RAMP3

RAMP3
Identifiers
Aliases	RAMP3, entrez:10268, receptor activity modifying protein 3
External IDs	OMIM: 605155 MGI: 1860292 HomoloGene: 4276 GeneCards: RAMP3
Gene location (Human)
Chr.	Chromosome 7 (human)[1]
End	45,186,302 bp[1]
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)[2]
End	6,627,475 bp[2]
RNA expression pattern
	Top expressed in
	right lung; ; upper lobe of left lung; ; right lobe of thyroid gland; ; left lobe of thyroid gland; ; gastric mucosa; ; left ventricle; ; subcutaneous adipose tissue; ; gallbladder; ; lymph node; ; right coronary artery;
	Top expressed in
	medial dorsal nucleus; ; lateral geniculate nucleus; ; medial geniculate nucleus; ; cervix; ; barrel cortex; ; proximal tubule; ; kidney; ; adrenal gland; ; visual cortex; ; posterior horn of spinal cord;
	More reference expression data
	n/a
Gene ontology
Molecular function	coreceptor activity; protein binding; amyloid-beta binding; adrenomedullin receptor activity; amylin receptor activity;
Cellular component	integral component of membrane; membrane; plasma membrane; receptor complex; integral component of plasma membrane; intracellular anatomical structure; cell surface; lysosome; amylin receptor complex 3; adrenomedullin receptor complex;
Biological process	G protein-coupled receptor signaling pathway; regulation of G protein-coupled receptor signaling pathway; cellular response to estradiol stimulus; receptor internalization; G protein-coupled receptor signaling pathway involved in heart process; transport; protein transport; protein localization to plasma membrane; intracellular protein transport; negative regulation of transcription, DNA-templated; calcium ion transport; positive regulation of receptor recycling; angiogenesis; adenylate cyclase-activating G protein-coupled receptor signaling pathway; positive regulation of gene expression; positive regulation of protein kinase A signaling; positive regulation of cell death; cellular response to hormone stimulus; positive regulation of peptidyl-serine phosphorylation; cross-receptor inhibition within G protein-coupled receptor heterodimer; positive regulation of protein kinase B signaling; positive regulation of ERK1 and ERK2 cascade; amylin receptor signaling pathway; positive regulation of protein localization to plasma membrane; response to amyloid-beta; positive regulation of calcium ion import across plasma membrane; adrenomedullin receptor signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	10268
	56089
	ENSG00000122679
	ENSMUSG00000041046
	O60896
	Q9WUP1
	NM_005856
	NM_019511
	NP_005847
	NP_062384
	Wikidata
View/Edit Human	View/Edit Mouse

Receptor activity modifying protein 3, also known as RAMP3, is a human gene.[5][6]

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.[5]

References

GRCh38: Ensembl release 89: ENSG00000122679 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000041046 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: RAMP3".
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. Bibcode:1998Natur.393..333M. doi:10.1038/30666. PMID 9620797. S2CID 4364526.

Kuwasako K, Kitamura K, Nagata S, Kato J (2008). "Functions of the extracellular histidine residues of receptor activity-modifying proteins vary within adrenomedullin receptors". Biochem. Biophys. Res. Commun. 377 (1): 109–13. doi:10.1016/j.bbrc.2008.09.105. PMID 18835256.
Roh J, Chang CL, Bhalla A, et al. (2004). "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. doi:10.1074/jbc.M305332200. PMID 14615490.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology". Science. 300 (5620): 767–72. Bibcode:2003Sci...300..767S. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205.
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.
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.
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.
Bomberger JM, Spielman WS, Hall CS, et al. (2005). "Receptor activity-modifying protein (RAMP) isoform-specific regulation of adrenomedullin receptor trafficking by NHERF-1". J. Biol. Chem. 280 (25): 23926–35. doi:10.1074/jbc.M501751200. PMID 15805108.
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.
Kuwasako K, Cao YN, Chu CP, et al. (2006). "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. doi:10.1074/jbc.M511147200. PMID 16410241.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
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.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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. Bibcode:2002PNAS...9916899M. 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. S2CID 7249716.
Harikumar KG, Simms J, Christopoulos G, et al. (2009). "Molecular basis of association of receptor activity-modifying protein 3 with the family B G protein-coupled secretin receptor". Biochemistry. 48 (49): 11773–85. doi:10.1021/bi901326k. PMC 2790544. PMID 19886671.
Flahaut M, Pfister C, Rossier BC, Firsov D (2003). "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. doi:10.1021/bi0347508. PMID 12939163.
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. S2CID 33491956.

External links

RAMP3 human gene location in the UCSC Genome Browser.
RAMP3 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000122679 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000041046 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: RAMP3".

[pmid9620797-6] 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. Bibcode:1998Natur.393..333M. doi:10.1038/30666. PMID 9620797. S2CID 4364526.

RAMP3

References

Further reading

External links