RAMP1

Receptor (G protein-coupled) activity modifying protein 1
PDB rendering based on 2yx8.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2YX8​, 3N7P​, 3N7R​, 3N7S​, 4RWG​
Identifiers
Symbol	RAMP1
External IDs	OMIM: 605153 MGI: 1858418 HomoloGene: 4275 IUPHAR: ChEMBL: 3316 GeneCards: RAMP1 Gene
Gene ontology Molecular function • receptor activity • calcitonin receptor activity • protein binding • protein transporter activity • coreceptor activity • calcitonin receptor binding Cellular component • extracellular space • intracellular • plasma membrane • integral component of plasma membrane • cell surface • receptor complex Biological process • angiogenesis • calcium ion transport • intracellular protein transport • G-protein coupled receptor signaling pathway • regulation of G-protein coupled receptor protein signaling pathway • protein transport • positive regulation of cAMP biosynthetic process • receptor internalization • cellular response to hormone stimulus • positive regulation of protein glycosylation • protein localization to plasma membrane Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10267	51801
Ensembl	ENSG00000132329	ENSMUSG00000034353
UniProt	O60894	Q9WTJ5
RefSeq (mRNA)	NM_001308353	NM_001168392
RefSeq (protein)	NP_001295282	NP_001161864
Location (UCSC)	Chr 2: 237.86 – 237.91 Mb	Chr 1: 91.18 – 91.23 Mb
PubMed search

Receptor activity modifying protein 1 is a protein that in humans is encoded by the RAMP1 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 (CALCRL) to the plasma membrane. CALCRL, 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 combination with the RAMP1 protein, CALCRL functions as the CGRP receptor. The RAMP1 protein is involved in the terminal glycosylation, maturation, and presentation of the CGRP receptor to the cell surface.^[1] The RAMP1 protein can also interact with the calcitonin receptor (CT) protein, where heteromerisation of RAMP1 with CT converts CT from a calcitonin receptor to the amylin receptor AMY₁ ^[3]

See also

Receptor activity-modifying protein

References

1. "Entrez Gene: RAMP1".
2. McLatchie LM, Fraser NJ, Main MJ, Wise A, Brown J, Thompson N, Solari R, Lee MG, Foord SM (May 1998). "RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor". Nature 393 (6683): 333–9. doi:10.1038/30666. PMID 9620797.
3. • "Calcitonin Receptors: Introduction". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.

Further reading

• Kusano S, Kukimoto-Niino M, Akasaka R, et al. (2008). "Crystal structure of the human receptor activity-modifying protein 1 extracellular domain.". Protein Sci. 17 (11): 1907–14. doi:10.1110/ps.036012.108. PMC 2578806. PMID 18725456.
• Héroux M, Hogue M, Lemieux S, Bouvier M (2007). "Functional calcitonin gene-related peptide receptors are formed by the asymmetric assembly of a calcitonin receptor-like receptor homo-oligomer and a monomer of receptor activity-modifying protein-1.". J. Biol. Chem. 282 (43): 31610–20. doi:10.1074/jbc.M701790200. PMID 17785463.
• Kuwasako K, Cao YN, Nagoshi Y, et al. (2004). "Characterization of the human calcitonin gene-related peptide receptor subtypes associated with receptor activity-modifying proteins.". Mol. Pharmacol. 65 (1): 207–13. doi:10.1124/mol.65.1.207. PMID 14722252.
• Nagoshi Y, Kuwasako K, Cao YN, et al. (2004). "Tumor necrosis factor-alpha downregulates adrenomedullin receptors in human coronary artery smooth muscle cells.". Peptides 25 (7): 1115–21. doi:10.1016/j.peptides.2004.04.010. PMID 15245870.
• Kuwasako K, Kitamura K, Nagoshi Y, Eto T (2003). "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. doi:10.1016/S0006-291X(02)03072-3. PMID 12565884.
• Wang YF, Zhang J, Li J, et al. (2004). "[Increased atria expression of receptor activity-modifying proteins in heart failure patients]". Zhonghua Yi Xue Yi Chuan Xue Za Zhi 21 (4): 351–4. PMID 15300632.
• Eskesen K, János T, Tibor H, et al. (2007). "Unaltered mRNA expression of calcitonin-like receptor and receptor activity modifying proteins in human arteries in stroke and myocardial infarction.". Ideggyogy Sz 60 (11-12): 459–66. PMID 18198792.
• Foord SM, Marshall FH (1999). "RAMPs: accessory proteins for seven transmembrane domain receptors.". Trends Pharmacol. Sci. 20 (5): 184–7. doi:10.1016/S0165-6147(99)01347-4. PMID 10354609.
• Fitzsimmons TJ, Zhao X, Wank SA (2003). "The extracellular domain of receptor activity-modifying protein 1 is sufficient for calcitonin receptor-like receptor function.". J. Biol. Chem. 278 (16): 14313–20. doi:10.1074/jbc.M211946200. PMID 12574158.
• Kuwasako K, Kitamura K, Nagoshi Y, et al. (2003). "Identification of the human receptor activity-modifying protein 1 domains responsible for agonist binding specificity.". J. Biol. Chem. 278 (25): 22623–30. doi:10.1074/jbc.M302571200. PMID 12684503.
• Bomberger JM, Parameswaran N, Hall CS, et al. (2005). "Novel function for receptor activity-modifying proteins (RAMPs) in post-endocytic receptor trafficking.". J. Biol. Chem. 280 (10): 9297–307. doi:10.1074/jbc.M413786200. PMID 15613468.
• Nakazato T, Nakayama T, Naganuma T, et al. (2009). "Haplotype-based case-control study of receptor (calcitonin) activity-modifying protein-1 gene in cerebral infarction.". J Hum Hypertens 24 (5): HASH(0x1512cf0). doi:10.1038/jhh.2009.68. PMID 19710695.
• Cottrell GS, Padilla B, Pikios S, et al. (2007). "Post-endocytic sorting of calcitonin receptor-like receptor and receptor activity-modifying protein 1.". J. Biol. Chem. 282 (16): 12260–71. doi:10.1074/jbc.M606338200. PMID 17310067.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Kunz TH, Mueller-Steiner S, Schwerdtfeger K, et al. (2007). "Interaction of receptor-activity-modifying protein1 with tubulin.". Biochim. Biophys. Acta 1770 (8): 1145–50. doi:10.1016/j.bbagen.2007.04.002. PMID 17493758.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Udawela M, Christopoulos G, Morfis M, et al. (2006). "A critical role for the short intracellular C terminus in receptor activity-modifying protein function.". Mol. Pharmacol. 70 (5): 1750–60. doi:10.1124/mol.106.024257. PMID 16912219.
• Padilla BE, Cottrell GS, Roosterman D, et al. (2007). "Endothelin-converting enzyme-1 regulates endosomal sorting of calcitonin receptor-like receptor and beta-arrestins.". J. Cell Biol. 179 (5): 981–97. doi:10.1083/jcb.200704053. PMC 2099187. PMID 18039931.
• Russo AF (2007). "Ramping it up: RAMP1 and the implications for migraine.". Pharmacogenomics 8 (7): 687–90. doi:10.2217/14622416.8.7.687. PMID 18240900.
• Qi T, Christopoulos G, Bailey RJ, et al. (2008). "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. doi:10.1124/mol.108.047142. PMID 18593822.

External links

• "Calcitonin Receptors". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
• RAMP1 human gene location in the UCSC Genome Browser.
• RAMP1 human gene details in the UCSC Genome Browser.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.