Translocates drugs and phospholipids across the membrane (PubMed:8898203, PubMed:2897240, PubMed:9038218, PubMed:35970996). Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins (PubMed:8898203). Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells (PubMed:2897240, PubMed:9038218, PubMed:35970996).
Phosphoglucomutase-2 (PGM2) is a member of PGM family, which catalyzes the inter-conversion of sugar phosphates and participates in anabolic and catabolic reactions. When cells are grown in glucose, PGM catalyzes the conversion of glucose-6-phosphate to glucose-1-phosphate an important precursor required for the synthesis of UDP glucose and trehalose. PGM2 catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses, and it may also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. But this protein has low glucose 1,6-bisphosphate synthase activity.
Immunoglobulin Superfamily Member 8 (IGSF8) is a single-pass membrane protein. IGSF8 contains four Ig-like C2 type domains. The Ig-like C2-type domains 3 and 4 are required for interactions with CD81. IGSF8 may regulate proliferation and differentiation of keratinocytes. IGSF8 may participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain. It also may play a role on integrin-dependent morphology and motility functions.
Pleckstrin Homology-Like Domain Family A Member 2 (PHLDA2) is a peripheral membrane protein that belongs to the PHLDA2 family. PHLDA2 is expressed in the placenta and adult prostate gland. In the placenta, it is present in all cells of the villous cytotrophoblast. PHLDA2 plays a role in regulating placenta growth. PHLDA2 may act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids.
Phosphomevalonate kinase (PMVK) is a cytosolic enzyme. PMVK can be highly expressed in the heart,skeletal muscle, liver, pancreas, and kidney; it is expressed at lower levels in the brain, lung, and placenta. Induced by sterol, PMVK takes part in isopentenyl diphosphate biosynthesis through the mevalonate pathway. PMVK catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate in the fifth reaction of the cholesterol biosynthetic pathway.
PHPT1, also known as 14 kDa phosphohistidine phosphatase, phosphohistidine phosphatase 1, protein janus-A homolog, PHP14, is a cytoplasm protein which belongs to thejanus family. PHPT1 / PHP14 is expressed abundantly in heart and skeletal muscle. Phosphatases are a diverse group of enzymes that regulate numerous cellular processes. Much of what is known relates to the tyrosine, threonine, and serine phosphatases, whereas the histidine phosphatases have not been studied as much. Protein histidine phosphorylation exists widely in vertebrates, and it plays important roles in signal transduction and other cellular functions. Protein histidine phosphorylation accounts for about 6% of the total protein phosphorylation in eukaryotic cells. The knowledge about eukaryotic PHPT (protein histidine phosphatase) is still very limited. To date, only one vertebrate PHPT has been discovered, and two crystal structures of human PHPT1 have been solved. PHPT1 / PHP14 can dephosphorylate a variety of proteins (e.g. ATP-citrate lyase and the beta-subunit of G proteins). A putative active site has been identified by its electrostatic character, ion binding, and conserved protein residues.
PHYH belongs to the family of iron(II)-dependent oxygenases, which typically incorporate one atom of dioxygen into the substrate and one atom into the succinate carboxylate group. PHYH is expressed in liver, kidney, and T-cells, but not in spleen, brain, heart, lung and skeletal muscle. It converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA. Defects in PHYH can cause Refsum disease (RD). RD is an autosomal recessive disorder characterized clinically by a tetrad of abnormalities: retinitis pigmentosa, peripheral neuropathy, cerebellar ataxia, and elevated protein levels in the cerebrospinal fluid (CSF). Patients exhibit accumulation of the branched-chain fatty acid, phytanic acid, in blood and tissues.
Elafin is a secreted protein. Elafin consists of two domains: the transglutaminase substrate domain (cementoin moiety) and the elastase inhibitor domain. The transglutaminase substrate domain serves as an anchor to localize Elafin covalently to specific sites on extracellular matrix proteins. It is shown that Elafin can be used as a biomarker for graft versus host disease of the skin. Elafin is expressed in the skin during wound healing through activation of the epidermal growth factor receptor. Elafin may prevent elastase-mediated tissue proteolysis.
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