Semaphorin-5A (SEMA5A) is a member of the Semaphorin family of axon guidance molecules. SEMA5A is a 140 kDa protein. Class 5 Semaphorins are type I transmembrane glycoproteins with an N- terminal Sema domain and multiple juxtamembrane type 1 Thrombospondin (TSP) repeats within their extracellular domains. SEMA5A is expressed in neuroepithelial cells surrounding retinal axons, oligodendrocytes, the base of limb buds, the mesoderm surrounding cranial vessels , and the cardiac atrial septum and endocardial cushions, Human SEMA5A cDNA encodes a signal sequence, a extracellular domain (ECD), a transmembrane sequence and an cytoplasmic portion. SEMA5A mutations have been implicated in the genetic syndrome,cri-du-chat,while some polymorphisms may increase risk for neurodegenerative diseases such as Parkinson. The expression of SEMA5A may be upregulated in metastatic cancer cells and downregulated in autism.
Semaphorins are secreted, transmembrane, and GPI-linked proteins, defined by cysteine-rich semaphorin protein domains, that have important roles in a variety of tissues. Humans have 20 semaphorins, Drosophila has five, and two are known from DNA viruses. Semaphorins are found in nematodes and crustaceans but not in non-animals. They are grouped into eight classes on the basis of phylogenetic tree analyses and the presence of additional protein motifs. Semaphorins have been implicated in diverse developmental processes such as axon guidance during nervous system development and regulation of cell migration. Semaphorin-5A, also known as Semaphorin-F, Sema F, SEMA5A and SEMAF, is a single-pass type I membrane protein which belongs to thesemaphorin family. Semaphorin5A / SEMA5A contains onePSI domain, oneSema domain and sevenTSP type-1 domains. It may act as positive axonal guidance cues. Semaphorin5A / SEMA5A is an axon regulator molecule and plays major roles during neuronal and vascular development. It plays an essential role in embryonic development. Semaphorin5A / SEMA5A induces endothelial cell migration from pre-existing vessels. It also plays a role in autism, reducing the ability of neurons to form connections with other neurons in certain brain regions.
Regenerating islet-derived protein 4, also known as REG-like protein, REG4, GISP and RELP, a member of the regenerating gene family belonging to the calcium (C-type) dependent lectin superfamily, has been found to be involved in malignancy in several different organs including the stomach, colorectum, pancreas and prostate. It is highly expressed in the gastrointestinal tract and markedly up-regulated in colon adenocarcinoma, pancreatic cancer, gastric adenocarcinoma, and inflammatory bowel disease. Expression of the Reg4 in different cell types has been associated with regeneration, cell growth and cell survival, cell adhesion and resistance to apoptosis. REG4 protein overexpression is associated with an unfavorable response to preoperative chemoradiotherapy and may be used as a predictive biomarker clinically. REG4 may play an important role in the development and progression of colorectal cancer, as well as in intestinal morphogenesis and epithelium restitution.
Semenogelin-1 (SEMG1) is the predominant protein in semen; it is a secretory protein involved in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, each possibly having a separate function. In the proteolysis process, Alpha-inhibin-92 and alpha-inhibin-31 are produced; they inhibit the secretion of pituitary follicle-stimulating hormone. At the same time, it breaks down the gel matrix, allowing the spermatozoa to move more freely.
SENP2 is an enzyme that belongs to the peptidase C48 family. SENP2 is a protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. SUMO1 is a small ubiquitin-like protein that can be covalently conjugated to other proteins. It has been implicated as a down-regulator of CTNNB1 levels and may therefore be a modulator of the Wnt pathway.
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 depolymerized 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.
Sentrin-Specific Protease 8 (SENP8) mediates the reversible covalent modification of proteins by NEDD8. SENP8 catalyzes the full-length NEDD8 to generate its mature form and deconjugation of NEDD8 from targeted proteins such as CUL2 , CUL4A in vivo, or p53. but it does not show activity against ubiquitin or SUMO proteins.
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