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- *****************************************
- * G-protein coupled receptors signature *
- *****************************************
-
- G-protein coupled receptors [1 to 4] (also called R7G) are an extensive group
- of hormones, neurotransmitters, odorants and light receptors which transduce
- extracellular signals by interaction with guanine nucleotide-binding (G)
- proteins. The receptors that are currently known to belong to this family are
- listed below.
-
- - 5-hydroxytryptamine (serotonin) 1A to 1F, 2A to 2C, 5A, 5B, 6 and 7 [5].
- - Acetylcholine, muscarinic-type, M1 to M5.
- - Adenosine A1, A2A, A2B and A3 [6].
- - Adrenergic alpha-1A to -1C; alpha-2A to -2D; beta-1 to -3 [7].
- - Angiotensin II types I and II.
- - B2 bradykinin.
- - C5a anaphylatoxin.
- - Cannabinoid CB1 and CB2.
- - Cholecystokinin-A.
- - Cholecystokinin-B/Gastrin.
- - Dopamine D1 to D5 [8].
- - Endothelin ET-a and ET-b [9].
- - fMet-Leu-Phe (fMLP) (N-formyl peptide).
- - Follicle stimulating hormone (FSH-R) [10].
- - Gastrin-releasing peptide (GRP-R).
- - Gonadotropin-releasing hormone (GNRH-R).
- - Histamine H1 and H2 (gastric receptor I).
- - Interleukin-8 (IL-8R).
- - Lutropin-choriogonadotropic hormone (LSH-R) [10].
- - Melanocortin MC1R to MC5R.
- - Neuromedin B (NMB-R).
- - Neuromedin K (NK-3R).
- - Neuropeptide Y types 1 and 2.
- - Neurotensin (NT-R).
- - Octopamine (tyramine), from insects.
- - Odorants [11].
- - Opioids delta-, kappa- and mu-types [12].
- - Oxytocin (OT-R).
- - Platelet activating factor (PAF-R).
- - Prostaglandin E, EP1 to EP3 subtypes.
- - Purinoreceptors (ATP) [13].
- - Somatostatin types 1 to 5.
- - Substance-K (NK-2R).
- - Substance-P (NK-1R).
- - Thrombin.
- - Thromboxane A2.
- - Thyrotropin (TSH-R) [10].
- - Thyrotropin releasing factor (TRH-R).
- - Vasopressin V1a and V2.
- - Visual pigments (opsins and rhodopsin) [14].
-
- - Proto-oncogene mas.
- - A number of orphan receptors (whose ligand is not known) from mammals and
- birds.
- - Caenorhabditis elegans putative receptors C06G4.5 and C38C10.1.
- - Three putative receptors encoded in the genome of cytomegalovirus: US27,
- US28, and UL33.
- - ECRF3, a putative receptor encoded in the genome of herpesvirus saimiri.
- - Slime mold cyclic AMP receptors.
-
- The structure of all these receptors is thought to be identical. They have
- seven hydrophobic regions, each of which most probably spans the membrane.
- The N-terminus is located on the extracellular side of the membrane and is
- often glycosylated, while the C-terminus is cytoplasmic and generally
- phosphorylated. Three extracellular loops alternate with three intracellular
- loops to link the seven transmembrane regions. Most, but not all of these
- receptors, lack a signal peptide. The most conserved parts of these proteins
- are the transmembrane regions and the first two cytoplasmic loops. A conserved
- acidic-Arg-aromatic triplet is present in the N-terminal extremity of the
- second cytoplasmic loop [15] and could be implicated in the interaction with G
- proteins.
-
- To detect this widespread family of proteins we have developed a pattern that
- contains the conserved triplet and that also spans the major part of the third
- transmembrane helix.
-
- -Consensus pattern: [GSTALIVMYWC]-[GSTANCPDE]-{EDPKRH}-x(2)-[LIVMNGA]-x(2)-
- [LIVMFT]-[GSTANC]-[LIVMFYWSTAC]-[DENH]-R-[FYWCSH]-x(2)-
- [LIVM]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- for Xenopus ET-3 receptor, ECFR3, prostaglandin E, EP3 subtype receptor and
- two gustative/odorant receptors.
- -Other sequence(s) detected in SWISS-PROT: 20.
-
- -Expert(s) to contact by email: Chollet A.
- arc3029@ggr.co.uk
- Attwood T.K.
- bph6tka@biovax.leeds.ac.uk
- Kolakowski L.F. Jr.
- lfk@receptor.mgh.harvard.edu
-
- -Last update: June 1994 / Pattern and text revised.
-
- [ 1] Strosberg A.D.
- Eur. J. Biochem. 196:1-10(1991).
- [ 2] Kerlavage A.R.
- Curr. Opin. Struct. Biol. 1:394-401(1991).
- [ 3] Probst W.C., Snyder L.A., Schuster D.I., Brosius J., Sealfon S.C.
- DNA Cell Biol. 11:1-20(1992).
- [ 4] Savarese T.M., Fraser C.M.
- Biochem. J. 283:1-9(1992).
- [ 5] Branchek T.
- Curr. Biol. 3:315-317(1993).
- [ 6] Stiles G.L.
- J. Biol. Chem. 267:6451-6454(1992).
- [ 7] Friell T., Kobilka B.K., Lefkowitz R.J., Caron M.G.
- Trends Neurosci. 11:321-324(1988).
- [ 8] Stevens C.F.
- Curr. Biol. 1:20-22(1991).
- [ 9] Sakurai T., Yanagisawa M., Masaki T.
- Trends Pharmacol. Sci. 13:103-107(1992).
- [10] Salesse R., Remy J.J., Levin J.M., Jallal B., Garnier J.
- Biochimie 73:109-120(1991).
- [11] Lancet D., Ben-Arie N.
- Curr. Biol. 3:668-674(1993).
- [12] Uhl G.R., Childers S., Pasternak G.
- Trends Neurosci. 17:89-93(1994).
- [13] Barnard E.A., Burnstock G., Webb T.E.
- Trends Pharmacol. Sci. 15:67-70(1994).
- [14] Applebury M.L., Hargrave P.A.
- Vision Res. 26:1881-1895(1986).
- [15] Attwood T.K., Eliopoulos E.E., Findlay J.B.C.
- Gene 98:153-159(1991).
-