This gene encodes a member of the M17 metalloprotease family. The encoded protein is specifically expressed in the brain, is a homodimeric dipeptidase which was identified as human carnosinase. This gene contains trinucleotide (CTG) repeat length polymorphism in the coding region.
Cytosolic non-specific dipeptidase, also known as CNDP dipeptidase 2, Glutamate carboxypeptidase-like protein 1, Peptidase A, CNDP2 and CN2, is a cytoplasm protein which belongs to thepeptidase M2A family. CNDP2/CPGL is a cytosolic enzyme that can hydrolyze carnosine to yield l-histidine and beta-alanine. CNDP2/CPGL hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Itmay be play a role as tumor suppressor in hepatocellular carcinoma (HCC) cells. Isoform1 of CNDP2/CPGL is ubiquitously expressed with higher levels in kidney and liver (at protein level). Isoform2 of CNDP2/CPGL is expressed in fetal tissues, it is only expressed in adult liver and placental tissues. CNDP2/CPGL is highly expressed in the histaminergic neurons in the tuberomammillary nucleus, implying that it may supply histidine to histaminergic neurons for histamine synthesis.
Coagulation Factor II Protein (FII, F2 Protein or Prothrombin) is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss. Coagulation Factor II Protein (FII, F2 Protein) also plays a role in maintaining vascular integrity during development and postnatal life. Prothrombin/Coagulation Factor II is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin/Coagulation Factor II and factor Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin. Prothrombin/Coagulation Factor II is expressed by the liver and secreted in plasma. Defects in prothrombin/Coagulation Factor II are the cause of factor II deficiency (FA2D). It is very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels. Defects in Coagulation Factor II are also a cause of susceptibility to thrombosis. It is a multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation.
Tissue Factor (TF)/CD142 (Coagulation factor III/Thromboplastin) is a type-I transmembrane glycoprotein that serves as the cell surface receptor and cofactor for blood coagulation factors VII and VIIa, and thus plays a central role in hemostasis and thrombosis (1). The TF:VIIa receptor-ligand complex is widely recognized as the initiator of the extrinsic blood coagulation protease cascade, which ultimately leads to the generation of fibrin and thrombin. A member of the type-II cytokine receptor superfamily, TF has also been shown to engage the PI3K and MAPK signaling cascades upon binding to factor VIIa in order to drive cellular responses such as cell migration, growth, and proliferation. Although the function of TF under physiologic conditions is to coordinate blood clotting in response to tissue damage, TF is implicated in pathologic conditions such as tumorigenesis. Indeed, TF is aberrantly expressed in colorectal cancer, breast cancer, pancreatic cancer, and glioblastoma multiforme. It has been shown to promote tumor angiogenesis, tumor growth, metastasis, and venous thrombosis. Given that TF overexpression is associated with numerous types of solid tumors, it has garnered much attention as a potential therapeutic target.
Coagulation factor IX, also known as Christmas factor, Plasma thromboplastin component and PTC, is a secreted protein which belongs to the peptidase S1 family. Coagulation factor IX/F9 contains two EGF-like domains, one Gla (gamma-carboxy-glutamate) domain and one?peptidase S1 domain. Coagulation factor IX/F9 is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca2+ons, phospholipids, and factor VIIIa. Defects in Coagulation factor IX/F9 are the cause of thrombophilia due to factor IX defect which is a hemostatic disorder characterized by a tendency to thrombosis. Defects in Coagulation factor IX/F9 are also the cause of recessive X-linked hemophilia B ( HEMB ) which also known as Christmas disease.
Cofilin is a ubiquitous actin-binding protein required for the reorganization of actin filaments. It is a member of ADF (actin-depolymerizing factor)/cofilin family that is a key regulator of actin dynamics and essential for cellular motility,cytokinesis,and endocytosis. Cofilin activity is tightly regulated by phosphorylation and dephosphorylation. Phosphorylation at Ser3 can inhibit its activity,also causing translocation from the nucleus to the cytoplasm.
Cofilin 1(CFL1) Homo sapiens The protein encoded by this gene can polymerize and depolymerize F-actin and G-actin in a pH-dependent manner. Increased phosphorylation of this protein by LIM kinase aids in Rho-induced reorganization of the actin cytoskeleton. Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.
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