golgi

Responsible for the biosynthesis of pyroglutamyl peptides. QPCTL Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 35.5 kDa and the accession number is Q9NXS2.

GOLPH3 Protein, Human, Recombinant (His) is expressed in E. coli.

Golgi membrane protein 1, also known as Golgi membrane protein GP73, Golgi phosphoprotein 2, and GOLM1, is a protein that belongs to the GOLM1 / CASC4 family. GOLM1 is widely expressed. It is highly expressed in the colon, prostate, trachea, and stomach. It is expressed at a lower level in testis, muscle, lymphoid tissues, white blood cells, and spleen. It is predominantly expressed by cells of the epithelial lineage. GOLM1 is expressed at a low level in the normal liver. Expression significantly increases in virus (HBV, HCV) infected liver. Expression of GOLM1 does not increase in liver disease due to non-viral causes (alcohol-induced liver disease, autoimmune hepatitis). Increased expression in hepatocytes appears to be a general feature of advanced liver disease. In liver tissue from patients with adult giant-cell hepatitis (GCH), GOLM1 is strongly expressed in hepatocyte-derived syncytial giant cells. GOLM1 is constitutively expressed by biliary epithelial cells but not by hepatocytes.

This protein may be involved in regulating membrane traffic to and from trans-Golgi network. Isoform TGN46 is widely expressed. Isoform TGN51 is more abundant in fetal lung and kidney. Isoform TGN48 is barely expressed in embryonic kidney and promyelocytic cells.

COG5 Protein, Human, Recombinant (His) is expressed in E. coli.

GOLM1 Protein, Human, Recombinant (GST) is expressed in E. coli.

GOPC, also known as PIST, interacts specifically with TC1 (a Rho-family small GTPase)] as a binding partner for Rhotekin. Rhotekin associates with PIST in vitro and both polarized and non-polarized MDCK (Madin-Darby canine kidney) cells. The C-terminal SPV (Ser-Pro-Val) motif of Rhotekin binds to the PDZ domain of PIST. The co-localization of PIST and Rhotekin at the Golgi apparatus can be detected in non-polarized fibroblast-like MDCK cells and AJs (adherens junctions) in the fully polarized cells. PIST and Rhotekin are recruited from the cytosol to AJs as the cell becomes polarized. Expression of constitutively active Rho or prevention of Rhotekin-PIST interaction induced diffuse cytoplasmic distribution of Rhotekin in polarized MDCK cells. GOPC may regulate CFTR chloride currents and acid-induced ACCN3 currents by modulating cell surface expression of both channels. It may also regulate the intracellular trafficking of the ADR1B receptor. GOPC is ubiquitously expressed and its overexpression results in CFTR intracellular retention and degradation in the lysosomes.

Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly. CLINT1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 72.3 kDa and the accession number is Q14677.

FAM20C Protein, Mouse, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 60.4 kDa and the accession number is Q5MJS3.

AP1B1 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.

APRIL (a proliferation-inducing ligand), also known as TNFSF13, TALL2, TRDL1, and CD256, is a member of the TNF ligand superfamily. It is synthesized as a 32 kDa proprotein which is cleaved by furin in the Golgi to release the active 17 kDa soluble molecule. Secreted human APRIL, which consists almost entirely of a single TNF homology domain, shares 85% amino acid sequence identity with mouse and rat APRIL. Both APRIL and its close relative BAFF bind and signal through the TNF superfamily receptors TACI and BCMA, while BAFF additionally functions through BAFF R. APRIL binds to heparan sulfate proteoglycans (HSPGs) independently of its binding to TACI and BCMA. APRIL can form bioactive heterotrimers with BAFF, and these circulate in the serum of patients with rheumatic immune disorders. APRIL enhances the proliferation and survival of plasma cells and also promotes T cell-dependent humoral responses. APRIL levels are elevated in the serum during coronary artery disease, and it is also elevated in many cancers primarily due to expression by tumor-infiltratin neutrophils.

SECTM1A (secreted and transmembrane 1A), is 192 amino acid (aa) protein, appears to share structural and functional characteristics with other SECTM1 proteins. Human SECTM1 can be found either found as an approximately 27 kDa intracellular type I transmembrane protein that shows a perinuclear, Golgi like staining pattern, or as a 20 kDa soluble, secreted form, and is produced by some myeloid cells and by thymic epithelia and fibroblasts. Stimulation with IFN gamma is often necessary to detect human SECTM1 expression, and it is thought to be an interferon early response gene. Mouse SECTM1A cDNA encodes a signal sequence, an extracellular domain with four potential N linked glycosylation sites, a transmembrane sequence, and a very short (approximately 6 aa) cytoplasmic sequence. SECTM1 proteins from human and mouse show species specific binding of CD7 and co stimulation of T cells, including enhancement of CD3 induced proliferation.

Parathyroid hormone (PTH) is a critical hormone in the regulation of Ca++ homeostasis. Parathyroid hormone is the most important endocrine regulator of calcium and phosphorus concentration in extracellular fluid. This hormone is secreted from cells of the parathyroid glands and finds its major target cells in bone and kidney. Another hormone, parathyroid hormone-related protein, binds to the same receptor as parathyroid hormone and has major effects on development. Like most other protein hormones, parathyroid hormone is synthesized as a preprohormone. After intracellular processing, the mature hormone is packaged with in the Golgi into secretory vesicles, the secreted into blood by exocytosis. In renal epithelium, PTH promotes conversion of Vitamin D to its active form, lowers Ca++ excretion and increases phosphate excretion. PTH also increases hematopoietic stem cell proliferation and mobilization and induces arterial vasodilation by regulating Ca++ influx in PTH1R-expressing arterial smooth muscle.

Valosin-Containing Protein (VCP) is a nuclear protein that belongs to the AAA ATPase family. VCP is a putative ATP-binding protein involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. It is necessary for the fragmentation of Golgi stacks during mitosis and their reassembly after mitosis. VCP has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation. VCP participates in the formation of the transitional endoplasmic reticulum (tER) and regulates E3 ubiquitin-protein ligase activity of RNF19A.

Plays a role in influencing the retrograde trafficking of lysosomal sorting receptors SORT1 and IGF2R from the endosomes to the trans-Golgi network by controlling the recruitment of retromer complex to the endosomal membrane. Regulates the localization and activation of RAB7A which is required to recruit the retromer complex to the endosomal membrane. CLN5 Protein, Human, Recombinant (His) is expressed in E. coli expression system with C-6xHis tag. The predicted molecular weight is 43.5 kDa and the accession number is O75503.

Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. CLTCL1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 20.8 kDa and the accession number is P53675.

Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for endosomal localization of WASHC2C. Mediates the association of the CSC with the WASH complex via WASHC2. Required for the endosomal localization of TBC1D5.; (Microbial infection) The heterotrimeric retromer cargo-selective complex (CSC) mediates the exit of human papillomavirus from the early endosome and the delivery to the Golgi apparatus.

SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network.

Structural protein involved in the envelopment of mature virion (MV) to form the wrapped virion (WV). The wrapping consists of the addition of Golgi membranes to the mature virion. Participates in mature virion (MV) movement within the infected cell. May play an indirect role in MV-cell fusion. Variola virus (isolate Human/India/Ind3/1967) OPG154 Protein (His) is expressed in HEK293 mammalian cells with N-6xHis tag. The predicted molecular weight is 16.5 kDa and the accession number is P33816.

RAB2A, a protein essential for ER-to-Golgi transport, is critical in promoting proteolytic activity and 3D invasiveness of breast cancer (BC) cell lines.RAB2A is amplified and elevated in human BC and is a powerful and independent predictor of disease recurrence in BC patients. Thus, RAB2A is a novel trafficking determinant essential for regulation of a mesenchymal invasive program of BC dissemination. At the cellular levels, RAB2A controls both canonical polarized Golgi-to-Plasma membrane trafficking of the junctional protein E-cadherin, and post-endocytic trafficking of the membrane-bound metalloprotease, MT1-MMP.

CHST11, also known as C4ST-1, belongs to the sulfotransferase 2 family. CHST11 localizes to the golgi membrane, and catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage, and is distributed on the surfaces of many cells and extracellular matrices. A chromosomal translocation involving CHST11 gene and IgH, t(12;14)(q23;q32), has been reported in a patient with B-cell chronic lymphocytic leukemia.

IMPAD1 protein (IMPA3, gPAPP or IMPase 3) belongs to the inositol monophosphatase family. It is found in Purkinje cells, brain stem, lung and chondrocytes. Mouse IMPAD1 gene encodes a type II transmembrane Golgi-embedded glycoprotein with 356 amino acid residues which generates a 306 amino acid residues mature protein after processing. It is expressed in embryo, and in theory may catalyze myo-inositol monophosphate to myo-inositol. Free myo-inositol is used to generate inositol phospholipid, an essential component of intracellular signaling pathways that mobilize calcium. Mouse IMPAD1 exhibits 91% sequence identity with the human homologue.

Integral Membrane Protein 2B (ITM2B) is expressed in the Golgi and on the cell surface. ITM2B forms homodimer through disulfide-linked interaction with SPPL2A, SPPL2B and APP. ITM2B is expressed in brain and the other tissues. Defects in ITM2B cause cerebral amyloid angiopathy ITM2B-related type 1(CAA-ITM2B1) and amyloid angiopathy ITM2B-related type 2(CAA-ITM2B2). CAA-ITM2B1 is characterized by amyloid deposition in the walls of cerebral blood vessels and neurodegeneration in the central nervous system. CAA-ITM2B2 characterized by amyloid deposition in the walls of the blood vessels of the cerebrum, choroid plexus, cerebellum, spinal cord and retina.

Rab6 is one of the most conserved Rab GTPaes throughout evolution and the most abundant Rab protein associated with the Golgi complex. The two ubiquitous Rab isoforms, Rab6A and Rab6A', that are generated by alternative splicing of the RAB6A gene, regulate several transport steps at the Golgi level, including retrograde transport between endosomes and Golgi, anterograde transport between Golgi and the plasma membrane, and intra-Golgi and Golgi to endoplasmic reticulum transport. In MEF cells, most of the functions were attributed to the two ubiquitous Rab6 isoforms.

The ADAMs (a disintegrin and metalloprotease) comprise a family of multidomain proteins with metalloprotease, cell adhesion, and signaling activities. Human ADAM12, which is implicated in diseases such as cancer, is expressed in two splice forms, the transmembrane ADAM12-L and the shorter and soluble ADAM12-S. ADAM12, also known as and Meltrin alpha, is a member of the ADAM protein family, which contains one disintegrin domain, one EGF-like domain and one peptidase M12B domain. ADAM12 is synthesized as a zymogen with the prodomain keeping the metalloprotease inactive through a cysteine-switch mechanism. Maturation and activation of the protease involves the cleavage of the prodomain in the trans-Golgi or possibly at the cell surface by a furin-peptidase. It is a membrane-anchored metalloprotease, which has been implicated in activation-inactivation of growth factors that play an important role in wound healing, including heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) and IGF binding proteins. ADAM12 may also regulate cell-cell and cell-extracellular matrix contacts through interactions with cell surface receptors - integrins and syndecans - potentially influencing the actin cytoskeleton. Moreover, ADAM12 interacts with several cytoplasmic signaling and adaptor molecules through its intracellular domain, thereby directly transmitting signals to or from the cell interior. These ADAM12-mediated cellular effects appear to be critical events in both biological and pathological processes. In addition to protease activity, ADAM12 possesses cell binding and cell signaling properties. In many studies, ADAM12 overexpression has been correlated with disease, and ADAM12 has been shown to promote tumor growth and progression in cancer. On the other hand, protective effects of ADAM12 in disease have also been reported.

HRas, also known as HRAS, belongs to the small GTPase superfamily, Ras family, and is widely expressed. It functions in signal transduction pathways. HRas can bind GTP and GDP, and they have intrinsic GTPase activity. It undergoes a continuous cycle of de- and re-palmitoylation, which regulates its rapid exchange between the plasma membrane and the Golgi apparatus. Defects in HRAS are the cause of faciocutaneoskeletal syndrome (FCSS). FCSS is a rare condition characterized by prenatally increased growth, postnatal growth deficiency, mental retardation, distinctive facial appearance, cardiovascular abnormalities, tumor predisposition, skin, and musculoskeletal abnormalities. Defects in HRAS also can cause congenital myopathy with excess of muscle spindles. HRAS deficiency may be a cause of susceptibility to Hurthle cell thyroid carcinoma. It has been shown that defects in HRAS can cause susceptibility to bladder cancer which is a malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and different sites in the bladder. Most bladder cancers are transitional cell carcinomas. They begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. Defects in HRAS are the cause of oral squamous cell carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

NAPG (NSF Attachment Protein Gamma, also known as gamma SNAP) is a Protein Coding gene. This gene encodes soluble NSF attachment protein gamma. The encoded protein mediates platelet exocytosis and controls the membrane fusion events of this process. NAPG is required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. NAPG belongs to the SNAP family. It is widely expressed in the brain, thyroid, and other tissues. SNAPs enable N-ethyl-maleimide-sensitive fusion protein (NSF) to bind to target membranes. NSF and SNAPs appear to be general components of the intracellular membrane fusion apparatus, and their action at specific sites of fusion must be controlled by SNAP receptors particular to the membranes being fused.

GATE-16, also known as ATG8, belongs to the MAP1 LC3 family. It is expressed at high levels in the brain, heart, prostate, ovary, spleen and skeletal muscle. GATE-16 is expressed at very low levels in lung, thymus and small intestine. GATE-16 is involved in intra-Golgi traffic. It modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1.

ARF3, also known as ADP-ribosylation factor 3, belongs to the RAS superfamily. Members of this family include ARF1, ARF2, ARF3, ARF4, ARF5 and ARF6. ARF3 gene is a member of the human ARF gene family. These genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. ARF3 functions as an allosteric activator of the cholera toxin subunit, an ADP-ribosyltransferase. It is involved in protein trafficking and may modulate vesicle budding and uncoating within the Golgi apparatus.

Synapse-associated protein 1 (SYAP1), also known as PRO3113 and BSTA, belongs to the synapse-associated BSD domain family, featuring three α-helices and two conserved tryptophan and phenylalanine residues located at the C-terminus. Expressed near neuronal Golgi and synaptic regions of cerebellar Purkinje cells, SYAP1 has been linked to intact sensorimotor control and general vesicular trafficking in neurons. SYAP1-deficient mice display impaired locomotor activity. In cultured adipocytes, SYAP1 facilitates mTORC2-mediated phosphorylation of protein kinase Akt1 and adipocyte differentiation. Chromosomal band Xp22.2 houses the human SYAP1 gene, a region associated with developmental delay and autism spectrum disorder. SYAP 1 may be a target for future cancer therapies as it was induced by tamoxifen in breast cancer cells sensitive to tamoxifen growth inhibition.

Cathepsin E (CTSE) is a gastric aspartyl protease that functions as a disulfide-linked homodimer. It is a member of the Peptidase C1 family, and has a specificity similar to that of Pepsin A and Cathepsin D. CTSE is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. It is expressed abundantly in the stomach, the Clara cells of the lung and activated B-lymphocytes, and at lower levels in lymph nodes, skin and spleen. CTSE is an intracellular proteinase that have a role in immune function, activation-induced lymphocyte depletion in the thymus, neuronal degeneration and glial cell activation in the brain. Futhermore, it probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation.

Mouse ULBP1, also known as RAET1I and NKG2DL1, is a member of the ULBP/RAET1 gene family. ULBP1 plays an important role in immune responses, especially in cancer and infectious diseases, and is well-known to bind to NKG2D together with at least ULBP 2 and 3. These proteins are distantly related to major histocompatibility class I (MHC I) molecules, possessing the alpha 1 and alpha 2 Ig-like domains, but lacking the alpha 3 domain. Unlike MHC Class I, they have no capacity to bind peptide or interact with beta2-microglobulin. It can activate multiple signaling pathways in primary NK cells, gamma delta T cells, and CD8+ alpha beta T cells, resulting in the production of cytokines and chemokines.ULBP1 is expressed in wide range of tissues including heart, brain, lung, liver, bone marrow and some tumor cells, T-cells, B-cells, As an unconventional member of the MHC class I family, ULBP1 is able to interact with soluble CMV glycoprotein UL16 in CMV infected cells. The interaction with UL16 blocked the interaction with the NKG2D receptor, and thus might escape the immune surveillance. Furthermore, UL16 also causes ULBP1 to be retained in the ER and cis-Golgi apparatus so that it does not reach the cell surface. The ULBP1 regulation may have implications for development of new therapeutic strategies against cancer cells.

Synaptobrevin Homolog YKT6 (YKT6) is an enzyme that belongs to the Synaptobrevin family. YKT6 contains a longin domain and a v-SNARE coiled-coil homology domain. YKT6 is highly conserved from yeast to human and it can functionally complement the loss of the yeast homolog in the yeast secretory pathway. It is a membrane associated, isoprenylated protein that functions at the endoplasmic reticulum-Golgi transport step. YKT6 is considered as one of the SNARE recognition molecules implicated in vesicular transport between secretory compartments.

Involved in transport from the endoplasmic reticulum to the Golgi apparatus. Required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation. SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining endoplasmic reticulum exit sites (ERES). SAR1A Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 49.4 kDa and the accession number is Q9NR31.

Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.

Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. Isoform 1, isoform 2 and isoform 3 play a role in unfolded protein response (UPR) by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress. Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway. Isoform 1 and isoform 3 play a key role in the regulation of the levels of PSEN1 by targeting its accumulation to aggresomes which may then be removed from cells by autophagocytosis. Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently downregulating the ORAI1-mediated Ca2+ mobilization. Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing.

The deletion of BNIP3L results in retention of mitochondria during lens fiber cell remodeling, and that deletion of BNIP3L also results in the retention of endoplasmic reticulum and Golgi apparatus. BNIP3L localizes to the endoplasmic reticulum and Golgi apparatus of wild-type newborn mouse lenses and is contained within mitochondria, endoplasmic reticulum and Golgi apparatus isolated from adult mouse liver. As the cells become packed with keratin bundles, Bnip3L expression triggers mitophagy to rid the cells of the last remaining 'living' characteristic, thus completing the march from 'living' to 'dead' within the hair follicle. during retinal development tissue hypoxia triggers HIF1A/HIF-1 stabilization, resulting in increased expression of the mitophagy receptor BNIP3L/NIX. BNIP3L-dependent mitophagy results in a metabolic shift toward glycolysis essential for RGC neurogenesis. BNIP3L could be a potential therapeutic target for ischemic stroke

LMAN2 (Lectin, Mannose Binding 2, also known as VIP36) is a Protein Coding gene. This gene encodes a type I transmembrane lectin that shuttles between the endoplasmic reticulum, the Golgi apparatus, and the plasma membrane. The encoded protein binds high mannose type glycoproteins and may facilitate their sorting, trafficking, and quality control. The L-type lectin LMAN2 appears to be specifically required for the accumulation of GPRC5B in the Golgi complex and restriction of GPRC5B transport along the exosomal pathway. This may occur due to interference with the adaptor protein GGA1-mediated trans-Golgi network-to-endosome transport of GPRC5B. A Golgi-traversing pathway for the exosomal release of the cargo protein GPRC5B in which CD2AP facilitates the entry and LMAN2 impedes the exit of the flux, respectively.

Secreted and transmembrane 1 (SECTM1), also known as K12, is a transmembrane and secreted protein with characteristics of a type 1a transmembrane protein of SECTM family. It is found in a perinuclear Golgi-like pattern and thought to be involved in hematopoietic and/or immune system processes. The human K12 protein has been shown to be primarily expressed in spleen, prostate, testis, small intestine, and in peripheral blood leukocytes. The K12 protein is expressed on the cell surface in such small amounts as to preclude detection. Alternatively, it may be that K12 on the cell surface is rapidly cleaved to generate a soluble K12 protein. Immunohistochemical analysis of peripheral blood cells shows that K12 is found in leukocytes of the myeloid lineage, with the strongest staining observed in granulocytes and no detectable expression in lymphocytes. May be involved in thymocyte signaling. It had been suggested a role for thymic microenvironment-produced K12 in regulation of thymocyte signaling and cytokine release, particularly in the setting of thymus pathology where IFN-gamma is upregulated such as myasthenia gravis. In addition, as a putative natural CD7 ligand, SECTM1/K12 may be responsible for the costimulatory role it plays in T cell activation.

STX3, also known as syntaxin 3, belongs to the syntaxin family. STX3 is a target membrane protein (t-SNARE) that is needed for membrane fusion. Membrane fusion requires the formation of a complex between a vesicle protein (v-SNARE) and t-SNAREs. STX3, together with syntaxin 2, are predominantly localized at the plasma membrane. Syntaxin 2 cycles between the plasma membrane and the perinuclear compartment whereas syntaxin 3 cycles between the plasma membrane and the trans-Golgi network. It is possible that this cycling has an important role in the regulation of t-SNARE function.

ARF5, also known as ADP-ribosylation factor 5, belongs to the small GTPase superfamily, Arf family. Members of this family stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. ARF5 functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARF5 Is involved in protein trafficking. ARF5 may also modulate vesicle budding and uncoating within the Golgi apparatus.

Neurocalcin-delta (NCALD) is a neuronal calcium-binding protein that belongs to the neuronal calcium sensor (NCS) family. It expressed in mammalian brains. NCALD contains an N-terminal myristoylation signal and four EF-hand calcium binding loops. The protein possesses a Ca2+ /myristoyl switch. It is cytosolic at resting calcium levels. However, elevated intracellular calcium levels induce a conformational change which exposes the myristoyl group, resulting in protein association with membranes and partial co-localization with the perinuclear trans-golgi network. NCALD protein is thought to be a regulator of G protein-coupled receptor signal transduction.

B cell maturation antigen (BCMA) is a member of the TNF receptor superfamily. It has been designated TNFRSF17. Mouse BCMA is a 185 amino acid (aa) protein consisting of a 49 aa extracellular domain, a 23 aa transmembrane domain, and a 113 aa intracellular domain. BCMA is a type III membrane protein containing one extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs and mature B cell lines. Although some expression has been observed at the cell surface, BCMA appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells. This data suggests that BCMA may play an important role in B cell development,function and regulation.

Tumor necrosis factor ligand superfamily member 13 belongs to the tumor necrosis factor family. It is also known as APRIL, TALL2, TRDL1, and CD256. It is synthesized as a 32 kDa proprotein which is cleaved by furin in the Golgi to release the active 17 kDa soluble molecule. TNFSF13 is a Cytokine that binds to TNFRSF13B/TACI and to TNFRSF17/BCMA and plays a role in the regulation of tumor cell growth. It expressed at high levels in transformed cell lines, cancers of colon, thyroid, lymphoid tissues and specifically expressed in monocytes and macrophages. Its expression by CD4+ T cells inhibits the production of Th2 cytokines and allergic inflammation.

Syntaxin-8 is a single-pass type IV membrane protein which belongs to the syntaxin family. It contains one t-SNARE coil homology domain. STX8 is highly expressed in heart, also found in brain, kidney, liver, lung, placenta, skeletal muscle, spleen and pancreas. STX8 is involved in protein trafficking from early to late endosomes via vesicle fusion and exocytosis. It as a vesicle trafficking protein functions in the early secretory pathway, possibly mediating retrograde transport form cis-golgi membrane to the ER.

Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade.

Catalyzes the transfer of CDP-ribitol to the distal N-acetylgalactosamine of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1). This constitutes the first step in the formation of the ribitol 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1. Required for normal location of POMGNT1 in Golgi membranes, and for normal POMGNT1 activity. May interact with and reinforce a large complex encompassing the outside and inside of muscle membranes. Could be involved in brain development (Probable).

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane. In epithelial cells, it regulates transport from the Golgi to the basolateral membrane. May play a role in the basolateral recycling pathway and in phagosome maturation. May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion. Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis. When phosphorylated by LRRK2 on Thr-73, it binds RILPL1 and inhibits ciliogenesis.

Structural protein involved in the envelopment of mature virion (MV) to form the wrapped virion (WV). The wrapping consists of the addition of Golgi membranes to the mature virion. Participates in mature virion (MV) movement within the infected cell. May play an indirect role in MV-cell fusion. Variola virus (isolate Human/India/Ind3/1967) OPG154 Protein (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 16.6 kDa and the accession number is P33816.