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RXFP1
Relaxin/insulin-like family peptide receptor 1, also known as RXFP1, is a human G protein coupled receptor that is one of the relaxin receptors. It is a rhodopsin-like GPCR which is unusual in this class as it contains a large extracellular binding and signalling domain. Some reports suggest that RXFP1 forms homodimers, however the most recent evidence indicates that relaxin binds a non-homodimer of RXFP1. See also * Relaxin family peptide hormones * Insulin/IGF/Relaxin family * Relaxin Relaxin is a protein hormone of about 6000 Da first described in 1926 by Frederick Hisaw. The relaxin family peptide hormones belong to the insulin superfamily and consists of seven peptides of high structural but low sequence similarity; rela ... ** Relaxin-3 References Further reading * * * * * * * * * * * * * * * * * External links * G protein-coupled receptors {{transmembranereceptor-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Relaxin Receptor
The relaxin receptors are a subclass of four closely related G protein-coupled receptors (GPCR) that bind relaxin peptide hormones. Below is list of human relaxin receptors, their endogenous peptide hormones, and what downstream enzymes are activated or inhibited by the receptor. See also * Relaxin family peptide hormones * Insulin/IGF/Relaxin family * Relaxin/insulin-like family peptide receptor 1 References External links * * G protein-coupled receptors {{transmembranereceptor-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Relaxin Family Peptide Hormones
Relaxin family peptide hormones in humans are represented by seven members: three relaxin-like (RLN) and four insulin-like (INSL) peptides: RLN1, RLN2, RNL3, INSL3, INSL4, INSL5, INSL6. This subdivision into two classes (RLN and INSL) is based primarily on early findings, and does not reflect the evolutionary origins or physiological differences between peptides. For example, it is known that the genes coding for RLN3 and INSL5 arose from one ancestral gene, and INSL3 shares origin with RLN2 and its multiple duplicates: RLN1, INSL4, INSL6. Genetics In humans and many other tetrapods, the RLN/INSL-encoding genes exist in four distinct clusters. The largest cluster contains four loci: RLN1, RLN2, INSL4 and INSL6, situated in tandem on human chromosome 9. This cluster arose from multiple local gene duplications that took place in the ancestor of placental mammals. The other three RLN/INSL genes exist as single loci in two linkage groups: RLN3 (chromosome 19), INSL3 (chromosom ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Relaxin
Relaxin is a protein hormone of about 6000 Da first described in 1926 by Frederick Hisaw. The relaxin family peptide hormones belong to the insulin superfamily and consists of seven peptides of high structural but low sequence similarity; relaxin-1 (RLN1), 2 (RLN2) and 3 (RLN3), and the insulin-like (INSL) peptides, INSL3, INSL4, INSL5 and INSL6. The functions of relaxin-3, INSL4, INSL5, and INSL6 remain uncharacterised. Synthesis In the female, relaxin is produced by the corpus luteum of the ovary, the breast and, during pregnancy, also by the placenta, chorion, and decidua. In the male, it is produced in the prostate and is present in human semen. Structure Structurally, relaxin is a heterodimer of two peptide chains of 24 and 29 amino acids linked by disulfide bridges, and it appears related to insulin. Relaxin is produced from its prohormone, "prorelaxin", by post-translational proteolytic cleavage of its signal peptide and C domain peptide. Function in Humans Re ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Relaxin-3
Relaxin-3 is a neuropeptide that was discovered in 2001, and which is highly conserved in species ranging from flies, fish, rodents and humans. Relaxin-3 is a member and ancestral gene of the relaxin family of peptides, which includes the namesake hormone relaxin (designated 'H2 relaxin' in humans) which mediates peripheral actions during pregnancy and which was found to relax the pelvic ligament in guinea pigs almost a century ago. The cognate receptor for relaxin-3 is the G-protein coupled receptor RXFP3 (relaxin family peptide 3 receptor), however relaxin-3 is pharmacologically able to also cross react with RXFP1 and RXFP3 (although the physiological relevance of such interactions, if they exist endogenously, are currently unknown). Structure Relaxin-3 consists of 51 amino acids in humans which are arranged into a two-chain structure (designated the A-chain and B-chain). There are three disulfide bonds (two interchain, one intrachain), with the residues that mediate binding ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
G Protein Coupled Receptor
G protein-coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptors, and G protein-linked receptors (GPLR), form a large group of evolutionarily-related proteins that are cell surface receptors that detect molecules outside the cell and activate cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times. Text was copied from this source, which is available under Attribution 2.5 Generic (CC BY 2.5) license. Ligands can bind either to extracellular N-terminus and loops (e.g. glutamate receptors) or to the binding site within transmembrane helices (Rhodopsin-like family). They are all activated by agonists although a spontaneous auto-activation of an empty receptor can also be observed. G protein-coupled receptors are found only in eukaryotes, including yeast, choanoflagellates, and an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Insulin/IGF/Relaxin Family
The insulin/IGF/relaxin family is a group of evolutionary related proteins which possess a variety of hormonal activities. Family members in human include two subfamilies: 1) insulin and insulin-like growth factors 2) relaxin family peptides: * relaxins 1 and 2 * relaxin 3 * Leydig cell-specific insulin-like peptide (gene INSL3) * early placenta insulin-like peptide (ELIP) (gene INSL4) * insulin-like peptide 5 (gene INSL5) * insulin-like peptide 6 Structure These proteins are characterized by having three disulfide bonds in a characteristic motif. Some family members have an additional disulfide bond also in a conserved location. All of these proteins have a helical segment (corresponding to B chain in insulin) followed by a variable-length chain, followed by a domain (A chain in insulin) with two helices pinned against each other via a disulfide bond. These two regions are linked by two or three disulfide bonds. Amongst the different proteins in the family, very little ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
