzes the hydrolysis of inorganic polyphosphate, a linear molecule composed of up to 1000 or more monomers linked by phospho-anhydride bonds. PPX is a processive exophosphatase, which means that it begins at the ends of the polyphosphate chain and cleaves the phospho-anhydride bonds to release orthophosphate as it moves along the polyphosphate molecule. PPX has several characteristics which distinguish it from other known polyphosphatases, namely that it does not act on ATP, has a strong preference for long chain polyphosphate, and has a very low affinity for polyphosphate molecules with less than 15 phosphate monomers.
PPX plays an important role in the metabolism of phosphate and energy in all living organisms. It is especially important for maintenance of appropriate levels of intracellular polyphosphate, which has been implicated in a variety of cellular functions including response to stressors such as deficiencies in amino acids, orthophosphate, or nitrogen, changes in pH, nutrient downshift, and high salt, and as an inorganic molecular chaperone.
PPX is classified as a polyphosphatase, which are part of the large DHH phosphoesterase family. Both subfamilies within this super family share four N-terminus motifs but have different C-terminus moieties.
PPX activity is quantified by measuring the loss of radioactively labeled 32P polyphosphate. PPX is mixed with a known quantity of labeled polyphosphate, |
https://en.wikipedia.org/wiki/FAD%20diphosphatase | In enzymology, a FAD diphosphatase () is an enzyme that catalyzes the chemical reaction
FAD + H2O AMP + FMN
Thus, the two substrates of this enzyme are FAD and H2O, whereas its two products are AMP and FMN.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is FAD nucleotidohydrolase. Other names in common use include FAD pyrophosphatase, riboflavin adenine dinucleotide pyrophosphatase, flavin adenine dinucleotide pyrophosphatase, riboflavine adenine dinucleotide pyrophosphatase, and flavine adenine dinucleotide pyrophosphatase. This enzyme participates in riboflavin metabolism.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fatty-acyl-CoA-transporting%20ATPase | In enzymology, a fatty-acyl-CoA-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + fatty acyl CoAcis ADP + phosphate + fatty acyl CoAtrans
The 3 substrates of this enzyme are ATP, H2O, and fatty acyl CoAcis, whereas its 3 products are ADP, phosphate, and fatty acyl CoAtrans.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (fatty-acyl-CoA-transporting).
References
EC 7.6.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Fe3%2B-transporting%20ATPase | In enzymology, a Fe3+-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + Fe3+out ADP + phosphate + Fe3+in
The 3 substrates of this enzyme are ATP, H2O, and Fe3+, whereas its 3 products are ADP, phosphate, and Fe3+.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (ferric-ion-transporting). This enzyme participates in abc transporters - general.
References
EC 7.2.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glycerol-3-phosphate-transporting%20ATPase | In enzymology, a glycerol-3-phosphate-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + glycerol-3-phosphateout ADP + phosphate + glycerol-3-phosphatein
The 3 substrates of this enzyme are ATP, H2O, and glycerol-3-phosphate, whereas its 3 products are ADP, phosphate, and glycerol-3-phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (glycerol-3-phosphate-importing). This enzyme participates in abc transporters - general.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Guanine-transporting%20ATPase | In enzymology, a guanine-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + guanineout ADP + phosphate + guaninein
The 3 substrates of this enzyme are ATP, H2O, and guanine, whereas its 3 products are ADP, phosphate, and guanine. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (guanine-importing).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Guanosine-5%27-triphosphate%2C3%27-diphosphate%20diphosphatase | In enzymology, a guanosine-5'-triphosphate,3'-diphosphate diphosphatase () is an enzyme that catalyzes the chemical reaction
guanosine 5'-triphosphate,3'-diphosphate + H2O guanosine 5'-diphosphate,3'-diphosphate + phosphate
Thus, the two substrates of this enzyme are guanosine 5'-triphosphate,3'-diphosphate and H2O, whereas its two products are guanosine 5'-diphosphate,3'-diphosphate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is guanosine-5'-triphosphate,3'-diphosphate 5'-phosphohydrolase. Other names in common use include pppGpp 5'-phosphohydrolase, guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase, guanosine 5'-triphosphate-3'-diphosphate 5'-phosphohydrolase, guanosine pentaphosphatase, guanosine pentaphosphate phosphatase, guanosine 5'-triphosphate 3'-diphosphate 5'-phosphatase, and guanosine pentaphosphate phosphohydrolase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Guanosine-diphosphatase | In enzymology, a guanosine-diphosphatase () is an enzyme that catalyzes the chemical reaction
GDP + H2O GMP + phosphate
Thus, the two substrates of this enzyme are GDP and H2O, whereas its two products are GMP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is GDP phosphohydrolase. This enzyme is also called GDPase.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Heme-transporting%20ATPase | In enzymology, a heme-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + hemein ADP + phosphate + hemeout
The 3 substrates of this enzyme are ATP, H2O, and heme, whereas its 3 products are ADP, phosphate, and heme.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (heme-exporting). This enzyme participates in abc transporters - general.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Iron-chelate-transporting%20ATPase | In enzymology, an iron-chelate-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + iron chelateout ADP + phosphate + iron chelatein
The 3 substrates of this enzyme are ATP, H2O, and iron chelate, whereas its 3 products are ADP, phosphate, and iron chelate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (iron-chelate-importing). This enzyme participates in abc transporters - general.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .
References
EC 3.6.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/K%2B-transporting%20ATPase | {{DISPLAYTITLE:K+-transporting ATPase}}
In enzymology, a K+-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + K+out ADP + phosphate + K+in
The 3 substrates of this enzyme are ATP, H2O, and K+, whereas its 3 products are ADP, phosphate, and K+.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (K+-importing). Other names in common use include K+-translocating Kdp-ATPase, and multi-subunit K+-transport ATPase. This enzyme participates in two-component system - general.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 3.6.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Lipopolysaccharide-transporting%20ATPase | In enzymology, a lipopolysaccharide-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + lipopolysaccharidein ADP + phosphate + lipopolysaccharideout
The 3 substrates of this enzyme are ATP, H2O, and lipopolysaccharide, whereas its 3 products are ADP, phosphate, and lipopolysaccharide.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (lipopolysaccharide-exporting).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Magnetic%20resonance%20spectroscopic%20imaging | Magnetic resonance spectroscopic imaging (MRSI) is a noninvasive imaging method that provides spectroscopic information in addition to the image that is generated by MRI alone.
Whereas traditional magnetic resonance imaging (MRI) generates a black-and-white image in which brightness is determined primarily by the T1 or T2 relaxation times of the tissue being imaged, the spectroscopic information obtained in an MRSI study can be used to infer further information about cellular activity (metabolic information). For example, in the context of oncology, an MRI scan may reveal the shape and size of a tumor, while an MRSI study provides additional information about the metabolic activity occurring in the tumor. MRSI can be performed on a standard MRI scanner, and the patient experience is the same for MRSI as for MRI. MRSI has broad applications in medicine, including oncology and general physiological studies.
When hydrogen is the target element, MRSI is also called 1H-nuclear magnetic resonance spectroscopic imaging and proton magnetic resonance spectroscopic imaging. MRSI can also be performed with phosphorus, or hyperpolarized carbon-13.
References
Magnetic resonance spectroscopic imaging entry in the public domain NCI Dictionary of Cancer Terms
External links
Magnetic resonance imaging |
https://en.wikipedia.org/wiki/GPR63 | Probable G-protein coupled receptor 63 is a protein that in humans is encoded by the GPR63 gene.
G protein-coupled receptors (GPCRs, or GPRs) contain 7 transmembrane domains and transduce extracellular signals through heterotrimeric G proteins.[supplied by OMIM]
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/M7G%285%27%29pppN%20diphosphatase | In enzymology, a m7G(5')pppN diphosphatase () is an enzyme that catalyzes the chemical reaction
7-methylguanosine 5'-triphospho-5'-polynucleotide + H2O 7-methylguanosine 5'-phosphate + polynucleotide
Thus, the two substrates of this enzyme are 7-methylguanosine 5'-triphospho-5'-polynucleotide and H2O, whereas its two products are 7-methylguanosine 5'-phosphate and polynucleotide.
This is the enzyme involved in the processing of amphetamines of the cathinone group, including mephedrone and khat.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is 7-methylguanosine-5'-triphospho-5'-polynucleotide 7-methylguanosine-5'-phosphohydrolase. Other names in common use include decapase, and m7G(5')pppN pyrophosphatase.
See also
7-Methylguanosine
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Malignant%20ectomesenchymoma | Malignant ectomesenchymoma (MEM) is a rare, fast-growing tumor of the nervous system or soft tissue that occurs in children and young adults. MEM is part of a group of small round blue cell tumors which includes neuroblastoma, rhabdomyosarcoma, non-Hodgkin's lymphoma, and the Ewing's family of tumors.
Typical Pathology
Malignant ectomesenchymomas may form in the head and neck, abdomen, perineum, scrotum, or limbs. The tumor is defined by its heterologous rhabdomyoblastic components. MEM histology is that of an elongated cell with an embryonic morphology. Onset time is relatively rapid and occurs early in life with the average age of onset is 0.6 years of age. However, children have been known to develop MEM up until they reach 5 years old. The neuroectodermal component has the potential to display any neuroblastic tumor including neuroblastoma, ganglioneuroblastoma, and ganglion cells with or without schwannian stroma. The rhabdomyoblastic component is derived from pluripotent migratory neural crest cells. The nature and wide migration patterns of neural crest cells allow them to give rise to both neural and non-nervous tissue including neurons, glia, smooth muscle, and melanocytes. Patients have the potential to display primary tumors in various locations prior to metastasis making this cancer particularly complicated.
Differing Representations Across Patients
Unfortunately, heterogenous tumors have the potential to represent further heterogeneity between patients. Beca |
https://en.wikipedia.org/wiki/Maltose-transporting%20ATPase | In enzymology, a maltose-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + maltoseout ADP + phosphate + maltosein
The 3 substrates of this enzyme are ATP, H2O, and maltose, whereas its 3 products are ADP, phosphate, and maltose.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (maltose-importing). This enzyme is a member of the ABC Transporter family.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.6.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Manganese-transporting%20ATPase | In enzymology, a manganese-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + Mn2+out ADP + phosphate + Mn2+in
The 3 substrates of this enzyme are ATP, H2O, and Mn2+, whereas its 3 products are ADP, phosphate, and Mn2+.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is called ATP phosphohydrolase (manganese-importing). This enzyme is also known as ABC-type manganese permease complex.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GPR101 | Probable G-protein coupled receptor 101 is a protein that in humans is encoded by the GPR101 gene.
G protein-coupled receptors (GPCRs, or GPRs) contain 7 transmembrane domains and transduce extracellular signals through heterotrimeric G proteins.
Clinical significance
A duplication event in GPR101 is implicated in cases of gigantism and acromegaly.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Mg2%2B-importing%20ATPase | In enzymology, a Mg2+-importing ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + Mg2+out ADP + phosphate + Mg2+in
The 3 substrates of this enzyme are ATP, H2O, and Mg2+, whereas its 3 products are ADP, phosphate, and Mg2+.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Mg2+-importing).
The mgtA gene which encodes this enzyme is thought to be regulated by a magnesium responsive RNA element. A human enzyme was found in erythrocytes but the observation could not be confirmed.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Malignant%20pleural%20effusion | Malignant pleural effusion is a condition in which cancer causes an abnormal amount of fluid to collect between the thin layers of tissue (pleura) lining the outside of the lung and the wall of the chest cavity. Lung cancer and breast cancer account for about 50-65% of malignant pleural effusions. Other common causes include pleural mesothelioma and lymphoma.
Diagnosis
Clinical evaluation
Clinical factors predicting the diagnosis of malignant pleural effusions are symptoms lasting more than 1 month and the absence of fever.
Imaging
Imaging is needed to confirm the presence of a pleural effusion. A Chest radiograph is usually performed first and may demonstrate an underlying lung cancer as well as the pleural effusion. Ultrasound has a sensitivity of 73% and specificity of 100% at distinguishing malignant pleural effusions from other causes of pleural effusion, based on the presence of visible pleural metastases, pleural thickening greater than 1 cm, pleural nodularity, diaphragmatic thickening measuring greater than 7mm and an echogenic swirling pattern visible in the pleural fluid.
Biochemical analysis
Malignant pleural effusions are exudates. A low pleural fluid pH is associated with poorer survival and reduced pleurodesis efficacy.
Histopathology
Pleural fluid cytology is positive in 60% of cases. However, in the remaining cases, pleural biopsy is required. Image guided biopsy and thoracoscopy have largely replaced blind biopsy due to their greater sensitivity a |
https://en.wikipedia.org/wiki/Microtubule-severing%20ATPase | In enzymology, a microtubule-severing ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to facilitate cellular and subcellular movement. The systematic name of this enzyme class is ATP phosphohydrolase (tubulin-dimerizing).
See also
Katanin
References
EC 3.6.4 |
https://en.wikipedia.org/wiki/Molybdate-transporting%20ATPase | In enzymology, a molybdate-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + molybdateout ADP + phosphate + molybdatein
The 3 substrates of this enzyme are ATP, H2O, and molybdate, whereas its 3 products are ADP, phosphate, and molybdate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (molybdate-importing). This enzyme participates in abc transporters - general.
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyroglutamylated%20RFamide%20peptide%20receptor | Pyroglutamylated RFamide peptide receptor also known as orexigenic neuropeptide QRFP receptor or G-protein coupled receptor 103 (GPR103) is a protein that in humans is encoded by the QRFPR gene.
Function
G protein-coupled receptors (GPCRs, or GPRs) contain 7 transmembrane domains and transduce extracellular signals through heterotrimeric G proteins.
A 26-amino acid RF-amide peptide, P518 functions as a high-affinity ligand of GPR103. Both GPR103 and P518 precursor mRNA exhibited highest expression in brain. The 43-amino acid QRFP peptide, a longer form of the P518 peptide is necessary to exhibit full agonistic activity with GPR103. Intravenous administration QRFP caused release of aldosterone, suggesting that QRFP and GPR103 regulate adrenal function.
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR123 | Probable G-protein coupled receptor 123 is a protein that in humans is encoded by the GPR123 gene. It is a member of the adhesion-GPCR family of receptors. Family members are normally characterized by an extended extracellular region with a variable number of protein domains coupled to a TM7 domain via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Monosaccharide-transporting%20ATPase | In enzymology, a monosaccharide-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + monosaccharideout ADP + phosphate + monosaccharidein
The 3 substrates of this enzyme are ATP, H2O, and monosaccharide, whereas its 3 products are ADP, phosphate, and monosaccharide.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (monosaccharide-importing). This enzyme participates in abc transporters - general.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.6.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/NAD%2B%20diphosphatase | In enzymology, a NAD+ diphosphatase () is an enzyme that catalyzes the chemical reaction
NAD+ + H2O AMP + NMN
Thus, the two substrates of this enzyme are NAD+ and H2O, whereas its two products are AMP and NMN.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is NAD+ phosphohydrolase. Other names in common use include nicotinamide adenine dinucleotide pyrophosphatase, NADP+ pyrophosphatase, and NADH pyrophosphatase. This enzyme participates in nicotinate and nicotinamide metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.6.1
NADH-dependent enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/GPR174 | Probable G-protein coupled receptor 174 is a protein that in humans is encoded by the GPR174 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Na%2B-exporting%20ATPase | {{DISPLAYTITLE:Na+-exporting ATPase}}
In enzymology, a Na+-exporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + Na+ ADP + phosphate + Na+
The 3 substrates of this enzyme are ATP, H2O, and Na+, whereas its 3 products are ADP, phosphate, and Na+.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Na+-exporting).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Na%2B-transporting%20two-sector%20ATPase | {{DISPLAYTITLE:Na+-transporting two-sector ATPase}}
In enzymology, a Na+-transporting two-sector ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (Na+-transporting).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/GPR128 | G protein-coupled receptor 128 is a protein encoded by the ADGRG7 gene. GPR128 is a member of the adhesion GPCR family.
Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
GPR128 is specifically expressed in human liver as well as in mouse bone marrow and intestinal tissues.
Function
Ni et al. showed that Gpr128 deletion in mice causes reduced body weight and induced intestinal contraction frequency.
Clinical significance
A 111-kb copy number gain with breakpoints within the TRK-fused gene (a target of translocations in lymphoma and thyroid tumors) and GPR128 has been identified in the genome of patients with atypical myeloproliferative neoplasms. Notably, the fused gene was also detected in few healthy individuals.
References
External links
Adhesion GPCR consortium
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Nickel-transporting%20ATPase | In enzymology, a nickel-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + Ni2+out ADP + phosphate + Ni2+in
The 3 substrates of this enzyme are ATP, H2O, and Ni2+, whereas its 3 products are ADP, phosphate, and Ni2+.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (nickel-importing).
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.6.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/GNRHR2 | Putative gonadotropin-releasing hormone II receptor is a protein that in humans is encoded by the GNRHR2 gene.
Function
The receptor for gonadotropin releasing hormone 2 (GnRH2) is encoded by the GnRH2 receptor (GnRHR2) gene. In non-hominoid primates and non-mammalian vertebrates, GnRHR2 encodes a seven-transmembrane G protein-coupled receptor. However, in human, the N-terminus of the predicted protein contains a frameshift and premature stop codon. In human, GnRHR2 transcription occurs but whether the gene produces a functional C-terminal multi-transmembrane protein is currently unresolved. Alternative splice variants have been reported. An untranscribed pseudogene of GnRHR2 is also on chromosome 14.
See also
Gonadotropin-releasing hormone receptor
References
Further reading
External links
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR146 | Probable G-protein coupled receptor 146 is a protein that in humans is encoded by the GPR146 gene. It has been identified as a possible receptor for C-peptide.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Nitrate-transporting%20ATPase | In enzymology, a nitrate-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + nitrateout ADP + phosphate + nitratein
The 3 substrates of this enzyme are ATP, H2O, and nitrate, whereas its 3 products are ADP, phosphate, and nitrate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (nitrate-importing).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MRGPRD | Mas-related G-protein coupled receptor member D is a protein that in humans is encoded by the MRGPRD gene.
See also
MAS1 oncogene
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Nonpolar-amino-acid-transporting%20ATPase | In enzymology, a nonpolar-amino-acid-transporting ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O + nonpolar amino acidout ADP + phosphate + nonpolar amino acidin
The 3 substrates of this enzyme are ATP, H2O, and nonpolar amino acid, whereas its 3 products are ADP, phosphate, and nonpolar amino acid.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (nonpolar-amino-acid-transporting).
References
EC 3.6.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Microstaging | Microstaging is a technique used to help determine the stage (extent) of melanoma and certain squamous cell cancers. A sample of skin that contains tumor tissue is examined under a microscope to find out how thick the tumor is and/or how deeply the tumor has grown into the skin or connective tissues.
External links
Microstaging entry in the public domain NCI Dictionary of Cancer Terms
Cancer staging |
https://en.wikipedia.org/wiki/MRGPRE | Mas-related G-protein coupled receptor member E is a protein that in humans is encoded by the MRGPRE gene.
See also
MAS1 oncogene
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Nucleoplasmin%20ATPase | In enzymology, a nucleoplasmin ATPase () is an enzyme that catalyzes the chemical reaction
ATP + H2O ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to facilitate cellular and subcellular movement. The systematic name of this enzyme class is ATP phosphohydrolase (nucleosome-assembling).
References
EC 3.6.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/MRGPRX2 | Mas-related G-protein coupled receptor member X2 is a protein that in humans is encoded by the MRGPRX2 gene.
It is most abundant on cutaneous mast cells.
Agonists are gyrase inhibitors like ciprofloxacin and non-depolarizing neuromuscular blocking agents like atracurium as well as vancomycin. Activation of MRGPRX2 leads to mast cell degranulation with subsequent pseudo-allergic reactions.
See also
MAS1 oncogene
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Nucleoside-diphosphatase | In enzymology, a nucleoside-diphosphatase () is an enzyme that catalyzes the chemical reaction
a nucleoside diphosphate + H2O a nucleotide + phosphate
Thus, the two substrates of this enzyme are nucleoside diphosphate and H2O, whereas its two products are nucleotide and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is nucleoside-diphosphate phosphohydrolase. Other names in common use include thiamine pyrophosphatase, UDPase, inosine diphosphatase, adenosine diphosphatase, IDPase, ADPase, adenosinepyrophosphatase, guanosine diphosphatase, guanosine 5'-diphosphatase, inosine 5'-diphosphatase, uridine diphosphatase, uridine 5'-diphosphatase, nucleoside diphosphate phosphatase, type B nucleoside diphosphatase, GDPase, CDPase, nucleoside 5'-diphosphatase, type L nucleoside diphosphatase, NDPase, and nucleoside diphosphate phosphohydrolase. This enzyme participates in purine metabolism and pyrimidine metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
External links
EC 3.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nucleoside%20phosphoacylhydrolase | In enzymology, a nucleoside phosphoacylhydrolase () is an enzyme that catalyzes the chemical reaction
Hydrolyses mixed phospho-anhydride bonds
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is nucleoside-5'-phosphoacylate acylhydrolase.
References
EC 3.6.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Nucleoside-triphosphatase | In enzymology, a nucleoside-triphosphatase (NTPase) () is an enzyme that catalyzes the chemical reaction
NTP + H2O NDP + phosphate
Thus, the two substrates of this enzyme are NTP and H2O, whereas its two products are NDP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is unspecific diphosphate phosphohydrolase. Other names in common use include nucleoside triphosphate phosphohydrolase, nucleoside-5-triphosphate phosphohydrolase, and nucleoside 5-triphosphatase. This enzyme participates in purine metabolism and thiamine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/GPR62 | Probable G-protein coupled receptor 62 is a protein that in humans is encoded by the GPR62 gene.
G protein–coupled receptors (GPCRs, or GPRs) contain 7 transmembrane domains and transduce extracellular signals through heterotrimeric G proteins.[supplied by OMIM]
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/Nucleoside-triphosphate%20diphosphatase | In enzymology, a nucleoside-triphosphate diphosphatase () is an enzyme that catalyzes the chemical reaction
a nucleoside triphosphate + H2O a nucleotide + diphosphate
Thus, the two substrates of this enzyme are nucleoside triphosphate and H2O, whereas its two products are nucleotide and diphosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is nucleoside-triphosphate diphosphohydrolase. This enzyme is also called nucleoside-triphosphate pyrophosphatase. This enzyme participates in purine metabolism and pyrimidine metabolism.
For example, enzyme deoxyribonucleoside triphosphate pyrophosphatase, encoded by YJR069C in S. cerevisiae and exhibiting (d)ITPase and (d)XTPase activities, hydrolyses ITP, dITP, XTP and dXTP releasing pyrophosphate and IMP, dIMP, XMP and dXMP, respectively.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .
References
EC 3.6.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Anchor%20cell | The anchor cell is a cell in nematodes such as Caenorhabditis elegans. It is important in the development of the reproductive system, as it is required for the production of the tube of cells that allows embryos to pass from the uterus through the vulva to the outside of the worm.
During the development of C. elegans hermaphrodites, the anchor cell produces a signalling molecule (LIN-3/EGF) that induces nearby epidermal cells to develop into the vulva. The anchor cell also produces another signal (the Notch ligand LAG-2) that induces adjacent uterine cells to become the π cells, some of which will later connect the uterus to the vulva. The anchor cell next removes the basement membrane that separates the uterus and vulva and invades, initiating the connection between the uterus and the vulva. Finally the anchor cell fuses with eight of the π cells to form the uterine seam cell.
References
External links
Anchor cell page at Wormbase – part of the anatomy ontology of C. elegans.
Nematode anatomy |
https://en.wikipedia.org/wiki/Chris%20Lattner | Christopher Arthur Lattner (born 1978) is an American computer scientist, former Google and Tesla employee and co-founder of LLVM, Clang compiler, MLIR compiler infrastructure and the Swift programming language. , he is the co-founder and CEO of Modular Inc, an artificial intelligence platform for developers. Before founding Modular AI, he worked as the President of Platform Engineering, SiFive after two years at Google Brain. Prior to that, he briefly served as Vice President of Autopilot Software at Tesla, Inc. and worked at Apple Inc. as Senior Director of the Developer Tools department, leading the Xcode, Instruments, and compiler teams.
Education
Lattner studied computer science at the University of Portland, graduating in with a Bachelor of Science degree in 2000. While in Oregon, he worked as an operating system developer, enhancing Sequent Computer Systems's DYNIX/ptx. He moved to the University of Illinois at Urbana-Champaign where he was awarded a Master of Science degree in 2002, followed by a PhD in 2005 for research on optimizing pointer-intensive programs, supervised by Vikram Adve.
Career
Lattner is the current CEO of Modular AI, a company that is building a next-generation Artificial Intelligence (AI) developer platform. Previously he has worked at SiFive, Google, Tesla, Inc. and Apple Inc.
SiFive
Lattner joined SiFive in January 2020 and the board changed to ("SiFive 2.0"), Lattner led the RISC-V Product and Engineering organizations (everything excluding |
https://en.wikipedia.org/wiki/Eleidin | Eleidin is clear intracellular protein which is present in the stratum lucidum of the skin.
Eleidin is a transformation product of the amino acid complex keratohyalin, the lifeless matter deposited in the form of minute granules within the protoplasm of living cells. Eleidin is then converted to keratin in the stratum corneum.
Eleidin can be found in the vermilion border of the lip. The lip is thinly keratinized and has a high concentration of eleidin. The red appearance of the vermillion border is due to several factors, one of which is the transparent nature of eleidin showing the color of the red blood cells beneath.
References
Human proteins |
https://en.wikipedia.org/wiki/Steiner%E2%80%93Lehmus%20theorem | The Steiner–Lehmus theorem, a theorem in elementary geometry, was formulated by C. L. Lehmus and subsequently proved by Jakob Steiner. It states:
Every triangle with two angle bisectors of equal lengths is isosceles.
The theorem was first mentioned in 1840 in a letter by C. L. Lehmus to C. Sturm, in which he asked for a purely geometric proof. Sturm passed the request on to other mathematicians and Steiner was among the first to provide a solution. The theorem became a rather popular topic in elementary geometry ever since with a somewhat regular publication of articles on it.
Direct proofs
The Steiner–Lehmus theorem can be proved using elementary geometry by proving the contrapositive statement: if a triangle is not isosceles, then it does not have two angle bisectors of equal length.
There is some controversy over whether a "direct" proof is possible;
allegedly "direct" proofs have been published, but not everyone agrees that these proofs are "direct."
For example, there exist simple algebraic expressions for angle bisectors in terms of the sides of the triangle. Equating two of these expressions and algebraically manipulating the equation results in a product of two factors which equal 0, but only one of them (a − b) can equal 0 and the other must be positive. Thus a = b. But this may not be considered direct as one must first argue about why the other factor cannot be 0.
John Conway
has argued that there can be no "equality-chasing" proof because the theorem (stated |
https://en.wikipedia.org/wiki/Erquitaia | Erquitaia is a poorly known genus of prehistoric galeomorph shark whose fossils are found in rocks dating from the Maastrichtian stage.
Classification
Originally, Erquitaia was thought to be a ray placed in the order Rajiformes, however it was subsequently moved to the shark super order Galeomorphii, which includes all modern sharks except the dogfish and their relatives.
See also
Flora and fauna of the Maastrichtian stage
List of prehistoric cartilaginous fish (Chondrichthyes)
Cretaceous sharks
Prehistoric cartilaginous fish genera |
https://en.wikipedia.org/wiki/Extrachromosomal%20array | An extrachromosomal array is a method for mosaic analysis in genetics. It is a cosmid, and contains two functioning (wild-type) closely linked genes: a gene of interest and a mosaic marker. Such an array is injected into germ line cells, which already contain mutant (specifically, loss of function) alleles of all three genes in their chromosomal DNA. The cosmid, which is not packed correctly during mitosis, is occasionally present in only one daughter cell following cell division. The daughter cell containing the array expresses the gene of interest; the cell lacking the array does not.
The mosaic marker is a gene which exhibits a visible phenotype change between the functioning and non-functioning alleles. For example, ncl-1, located in chromosomal DNA, exhibits a larger nucleolus than the wild-type allele, which is in the array. Thus, cells which exhibit larger nucleoli have usually not retained the extrachromosomal array.
The gene of interest is the target of the mosaic analysis. Cells lacking the extrachromosomal array also lack the functional gene of interest. Cells which develop normally without the array do not require the gene of interest for normal function. Cells which do not develop normally are said to require the gene. In this way, those cell lineages which require a specific gene can be identified.
Extrachromosomal arrays replace an earlier technique involving a duplicated piece of chromosome called a free duplication. The latter technique required that the g |
https://en.wikipedia.org/wiki/Prokineticin%20receptor%202 | Prokineticin receptor 2 (PKR2), is a dimeric G protein-coupled receptor encoded by the PROKR2 gene in humans.
Function
Prokineticins are secreted proteins that can promote angiogenesis and induce strong gastrointestinal smooth muscle contraction. The protein encoded by this gene is an integral membrane protein and G protein-coupled receptor for prokineticins. PKR2 is composed of 384 amino acids. Asparagine residues at position 7 and 27 undergo N-linked glycosylation. Cysteine residues at position 128 and 208 form a disulfide bond. The encoded protein is similar in sequence to GPR73, another G protein-coupled receptor for prokineticins. PKR2 is also linked to mammalian circadian rhythm. Levels of PKR2 mRNA fluctuate in the suprachiasmatic nucleus, increasing during the day and decreasing at night.
Mutations in the PROKR2 (also known as KAL3) gene have been implicated in hypogonadotropic hypogonadism and gynecomastia. Total loss of PKR2 in mice leads to spontaneous torpor usually beginning at dusk and lasting for 8 hours on average.
PKR2 functions as a G protein-coupled receptor, thus it has a signaling cascade when it's ligand binds. PKR2 is a Gq-coupled protein, so when the ligand binds, beta-type phospholipase C is activated which creates inositol triphosphate. This then triggers calcium release inside the cell.
See also
Prokineticin receptor
Kallmann syndrome
References
Further reading
External links
GeneReviews/NCBI/NIH/UW entry on Kallmann syndrome
G p |
https://en.wikipedia.org/wiki/GPR112 | G protein-coupled receptor 112 is a protein encoded by the ADGRG4 gene. GPR112 is a member of the adhesion GPCR family.
Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
GPR112 is expressed in human enterochromaffin cells and in the mouse intestine. The N-terminal fragment (NTF) of GPR112 contains pentraxin (PTX)-like modules. GPR112 gene expression has been identified as a marker for neuroendocrine carcinoma cells.
References
External links
Adhesion GPCR consortium
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR119 | G protein-coupled receptor 119 also known as GPR119 is a G protein-coupled receptor that in humans is encoded by the GPR119 gene.
GPR119, along with GPR55 and GPR18, have been implicated as novel cannabinoid receptors.
Pharmacology
GPR119 is expressed predominantly in the pancreas and gastrointestinal tract in rodents and humans, as well as in the brain in rodents. Activation of the receptor has been shown to cause a reduction in food intake and body weight gain in rats. GPR119 has also been shown to regulate incretin and insulin hormone secretion. As a result, new drugs acting on the receptor have been suggested as novel treatments for obesity and diabetes.
Ligands
A number of endogenous, synthetic and plant derived ligands for this receptor have been identified:
2-Oleoylglycerol (2OG)
Anandamide
AR-231,453
MBX-2982
Oleoylethanolamide (OEA) (Endogenous Ligand)
PSN-375,963
PSN-632,408
Human microbiota and GPR119 activation
Commensal bacteria are found to have important roles in human health, as bacterial metabolites are likely to be key components of host interactions by which they affect mammalian physiology. N-acyl amide synthase genes are found enriched in gastrointestinal bacteria and the lipids, that they encode, interact with GPCRs, which regulate gastrointestinal tract physiology, where cell-based models have demonstrated, that commensal GPR119 agonists regulate metabolic hormones and glucose homeostasis as efficiently as human ligands, and the cleare |
https://en.wikipedia.org/wiki/GPR155 | Integral membrane protein GPR155, also known as G protein-coupled receptor 155, is a protein that in humans is encoded by the GPR155 gene. Mutations in this gene may be associated with autism.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR113 | GPR113 is a gene that encodes the Probable G-protein coupled receptor 113 protein.
Gene
The Homo sapiens GPR113 gene is located on chromosome 2 (2p23.3). This gene spans the length of a 38.65kb region from base 26531041 to 26569685 on the negative strand. The GPR113 gene has two neighbors on either side on the negative strand: OTOF otoferlin preceding and HADHA hydroxyacyl-CoA following. Directly opposite the GPR113 on the positive strand is the EPT1 gene.
The GPR113 gene is also known by the aliases PGR23 and HGPCR37.
Homology & Evolution
The GPR113 has 5 human paralogs GPR110, GPR115, GPR128, GPR111, and GPR116. GPR113 is well conserved in mammals from primates to semi-aquatic species, as well as some amphibians. These include the Common Chimpanzee, the African Bush Elephant, the Platypus, and the Western Clawed Frog. Homologous domains that are well conserved throughout orthologs center in the 7 transmembrane receptor (Secretin family) region highlighted in purple in the figure.
Protein
The protein product of GPR113 gene is a G-protein coupled receptor. The protein has three transcript variants in humans. Of these three, GPR113 Variant 1 has the longest amino acid sequence, and has the highest identity to orthologs. This leads to the conclusion that GPR113 Variant 1 is the homo sapiens descendant of the ancestral GPR113 gene. GPR113 Var 1 contains 1079 Amino Acids, and is integral to the plasma membrane. The 7-pass receptor contains 4 domains highlighted in the figure |
https://en.wikipedia.org/wiki/GPR156 | GPR156 (G protein-coupled receptor 156), is a human gene which encodes a G protein-coupled receptor belonging to metabotropic glutamate receptor subfamily. By sequence homology, this gene was proposed as being a possible GABAB receptor subunit, however when expressed in cells alone or with other GABAB subunits, no response to GABAB ligands could be detected. Therefore, the function of this protein remains to be elucidated. In vitro studies on GPR156 constitutive activity revealed a high level of basal activation and coupling with members of the Gi/Go heterotrimeric G protein family.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR125 | Adhesion G-protein coupled receptor A3 (ADGRA3), also known as GPR125, is an adhesion GPCR that in humans is encoded by the Adgra3 gene (previously Gpr125).
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/C.%20L.%20Lehmus | Daniel Christian Ludolph Lehmus (July 3, 1780 in Soest – January 18, 1863 in Berlin) was a German mathematician, who today is best remembered for the Steiner–Lehmus theorem, that was named after him.
Lehmus was the grandson of the German poet Johann Adam Lehmus (1707-1788) and the Berlin-based physician Emilie Lehmus (1841-1932) was his grandniece. His father Christian Balthasar Lehmus was a science teacher and director of a gymnasium in Soest, as such he took it upon himself to school his son. From 1799 to 1802 Lehmus studied at universities of Erlangen and Jena. In 1803 he went to Berlin, where he was giving private lectures in mathematics and pursued further studies at the university, which awarded him a PhD in 1811. From December 18, 1813 to Easter 1815 Lehmus was employed as a lecturer (Privatdozent) by the university, but in 1814 he became a teacher for math and science at the Hauptbergwerks-Eleven-Institut (mining school) in Berlin as well. In 1826 he also assumed a teaching position at the Königlichen Artillerie- und Ingenieurschule (military engineering school) and was granted the title of a professor at that school in 1827. In 1836 he was awarded the Order of the Red Eagle (4th class). In addition to his two teaching positions Lehmus was giving lectures at the university until 1837 as well.
Lehmus wrote a number of math and science textbooks, best known was probably his Lehrbuch der Geometrie, which saw several editions. He published articles in various math jour |
https://en.wikipedia.org/wiki/GPR114 | G protein-coupled receptor 114 is a protein encoded by the ADGRG5 gene. GPR114 is a member of the adhesion GPCR family.
Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
GPR114 mRNA is specifically expressed in human eosinophils as well as in mouse lymphocytes, monocytes, macrophage, and dendritic cells.
Signaling
The cyclic adenosine monophosphate (cAMP) assay in overexpressing HEK293 cells has demonstrated coupling of GPR114 to Gαs protein.
References
External links
Adhesion GPCR consortium
G protein-coupled receptors |
https://en.wikipedia.org/wiki/OPN5 | Opsin-5, also known as G-protein coupled receptor 136 or neuropsin is a protein that in humans is encoded by the OPN5 gene. Opsin-5 is a member of the opsin subfamily of the G protein-coupled receptors. It is a photoreceptor protein sensitive to ultraviolet (UV) light. The OPN5 gene was discovered in mouse and human genomes and its mRNA expression was also found in neural tissues. Neuropsin is bistable at 0 °C and activates a UV-sensitive, heterotrimeric G protein Gi-mediated pathway in mammalian and avian tissues.
Function
Human neuropsin is expressed in the eye, brain, testes, and spinal cord. Neuropsin belongs to the seven-exon subfamily of mammalian opsin genes that includes peropsin (RRH) and retinal G protein coupled receptor (RGR). Neuropsin has different isoforms created by alternative splicing.
Photochemistry
When reconstituted with 11-cis-retinal, mouse and human neuropsins absorb maximally at 380 nm. When illuminated these neuropsins are converted into blue-absorbing photoproducts (470 nm), which are stable in the dark. The photoproducts are converted back to the UV-absorbing form, when they are illuminated with orange light (> 520 nm).
Species distribution
Neuropsins are known from echinoderms, annelids, arthropods, brachiopods, tardigrades, mollusks, and most are known from craniates. The craniates are the taxon that contains mammals and with them humans. However, neuropsin orthologs have only been experimentally verified in a small number of animals, amo |
https://en.wikipedia.org/wiki/GPR115 | Probable G-protein coupled receptor 115 is a protein that in humans is encoded by the GPR115 gene.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR116 | Probable G-protein coupled receptor 116 is a protein that in humans is encoded by the GPR116 gene. GPR116 has now been shown to play an essential role in the regulation of lung surfactant homeostasis.
References
Further reading
G protein-coupled receptors |
https://en.wikipedia.org/wiki/GPR97 | G-protein coupled receptor 97 also known as adhesion G protein-coupled receptor G3 (ADGRG3) is a protein that in humans is encoded by the ADGRG3 gene. GPR97 is a member of the adhesion GPCR family.
Adhesion GPCRs are characterized by an extended extracellular region often possessing N-terminal protein modules that is linked to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.
GPR97 is expressed in human granulocytes and endothelial cells of the vasculature as well as in mouse granulocytes, monocytes, macrophages, and dendritic cells.
Signaling
The inositol phosphate (IP3) accumulation, aequorin, and 35S isotope binding assays in overexpressing HEK293 cells have demonstrated coupling of GPR97 to Gαo protein triggering cyclic adenosine monophosphate (cAMP). GPR97 actives cAMP response element-binding protein (CREB), NF-κB, and small GTPases to regulate cellular functions.
Function
Systemic steroid exposure is a therapy to treat a variety of medical conditions and is associated with epigenetic processes such as DNA methylation that may reflect pharmacological responses and/or side effects. GPR97 was found to be differently methylated at CpG sites in the genome of blood cells from patient under systemic steroid treatment. GPR97 is transcribed in immune cells. Gene-deficient mice revealed that Gpr97 is crucial for maintaining B-cell population via constitutive CREB and NF-κB activities. Human lymphatic endothelial cells (LECs) abundantly expr |
https://en.wikipedia.org/wiki/GPR111 | Probable G-protein coupled receptor 111 is a protein that in humans is encoded by the GPR111 gene.
References
Further reading
G protein-coupled receptors |
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