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Low affinity immunoglobulin gamma Fc region receptor III-A (FCGR3A) is a receptor for the Fc portion of immunoglobulin G, and is involved in the elimination of antigen-antibody complexes from the circulation, as well as other antibody-dependent responses. FCGR3A needs to associate with the gamma subunit of Fc epsilon. The FCGR3A receptor is expressed on natural killer (NK) cells as an integral membrane glycoprotein anchored through a transmembrane peptide, while FCGR3B is expressed on polymorphonuclear neutrophils (PMN) where the receptor is anchored through a phosphatidylinositol (PI) linkage. In addition, FCGR3A is expressed on macrophages, subpopulation of T-cells, immature thymocytes and placental trophoblasts. FCGR3A mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis. FCGR3A gene mutations are linked with susceptibility to recurrent viral infections, susceptibility to systemic lupus erythematosus, and alloimmune neonatal neutropenia.

TCEAL3 belongs to the transcription elongation factor A (SII)-like (TCEAL) gene family. TCEAL family members hold TFA domains and operate as nuclear phosphoproteins which control transcription in a promoter context-dependent fashion. Various family members are situated in the X chromosome.

TFB1M is a member of the methyltransferase superfamily. TFB1M is a dimethyltransferase which methylates mitochondrial 12S rRNA at the conserved stem loop. The TFB1M protein also is part of the basal mitochondrial transcription complex and is required for mitochondrial gene expression. TFB1M stimulates transcription independently of the methyltransferase activity.

Calmodulin Like 5, also known as CALML5 is a part of the calmodulin family of calcium binding proteins. CALML5 undergoes a conformational change as a result of binding calcium. CALML5 is taking part in terminal differentiation of keratinocytes and encodes a calcium binding protein expressed in the epidermis.

TGFBR1 is a single-pass type 1 membrane protein which is a part of the TGFB receptor subfamily and the protein kinase superfamily. TGFBR1 is a secreted protein that performs many cellular functions such as the control of cell growth, cell differentiation, cell proliferation and apoptosis. TGFBR1 also controls the immune system and shows different activities on various types of cell, or cells at different developmental stages.

All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

Transmembrane Protein 27 (TMEM27) is a type 1 transmembrane protein which is imperative for trafficking amino acid transporters to the apical brush border of proximal tubules. TMEM27 binds to amino acid transporters and regulates their expression on the plasma membrane. The extracellular domain of TMEM27 is cleaved off the surface of beta cells.

Jumping Translocation Breakpoint (JTB) takes part in the regulation of cell proliferation and is essential for cytokinesis during mitosis. JTB inhibits apoptosis induced by TGFB1 and increases AURKB activity. JTB is also a part of the chromosomal passenger complex (CPC) which is a key regulator of mitosis.

Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.

Lipase Endothelial (LIPG) has extensive phospholipase activity and may be involved in lipoprotein metabolism and vascular biology. The LIPG protein is considered a member of the TG lipase family through its sequence and characteristic lid region which provides substrate specificity for enzymes of the TG lipase family. In addition, the LIPG has triglyceride lipase activities. LIPG hydrolyzes HDLs more efficiently than other lipoproteins. LIPG also binds heparin.

PTP4A2 is part of a small class of the protein tyrosine phosphatase (PTP) family. PTP4A2 is localized to the early endosome that take part in a variety of cellular activities. PTP4A2 protein interacts with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), therefore has a role as a regulator of GGT II activity. Overexpression of PTP4A2 in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis.

Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation.
Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occuring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.

Japanese encephalitis previously known as Japanese B encephalitis is a virus from the family Flaviviridae. it is closely related to the West Nile virus and St. Louis encephalitis virus. Positive sense single stranded RNA genome is packaged in the capsid, formed by the capsid protein. The outer envelope is formed by envelope (E) protein and is the protective antigen. It aids in entry of the virus to the inside of the cell. The genome also encodes several nonstructural proteins also (NS1,NS2a,NS2b,NS3,N4a,NS4b,NS5). NS1 is produced as secretory form also. NS3 is a putative helicase, and NS5 is the viral polymerase. It has been noted that the Japanese encephalitis virus (JEV) infects the lumen of the endoplasmic reticulum (ER) and rapidly accumulates substantial amounts of viral proteins for the JEV. Japanese Encephalitis is diagnosed by detection of antibodies in serum and CSF (cerebrospinal fluid) by IgM capture ELISA.

E1 and E2 glycoproteins form a heterodimer which is involved in virus attachment to the host cell, virion internalization via clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to human LDLR, CD81 and SCARB1/SR-BI receptors, however this binding insufficient for infection, some additional liver specific cofactors may be required. The fusion function may perhaps be conducted by E1. E2 hinders human EIF2AK2/PKR activation, preventing the establishment of an antiviral state. E2 is a viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively located on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses. These interactions allow seizure of circulating HCV particles by these cells and subsequent diffusion to permissive cells.

Cystatin-A is the intracellular inhibitor of cysteine proteinase cathepsin B (CatB) and belongs to family 1 of the cystatin superfamily of inhibitor proteins. CSTA is a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. It has been proposed that extracellular CatB together with other classes of proteinases are all subjected to a cascade-like manner of activation. CatB and its inhibitor Cystatin-A are involved in degradation of extracellular matrix proteins during tissue remodeling. CSTA is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Cystatin-A has been reported to be found in high concentrations in epithelial cells, polymorphonuclear leukocytes and lymphoid tissue. Stefins may be used as prognostic and diagnostic tools for cancer.

HINT1, also known as Histidine triad nucleotide-binding protein 1 is part of the superfamily named for a near C-terminal HXHXHXX motif (H:Histidine, X:a hydrophobic amino acid) positioned at the ?-phosphate of nucleotide substrates. HINT1 hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2. Though it was initially considered to be a protein kinase C inhibitor and act as a haplod-insufficient tumor suppressor including spontaneous tumor formation in Hint+/- and Hint-/- , its actual physiologic function is not known.

SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

Dehydrogenase/reductase SDR family member 8 (HSD17B11) is a member of the HSD17B family of proteins, which regulate the availability of steroids within various tissues throughout the body. HSD17B11 is widely expressed with the highest levels found in the retina, pancreas, kidney, liver, lung, adrenal, small intestine, ovary and heart as well as in steroidogenic cells. HSD17B11 converts androstan-3-?,17-?-diol (3-?-diol) to androsterone, suggesting it may participate in androgen metabolism during steroidogenesis.

SGTA is a ubiquitously expressed protein that contains three TPR protein-protein interaction duplicates. SGTA takes part as a component of the androgen receptor (AR)-chaperone-cochaperone complex, functions as a cochaperone and participates in androgen signaling. SGTA binds directly to HSC70 and HSP70 and mediates their ATPase activity. SGTA gene encodes a protein that is able to interact with the chief nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate. In addition, SGTA interacts with Vpu and Gag from HIV-1, SARS-CoV accessory protein 7a, DNAJC5 and DNAJC5B. Since this transcript is expressed universally in several tissues, SGTA serves a housekeeping function. While being involved in apoptosis and androgen signaling, SGTA is a possible molecule for polycystic ovary syndrome, a disorder characterized by androgen excess, obesity and menstrual disturbances.

HSPA9 is part of the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members that are also called heat-shock cognate proteins. HSPA9 encodes a heat-shock cognate protein that is involved in the control of cell proliferation and acts as a chaperone. HSPA9 was restricted to chromosome 5, band q31, a region that is often deleted in myeloid leukemias and myelodysplasia (MDS), making it a candidate tumor suppressor gene, which is consistent with the biological function of its murine homologue. HSPA9 supresses nuclear translocation, transcriptional activation, and control of centrosome-duplication functions of p53.

CAPSL is a calcium-binding protein holding two conserved calcium-binding motifs (EF-hands) which are found in a superfamily of calcium sensors and calcium signal modulators. In addition, the CAPSL gene is in the same linkage disequilibrium (LD) block as the IL7R gene and there is well known association between the CAPSL-IL7R locus and type 1 diabetes.

THTPA enzyme is part of the THTPase family. THTPA is localized to the cytoplasm and expressed at small quantities in a variety of tissues, including testis, uterus, prostate, bladder, lung and kidney. THTPA is a hydrolase that catalyzes the H2O-dependent hydrolysis of thiamine triphosphate (THTP) to thiamine diphosphate (THDP), the main form of thiamine within the cell. THTPA occurs as a monomer and is activated at an optimal pH of 8.5.

TNNT2 is the tropomyosin-binding subunit of the troponin complex, which is situated on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration. Mutations in TNNT2 gene are related with familial hypertrophic cardiomyopathy as well as with dilated cardiomyopathy. TNNT2 mutation takes part in hypertrophic cardiomyopathy.

TPD52L1 (hD53, hD53L1) is a member of D52 gene family and overexpressed in human breast carcinoma. TPD52L1 contains coiled-coil motif, which is responsible for homo- and heteromeric interaction, and may be a regulator of cell proliferation and calcium-mediated signal transduction.
Moreover, TPD52L1 interacts with the mitogen-activated protein kinase kinase kinase 5 (MAP3K5/ASK1) and positively regulates MAP3K5-induced apoptosis.