RAMP3 explained

Receptor activity modifying protein 3, also known as RAMP3, is a human gene.^{[1] [2]}

The protein encoded by this gene is a member of the RAMP family of single-transmembrane-domain proteins, called receptor (calcitonin) activity modifying proteins (RAMPs). RAMPs are type I transmembrane proteins with an extracellular N terminus and a cytoplasmic C terminus. RAMPs are required to transport calcitonin-receptor-like receptor (CRLR) to the plasma membrane. CRLR, a receptor with seven transmembrane domains, can function as either a calcitonin gene-related peptide (CGRP) receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. In humans and other mammals, there are 3 RAMPS, while in fish there are more, with sub-variants. In the presence of this (RAMP3) protein, CRLR functions as an adrenomedullin receptor with low affinity for CGRP.^[1]

Further reading

• Kuwasako K, Kitamura K, Nagata S, Kato J . Functions of the extracellular histidine residues of receptor activity-modifying proteins vary within adrenomedullin receptors. . Biochem. Biophys. Res. Commun. . 377 . 1 . 109–13 . 2008 . 18835256 . 10.1016/j.bbrc.2008.09.105 .
• Roh J, Chang CL, Bhalla A, etal . Intermedin is a calcitonin/calcitonin gene-related peptide family peptide acting through the calcitonin receptor-like receptor/receptor activity-modifying protein receptor complexes. . J. Biol. Chem. . 279 . 8 . 7264–74 . 2004 . 14615490 . 10.1074/jbc.M305332200 . free .
• Stelzl U, Worm U, Lalowski M, etal . A human protein-protein interaction network: a resource for annotating the proteome. . Cell . 122 . 6 . 957–68 . 2005 . 16169070 . 10.1016/j.cell.2005.08.029 . 11858/00-001M-0000-0010-8592-0 . 8235923 . free .
• Scherer SW, Cheung J, MacDonald JR, etal . Human chromosome 7: DNA sequence and biology. . Science . 300 . 5620 . 767–72 . 2003 . 12690205 . 2882961 . 10.1126/science.1083423 . 2003Sci...300..767S .
• Kuwasako K, Cao YN, Nagoshi Y, etal . Characterization of the human calcitonin gene-related peptide receptor subtypes associated with receptor activity-modifying proteins. . Mol. Pharmacol. . 65 . 1 . 207–13 . 2004 . 14722252 . 10.1124/mol.65.1.207 .
• Kuwasako K, Kitamura K, Nagoshi Y, Eto T . Novel calcitonin-(8-32)-sensitive adrenomedullin receptors derived from co-expression of calcitonin receptor with receptor activity-modifying proteins. . Biochem. Biophys. Res. Commun. . 301 . 2 . 460–4 . 2003 . 12565884 . 10.1016/S0006-291X(02)03072-3 .
• Wang YF, Zhang J, Li J, etal . [Increased atria expression of receptor activity-modifying proteins in heart failure patients] . Zhonghua Yi Xue Yi Chuan Xue Za Zhi . 21 . 4 . 351–4 . 2004 . 15300632 .
• Foord SM, Marshall FH . RAMPs: accessory proteins for seven transmembrane domain receptors. . Trends Pharmacol. Sci. . 20 . 5 . 184–7 . 1999 . 10354609 . 10.1016/S0165-6147(99)01347-4 .
• Bomberger JM, Spielman WS, Hall CS, etal . Receptor activity-modifying protein (RAMP) isoform-specific regulation of adrenomedullin receptor trafficking by NHERF-1. . J. Biol. Chem. . 280 . 25 . 23926–35 . 2005 . 15805108 . 10.1074/jbc.M501751200 . free .
• Bomberger JM, Parameswaran N, Hall CS, etal . Novel function for receptor activity-modifying proteins (RAMPs) in post-endocytic receptor trafficking. . J. Biol. Chem. . 280 . 10 . 9297–307 . 2005 . 15613468 . 10.1074/jbc.M413786200 . free .
• Kuwasako K, Cao YN, Chu CP, etal . Functions of the cytoplasmic tails of the human receptor activity-modifying protein components of calcitonin gene-related peptide and adrenomedullin receptors. . J. Biol. Chem. . 281 . 11 . 7205–13 . 2006 . 16410241 . 10.1074/jbc.M511147200 . free .
• Hillier LW, Fulton RS, Fulton LA, etal . The DNA sequence of human chromosome 7. . Nature . 424 . 6945 . 157–64 . 2003 . 12853948 . 10.1038/nature01782 . 2003Natur.424..157H . free .
• Suzuki Y, Yamashita R, Shirota M, etal . Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions. . Genome Res. . 14 . 9 . 1711–8 . 2004 . 15342556 . 10.1101/gr.2435604 . 515316 .
• Gerhard DS, Wagner L, Feingold EA, etal . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
• Ota T, Suzuki Y, Nishikawa T, etal . Complete sequencing and characterization of 21,243 full-length human cDNAs. . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . free .
• Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2002 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Udawela M, Christopoulos G, Morfis M, etal . A critical role for the short intracellular C terminus in receptor activity-modifying protein function. . Mol. Pharmacol. . 70 . 5 . 1750–60 . 2006 . 16912219 . 10.1124/mol.106.024257 . 7249716 .
• Harikumar KG, Simms J, Christopoulos G, etal . Molecular basis of association of receptor activity-modifying protein 3 with the family B G protein-coupled secretin receptor. . Biochemistry . 48 . 49 . 11773–85 . 2009 . 19886671 . 10.1021/bi901326k . 2790544 .
• Flahaut M, Pfister C, Rossier BC, Firsov D . N-Glycosylation and conserved cysteine residues in RAMP3 play a critical role for the functional expression of CRLR/RAMP3 adrenomedullin receptor. . Biochemistry . 42 . 34 . 10333–41 . 2003 . 12939163 . 10.1021/bi0347508 .
• Qi T, Christopoulos G, Bailey RJ, etal . Identification of N-terminal receptor activity-modifying protein residues important for calcitonin gene-related peptide, adrenomedullin, and amylin receptor function. . Mol. Pharmacol. . 74 . 4 . 1059–71 . 2008 . 18593822 . 10.1124/mol.108.047142 . 33491956 .

Notes and References

1. Web site: Entrez Gene: RAMP3 .
2. McLatchie LM, Fraser NJ, Main MJ, Wise A, Brown J, Thompson N, Solari R, Lee MG, Foord SM . RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor . Nature . 393 . 6683 . 333–9 . May 1998 . 9620797 . 10.1038/30666 . 1998Natur.393..333M . 4364526 .