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Chitotriosidase-1 (CHIT1) is a glycoprotein that belongs to the Glycosyl Hydrolase 18 family and Chitinase class II subfamily. It is secreted by cultured macrophages and serves to degrade chitin, chitotriose and chitobiose. CHIT1 may participate in the defense against nematodes and other pathogens. It is highly expressed in the plasma of patients with Gaucher's disease type I, which can be used as diagnostic aid and to evaluate the success of treatment that brings levels back to normal. The amino acid sequence of human CHIT1 is 99%, 76%, 75% and 55% identical to that of chimpansee, rat, mouse and fruit fly, respectively.

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Carbonic Anhydrase-Related Protein 10 (CA10) belongs to the Carbonic Anhydrase family of Zinc Metalloenzymes. It is an acatalytic member of the alpha-carbonic anhydrase subgroup. CA10 expression is detected in the adult total brain and almost all parts of the central nervous system, but not in the fetal brain. CA10 catalyse the reversible hydration of carbon dioxide in various biological processes, which is fundamental to many processes such as respiration, renal tubular acidification and bone resorption. It is thought to play a role in the central nervous system, especially in brain development.

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Chitinase-3-Like Protein 1 (CHI3L1) belongs to the glycosyl hydrolase 18 family. CHI3L1 is expressed in activated macrophages, articular chondrocytes, synovial cells as well as in liver. It lacks chitinase activity and is secreted by activated macrophages, chondrocytes, neutrophils and synovial cells. CHI3L1 is thought to play a role in defense against pathogens, or in tissue remodeling, and in the capacity of cells to respond to and cope with changes in their environment. In addition, CHI3L1 is associated with susceptibility to asthma-related traits type 7 (ASRT7) which assessed by methacholine challenge test, serum IgE levels, atopy, and atopic dermatitis.

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Dipeptidyl peptidase 3(DPP3), is a member of the S9B family in clan SC of the serine proteases. DPP3 has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH). It releases an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity and also acts on dipeptidyl 2-naphthylamides.Increased activity of this protein has a relationship with endometrial and ovarian cancers.

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Chymotrypsin-Like Protease CTRL-1 is a protease that belongs to the peptidase S1 family. Human CTRL-1 is synthesised as a 264 amino acid (aa) precursor that contains an 18 aa signal sequence, 15 aa activation peptide and a 231 aa mature chain. CTRL-1 Contains 1 peptidase S1 domain. It has many molecular functions, such as hydrolase, protease, and serine protease. CTRL-1 plays a role in digest and hydrolyse proteins in biological process.

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Carbonic Anhydrase 7 (CA7) is a member of the alpha-carbonic anhydrase family. Alpha-carbonic anhydrase is a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. Furthermore, Alpha-carbonic anhydrase is associated with many biological processes, including calcification, respiration, bone resorption, acid-base balance and the formation of aqueous humor. CA7 is activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine, but it is inhibited coumarins, sulfonamide derivatives such as acetazolamide (AZA) by saccharin and Foscarnet.

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Hyaluronidase-1 (HYAL1) is a secreted lysosomal hyaluronidase that belongs to the glycosyl hydrolase 56 family. HYAL1 contains one EGF-like domain and is highly expressed in the liver, kidney, and heart, but it is weakly expressed in the lung, placenta, and skeletal muscle. HYAL1 is thought to be involved in cell proliferation, migration, and differentiation. It may play a role in promoting tumor progression and blocking the TGFB1-enhanced cell growth. Mutations in HYAL1 are associated with mucopolysaccharidosis type IX, or hyaluronidase deficiency.

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Fructose-1,6-Bisphosphatase 1 (FBPase 1) is a member of the FBPase class 1 family. FBPase 1 is a gluconeogenesis regulatory protein, which catalyses the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBPase 1 can assume an active R-state, or an inactive T-state. FBPase 1 deficiency is inherited as an autosomal recessive disorder mainly in the liver and causes life-threatening episodes of hypoglycemia and metabolic acidosis in newborn infants or young children. FBPase 1 coupled with phosphofructokinase (PFK) is involved in the metabolism of pancreatic islet cells.

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Pyruvate Kinase Isozymes R/L (PKLR) belongs to the pyruvate kinase family, There are 4 isozymes of pyruvate kinase in mammals: L, R, M1 and M2. L type is major isozyme in the liver; R is found in red cells; M1 is the main form in muscle, heart and brain; M2 is found in early fetal tissues. PKLR exists as a homotetramer and catalyses the production of phosphoenolpyruvate from pyruvate and ATP. Defects in PKLR are also the cause of pyruvate kinase deficiency of red cells, which is a frequent cause of hereditary non-spherocytic hemolytic anemia.

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Polypeptide N-acetylgalactosaminyltransferase 3(GALNT3) belongs to the glycosyltransferase 2 family and galNAc-T subfamily. It expressed in organs that contain secretory epithelial glands and it highly expressed in pancreas, skin, kidney and testis. There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding .This protein plays a major role in regulating phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults.

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Human Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 (B3GAT3) is an enzyme that in humans is encoded by the B3GAT3 gene, belongs to the glycosyltransferase 43 family. B3GAT3 is involved in a number of biological processes such as catalyzing the formation of the glycosaminoglycan-protein linkage by way of a glucuronyl transfer reaction in the final step of the biosynthesis of the linkage region of proteoglycans, forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate, gGlycosaminoglycans biosynthesis, transfering a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans.It also plays a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins , hows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc and stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation.

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X-Prolyl Aminopeptidase (XPNPEP1) is a proline-specific metalloaminopeptidase that specifically catalyses the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-Prolyl Aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases. X-Prolyl Aminopeptidase is a member of the M24 family of metalloproteases, which also contains methionine aminopeptidases, X-Pro dipeptidase, aminopeptidase P2, aminopeptidase P homolog, proliferation-associated protein 1, and suppressor of Ty homolog or chromatin-specific transcription elongation factor large subunit. It is a soluble enzyme, in contrast to the GPI-anchored Aminopeptidase P2 encoded by XPNPEP2. Deficiency of X-Prolyl Aminopeptidase results in excretion of large amounts of imino-oligopeptides in urine. Human Aminopeptidase P1 is widely expressed. The amino acid sequence of human X-Prolyl Aminopeptidase is 99%, 97%, 95%, 74% and 73% identical to that of canine, bovine, mouse/rat, Xenopus and zebrafish, respectively.

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Peptidyl-Prolyl Cis-Trans Isomerase FKBP7 (FKBP7) is a member of the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. FKBP7 contains two EF-hand domains and one PPIase FKBP-type domain. FKBP7 exhibits PPIase activity and function as molecular chaperones. In addition, FKBP7 accelerates the folding of proteins during protein synthesis. It has been shown that Hsp90 complex to the nucleus bind its PPIase domain to cytoplasmic dynein, the motor protein responsible for retrograde movement along microtubules.

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Carbonic Anhydrase 14 (CA14) belongs to the Alpha-Carbonic Anhydrase family. It is highly expressed in all parts of the central nervous system and lowly expressed in adult liver, heart, small intestine, colon, kidney, urinary bladder, and skeletal muscle. CA14 along with other Carbonic Anhydrases (CAs) participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA14 is predicted to be a type I membrane protein and catalyses the reversible hydration of carbon dioxide.

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Acid sphingomyelinase-like phosphodiesterase 3a (SMPDL3A ) is a novel liver X receptor (LXR) -regulated gene, with an LXR response element within its promoter. The induction of SMPDL3A is LXR-dependent and is restricted to human blood cells with no induction observed in mouse cellular systems. LXR function as physiological sensors of cholesterol metabolites (oxysterols), regulating key genes involved in cholesterol and lipid metabolism. LXRs have been extensively studied in both human and rodent cell systems, revealing their potential therapeutic value in the contexts of atherosclerosis and inflammatory diseases.

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Sorbitol dehydrogenase, also known as L-iditol 2-dehydrogenase and SORD, is a member of the zinc-containing alcohol dehydrogenase family. SORD exsits in a homotetramer and binds one zinc ion per subunit. SORD is expressed in kidney and epithelial cells of both benign and malignant prostate tissue. SORD can converts sorbitol to fructose and catalyses the interconversion of polyols and their corresponding ketoses, and together with aldose reductase to make up the sorbitol pathway. SORD is up-regulated by androgens and down-regulated by castration. SORD may play a role in the sperm motility by providing an energetic source for sperm.

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NAD kinase catalyses the transfer of a phosphate group from ATP to NAD+ to generate NADP+, which in its reduced form acts as an electron donor for biosynthetic reactions. NADP+ is an essential coenzyme in metabolism and provides reducing power to biosynthetic processes such as fatty acid biosynthesis. NAD kinase from Bacillus subtilis is not ATP-dependent but has a broader substrate specificity than human NAD kinase. It can economically produce NADP+ by using other nucleoside triphosphates as well as inorganic polyphosphate as a source of phosphorus. Catalytic activity: ATP + NAD+ = ADP + NADP+.

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Sentrin-Specific Protease 7 (SENP7) acts as a SUMO-2/3-specific protease. SENP7 is likely to regulate the metabolism of poly-SUMO-2/3 rather than SUMO-1 conjugation in vivo. SENP7 has a restricted substrate specificity, and displaying paralogue-specific isopeptidase activity. The C-terminal catalytic domain of SENP7 depolymerised poly-SUMO-2 chains but does not have activity against poly-SUMO-1 chains. SENP7 also had isopeptidase activity against di-SUMO-2- and SUMO-2-modified RanGAP1 (Ran GTPase-activating protein 1) but had limited activity against SUMO-1-modified RanGAP1.

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Glycine N-Methyltransferase (GNMT) is a tetrameric cytosolic protein. GNMT catalyses the synthesis of N-methylglycine from glycine using S-adenosylmethionine (AdoMet) as the methyl donor. It can affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine, playing an important role in maintaining normal AdoMet levels. GNMT is highly expressed in liver. As a major folate-binding protein, GNMT takes part in the detoxification pathway. Defects in GNMT are the cause of hypermethioninemia. the patients with this deficiency are mild hepatomegaly and chronic elevation of serum transaminases.

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PGK1 is called phosphoglycerate kinase that involved in a critical energy-producing process known as glycolysis. Phosphoglycerate kinase helps carry out a chemical reaction that converts a molecule called 1,3-diphosphoglycerate, which is produced during the breakdown of glucose, to another molecule called 3-phosphoglycerate during glycolysis. PGK1 The encoded protein may also act as a cofactor for polymerase alpha.. The protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions.

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Carbonic Anhydrase X (CA10) belongs to CA family of zinc metalloenzymes, which catalyze the reversible hydration of carbon dioxide in various biological processes such as respiration, renal tubular acidification and bone resorption. While CA10 is a secreted protein without Carbonic Anhydrase activity (i.e., the reversible hydration of CO2) due to point mutations in the zinc binding site, it has esterase activity. The human and mouse CA10 are expressed in the brain, indicating that they may play a role in brain development.

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Carbonic Anhydrase-Related Protein 11 (CA11) is a secreted protein member of the alpha-carbonic anhydrase family. Carbonic Anhydrases (CAs) are a large family of zinc metalloenzymes that catalyse the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA11 is expressed abundantly in the brain with moderate expression also present in spinal cord and thyroid. CA11 may play a general role in the central nervous system.

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Carbonic Anhydrase 3 (CA3) belongs to the Alpha-Carbonic Anhydrase family that encodes carbonic anhydrase isozymes. These carbonic anhydrases are a class of metalloenzymes that catalyse the reversible hydration of carbon dioxide and are differentially expressed in a number of cell types. The expression of the CA3 gene is strictly tissue specific and it is present at high levels in skeletal muscle with much lower levels found in cardiac and smooth muscle. CA3 is activated by proton donors such as imidazole and the dipeptide histidylhistidine. CA3 is inhibited by coumarins and sulfonamide derivatives such as acetazolamide.

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Isopentenyl Pyrophosphate Isomerase 2 (IDI2) belongs to the IPP isomerase type 1 family. Both isozymes, IDI1 and IDI2 are localised to the peroxisome by a PTS1-dependent pathway. IDI2 is expressed in skeletal muscle, which contains one nudix hydrolase domain. IDI2 binds one magnesium per subunit. IDI2 catalyses the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). It is reported that IDI2 is regulated independently from IDI1, by a mechanism that may involve PPAR- alpha.

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Calcium/Calmodulin-Dependent Protein Kinase Type 1 (CAMK1) belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family, and CaMK subfamily. CAMK1 contains one protein kinase domain and widely expressed. CAMK1 is phosphorylated by CaMKK1 and CaMKK2 on Thr-177. CAMK1 regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organisation, and neurite outgrowth. CAMK1 plays a role in K+ and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex.

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Carboxypeptidase A4 (CPA4) is a member of the peptidase M14 family. CPA4 is metalloprotease that could be involved in the histone hyperacetylation pathway. CPA4 binds one zinc ion per subunit and could catalyse to release of a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val.They have distinct expression patterns and different specificities for example, preferentially cleaving aromatic (carboxypeptidase As) or basic (carboxypeptidase Bs) residues. Several, such as carboxypeptidase Xs, have lost their catalytic activity. Carboxypeptidases play important roles in digestion of food, processing of bioactive peptides and blood coagulation.

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Thimet Oligopeptidase (THOP1) belongs to the peptidase M3 family which includes neurolysin and mitochondrial intermediate peptidase. THOP1 is located in Cytoplasm. THOP1 is widely expressed in human tissues and can detected in different subcellular locations. THOP1 is preferential cleavage for bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues. THOP1 is involved in the metabolism of neuropeptides under 20 amino acid residues and degradation of cytoplasmic peptide. In addition, THOP1 also can degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.

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Carbonic Anhydrase 8 (CA8) belongs to the alpha-carbonic anhydrase family. Alpha-carbonic anhydrase is a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. Because CA8 has some sequence similarity with other known carbonic anhydrase genes, it was firstly called as CA-related protein. Nevertheless, CA8 does not have a carbonic anhydrase catalytic activity. Defects in CA8 are the cause of cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3), which is a congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mild mental retardation.

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Inositol Monophosphatase 1 (IMPA1) belongs to the inositol monophosphatase family. IMPA1 is responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides, IMPA1 can use myo-inositol-1,3-diphosphate, myo-inositol-1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2-AMP as substrates. IMPA1 has been implicated as the pharmacological target for lithium action in brain. IMPA1 shows magnesium-dependent phosphatase activity and is inhibited by therapeutic concentrations of lithium. In addition, IMPA1 plays a improtant role in intracellular signal transduction.

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Flap Endonuclease 1 (FEN1) is a member of the XPG/RAD2 endonuclease family. During DNA replication, FEN1 cleaves the 5'-overhanging flap structure and processes the 5' ends of Okazaki fragments for synthesis. FEN1 also exhibits RNase H activity by possessing 5'-3' exonuclease activity on gapped double-stranded or nicked DNA, FEN1 is involved in the long patch base excision repair (LP-BER) pathway, it can cleave within the apurinic/apyrimidinic (AP) site-terminated flap. FEN1 can prevent flaps from equilibrating into structures that lead to duplications and deletions. FEN1 is also involved in replication and repair of rDNA and in repairing mitochondrial DNA.