PS50261

G-protein coupled receptors family 2 profile 2

PROSITE profiles entry
Member databasePROSITE profiles
PROSITE profiles typedomain
Short nameG_PROTEIN_RECEP_F2_4

Description

A number of peptide hormones bind to G-protein coupled receptors that, while structurally similar to family 1 of G-protein coupled receptors (R7G), do not show any similarity at the level of their sequence, thus representing a new family whose current known members
[2]
are listed below: - Calcitonin receptor. - Calcitonin gene-related peptide receptor. - Corticotropin releasing factor receptor types 1 and 2. - Gastric inhibitory polypeptide receptor. - Glucagon receptor. - Glucagon-like peptide 1 receptor. - Growth hormone-releasing hormone receptor. - Parathyroid hormone / parathyroid hormone-related peptide types 1 and 2. - Pituitary adenylate cyclase activating polypeptide receptor. - Secretin receptor. - Vasoactive intestinal peptide receptor types 1 and 2. - Insects diuretic hormone receptor. In addition to the above characterized receptors, this family also includes: - Caenorhabditis elegans putative receptor C13B9.4. - Caenorhabditis elegans putative receptor ZK643.3. - Leucocyte antigen CD97, a protein that contains, in its N-terminal section, 3 EGF-like domains. - Cell surface glycoprotein EMR1, a protein that contains, in its N-terminal section, 6 to 7 EGF-like domains. All the characterized receptors are coupled to G-proteins which activate both adenylyl cyclase and the phosphatidylinositol-calcium pathway. Like family 1 R7G they seem to contain seven transmembrane regions. Their N-terminus is probably located on the extracellular side of the membrane and potentially glycosylated, while their C-terminus is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products. Family two G protein coupled receptors contain a long conserved region in their N terminal extracellular part which allow the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP
[1]
. This region contains five conserved cysteines residues which could be involved in disulfide bonds; we have developed a pattern in the region that spans the first three cysteines. We also developed a profile that covers the whole extracellular domain. One of the most highly conserved regions spans the C-terminal part of the last transmembrane region and the beginning of the adjacent intracellular region. We have used this region as a second signature pattern. We also developed a profile that spans the seven transmembrane regions.

References

1.Molecular tinkering of G protein-coupled receptors: an evolutionary success. Bockaert J, Pin JP. EMBO J. 18, 1723-9, (1999). View articlePMID: 10202136

2.Structure of the human CD97 gene: exon shuffling has generated a new type of seven-span transmembrane molecule related to the secretin receptor superfamily. Hamann J, Hartmann E, van Lier RA. Genomics 32, 144-7, (1996). View articlePMID: 8786105

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