"Biosensis"

Supplier: Biosensis

FUNCTION: This is a receptor for the tachykinin neuropeptide neuromedin K (neurokinin B). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. PTM: The anchoring of this receptor to the plasma membrane is probably mediated by the palmitoylation of a cysteine residue. MISCELLANEOUS: The rank order of affinity of this receptor to tachykinins is: neuromedin K > substance K > substance P. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.

Supplier: Biosensis

FUNCTION: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. Orexin-A binds to both OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R with a similar high affinity. SUBCELLULAR LOCATION: Endoplasmic reticulum; rough endoplasmic reticulum. Associated with perikaryal rough endoplasmic reticulum as well as cytoplasmic large granular vesicles at synapses. SIMILARITY: Belongs to the orexin family.

Supplier: Biosensis

FUNCTION: Nociceptin is the ligand of the opioid receptor-like receptor (OPRL1). It may act as a transmitter in the brain by modulating nociceptive and locomotor behavior. May be involved in neuronal differentiation and development. SUBCELLULAR LOCATION: Secreted protein. TISSUE SPECIFICITY: Expressed predominantly in the spinal cord and brain, being more abundant in the hypothalamus and striatum. Also found in small amounts in ovary. PTM: Specific enzymatic cleavages at paired basic residues probably yield other active peptides besides nociceptin. PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. SIMILARITY: Belongs to the opioid neuropeptide precursor family.

Supplier: Biosensis

The neural adhesion molecule Contactin-6, also known as NB-3, is a contactin/F3 subgroup member of immunoglobulin superfamily. It is expressed exclusively in the nervous system and mainly upregulated at the early postnatal stage during mouse brain development. Employing Northern blot analysis Kamei et al found that amongst different regions of the adult human nervous system cerebellum expressed highest level of NB-3 mRNA. The expression of NB-3 in the cerebellum increases until adulthood. In contrast, the expression in the cerebrum declines to a low level after postnatal day 7. NB-3 like other neural recognition molecules plays a vitally important role in axonal guidance during development, plasticity, and maintenance of synaptic connections in the adult brain. Cui et al recently showed that NB-3 acts as a novel Notch ligand to participate in oligodendrocyte generation. Furthermore, NB-3 triggers nuclear translocation of the Notch intracellular domain and promotes oligodendrogliogenesis from progenitor cells and differentiation of oligodendrocyte precursor cells via Deltex1. In primary oligodendrocytes, NB-3 increases myelin-associated glycoprotein transcripts. Hence, the NB-3/Notch signaling pathway may be worthwhile a closer examination for its potential for the treatment of demyelinating diseases. Human NB-3 shares with rat NB-3 86% identity in nucleotide sequences and 90% identity in amino acid sequences. FUNCTION: Contactins mediate cell surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Involved in motor coordination. SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Expressed in brain. In brain, it is preferentially expressed in the accessory olfactory bulb, layers II/III and V of the cerebral cortex, piriform cortex, anterior thalamic nuclei, locus coeruleus of the pons and mesencephalic trigeminal nucleus and in Purkinje cells of the cerebellum.

Supplier: Biosensis

Myelin is a membrane characteristic of the nervous tissue and functions as an insulator to increase the velocity of the stimuli being transmitted between a nerve cell body and its target. Myelin isolated from human and bovine nervous tissue is composed of approximately 80% lipid and 20% protein, and 30% of the protein fraction constitutes myelin basic protein (MBP). MBP is an 'intrinsically unstructured' protein with a high proportion (approximately 75%) of random coil, but postulated to have core elements of beta-sheet and alpha-helix. MBP is a major protein in CNS myelin and is expressed specifically in the nervous system. A detailed immunochemical examination of monoclonal and polyclonal antibody responses to MBP and its peptides has revealed the existence of as many as 27 antigenic determinants, many of them conformational. Topological mapping of the potential antigenic determinants onto a model of MBP secondary structure places these determinants within 11 separate regions of the molecule, including those portions that have been found to be encephalitogenic. The message for myelin basic protein is selectively translocated to the ends of the cell processes. Immunization with myelin-associated antigens including MBP significantly promotes recovery after spinal cord contusion injury in the rat model. FUNCTION: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity). SUBUNIT: Homodimer (By similarity). SUBCELLULAR LOCATION: Myelin membrane; peripheral membrane protein; cytoplasmic side. Cytoplasmic side of myelin. TISSUE SPECIFICITY: Found in both the central and the peripheral nervous system.

Supplier: Biosensis

DBH is an oxireductase belonging to the copper type II ascorbate-dependent monooxygenase family. DBH exists as a homotetramer composed of two non-covalently bound disulfide-linked dimers. It is present in the synaptic vesicles of postganglionic sympathetic neurons and converts dopamine to norepinephrine. It binds 2 copper ions and 1 PQQ per subunit . Depending on the presence of a signal peptide, DBH can exist in both soluble and membrane-bound forms.

Supplier: Biosensis

FUNCTION: Required for autophagy. Conjugates to ATG12 and associates with isolation membrane to form cup-shaped isolation membrane and autophagosome. The conjugate detaches from the membrane immediately before or after autophagosome formation is completed. FUNCTION: May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. SUBCELLULAR LOCATION: Cytoplasm. Colocalizes with nonmuscle actin. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Ubiquitous. The mRNA is present at similar levels in viable and apoptotic cells, whereas the protein is dramatically highly expressed in apoptotic cells. INDUCTION: By apoptotic stimuli. PTM: Conjugated to ATG12; which is essential for autophagy, but is not required for association with isolation membrane. SIMILARITY: Belongs to the ATG5 family.

Supplier: Biosensis

FUNCTION: Required for autophagy. SUBUNIT: Conjugated to ATG5. SUBCELLULAR LOCATION: Cytoplasm. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Ubiquitous. SIMILARITY: Belongs to the ATG12 family.

Supplier: Biosensis

FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP and SEPT5. May play a more general role in the ubiquitin proteasomal pathway by participating in the removal and/or detoxification of abnormally folded or damaged protein. Loss of this ubiquitin ligase activity appears to be the mechanism underlying pathogenesis of PARK2. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. Regulates cyclin E during neuronal apoptosis. May represent a tumor suppressor gene. SUBCELLULAR LOCATION: Cytoplasm. Co-localizes with STY11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies. TISSUE SPECIFICITY: Highly expressed in the brain including the substantia nigra. Expressed in heart, testis and skeletal muscle. Expression is down-regulated or absent in tumor biopsies, and absent in the brain of PARK2 patients. Overexpression protects dopamine neurons from kainate-mediated apoptosis.

Supplier: Biosensis

FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include SYT11, CCNE1, GPR37, STUB1, a 22 kDa O-linked glycosylated isoform of SNCAIP and SEPT5. May play a more general role in the ubiquitin proteasomal pathway by participating in the removal and/or detoxification of abnormally folded or damaged protein. Loss of this ubiquitin ligase activity appears to be the mechanism underlying pathogenesis of PARK2. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. Regulates cyclin E during neuronal apoptosis. May represent a tumor suppressor gene. SUBCELLULAR LOCATION: Cytoplasm. Co-localizes with STY11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies. TISSUE SPECIFICITY: Highly expressed in the brain including the substantia nigra. Expressed in heart, testis and skeletal muscle. Expression is down-regulated or absent in tumor biopsies, and absent in the brain of PARK2 patients. Overexpression protects dopamine neurons from kainate-mediated apoptosis.

Supplier: Biosensis

FUNCTION: Ubiquitin-like protein which binds to a wide range of target proteins. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved in targeting RANGAP1 to the nuclear pore complex protein RANBP2. SUBUNIT: Covalently attached to a number of proteins such as PML, RANGAP1, HIPK2, SP100, p53, p73alpha, MDM2, JUN and DNMT3B. Also interacts with HIF1A, HIPK2, HIPK3, CHD3, PIAS1, EXOSC9, TDG, RAD51 and RAD52. SUBCELLULAR LOCATION: Nucleus; nuclear membrane. Nucleus; nucleoplasm; nuclear speckle. Cytoplasm. SIMILARITY: Belongs to the ubiquitin family. SMT3 subfamily. SIMILARITY: Contains 1 ubiquitin-like domain.

Supplier: Biosensis

Synuclein alpha interacting protein (Synphilin-1) contains several protein-protein interaction domains and interacts with alpha synuclein in neurons. Mutations of SNCAIP have been linked to Parkinson disease. The amino acid sequence of synphilin-1 shares a high level of identity with its human counterpart, particularly in regions containing ankyrin-like motifs and the coiled-coil domain. Expression pattern of synphilin-1 in tissues is similar in both mouse and human. Synphilin-1 has an important role in the formation of aggregates and cytotoxicity in Parkinson disease and also Dorfin may be involved in the pathogenic process by ubiquitylation of synphilin-1.

Supplier: Biosensis

Synuclein alpha interacting protein (Synphilin-1) contains several protein-protein interaction domains and interacts with alpha synuclein in neurons. Mutations of SNCAIP have been linked to Parkinson disease. The amino acid sequence of synphilin-1 shares a high level of identity with its human counterpart, particularly in regions containing ankyrin-like motifs and the coiled-coil domain. Expression pattern of synphilin-1 in tissues is similar in both mouse and human. Synphilin-1 has an important role in the formation of aggregates and cytotoxicity in Parkinson disease and also Dorfin may be involved in the pathogenic process by ubiquitylation of synphilin-1.

Supplier: Biosensis

Tyrosine hydroxylase (TH) is the rate-limiting enzyme in the synthesis of the catecholamines dopamine, epinephrine and norepinephrine. Therefore the regulation of the TH enzyme represents the central means for controlling the synthesis of these important catecholamines. FUNCTION: Plays an important role in the physiology of adrenergic neurons. CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O2 = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin. COFACTOR: Fe(2+) ion. ENZYME REGULATION: Phosphorylation leads to an increase in the catalytic activity. PATHWAY: Catecholamine biosynthesis; first step. SUBUNIT: Homotetramer. PTM: In vitro, phosphorylation of Ser-19 increases the rate of Ser-40 phosphorylation, which results in enzyme opening and activation. SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family. The presence of different DNA sequences at the TH locus confers susceptibility to various disorders of the brain including manic-depression and schizophrenia. Parkinson's disease is also considered a TH deficiency as low dopamine levels are a consistent neurochemical abnormality.

Supplier: Biosensis

FUNCTION: This is a specific receptor for parathyroid hormone. The activity of this receptor is mediated by g proteins which activate adenylyl cyclase. PTHR2 may be responsible for PTH effects in a number of physiological systems. It may play a significant role in pancreatic function. PTHR2 presence in neurons indicates that it may function as a neurotransmitter receptor. SUBUNIT: Binds to TIPF39/TIP39. SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. TISSUE SPECIFICITY: Abundantly expressed in brain, arterial and cardiac endothelium. Found as well in sperm, in the head of the epididymis. Lower expression is found in vascular smooth muscle, exocrine pancreas, testis and placenta. SIMILARITY: Belongs to the G-protein coupled receptor 2 family.

Supplier: Biosensis

FUNCTION: Receptor for brain-derived neurotrophic factor (BDNF), neurotrophin-3 and neurotrophin-4/5 but not nerve growth factor (NGF). Involved in the development and/or maintenance of the nervous system. This is a tyrosine-protein kinase receptor. Known substrates for the TRK receptors are SHC1, PI-3 kinase, and PLC-gamma-1. CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. SUBUNIT: Exists in a dynamic equilibrium between monomeric (low affinity) and dimeric (high affinity) structures (By similarity). Binds APS. Interacts with SQSTM1. SUBCELLULAR LOCATION: Membrane; single-pass type I membrane protein. ALTERNATIVE PRODUCTS: 3 named isoforms produced by alternative splicing. Additional isoforms seem to exist. TISSUE SPECIFICITY: The different forms are differentially expressed in various cell types. Isoform T2 is primarily expressed in neurons. PTM: Ligand-mediated auto-phosphorylation. SIMILARITY: Belongs to the Tyr protein kinase family. Insulin receptor subfamily. SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like) domains. SIMILARITY: Contains 2 LRR (leucine-rich) repeats. SIMILARITY: Contains 1 protein kinase domain.