Receptor activity-modifying protein 2
Details
- Name
- Receptor activity-modifying protein 2
- Synonyms
- Calcitonin-receptor-like receptor activity-modifying protein 2
- CRLR activity-modifying protein 2
- Gene Name
- RAMP2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0001714|Receptor activity-modifying protein 2 MASLRVERAGGPRLPRTRVGRPAALRLLLLLGAVLNPHEALAQPLPTTGTPGSEGGTVKN YETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAELFDLGFPNPLAERII FETHQIHFANCSLVQPTFSDPPEDVLLAMIIAPICLIPFLITLVVWRSKDSEAQA
- Number of residues
- 175
- Molecular Weight
- 19607.44
- Theoretical pI
- 5.58
- GO Classification
- Functionscoreceptor activity / protein transporter activityProcessesadherens junction assembly / angiogenesis / basement membrane assembly / bicellular tight junction assembly / calcium ion transport / cAMP biosynthetic process / cellular response to hormone stimulus / cellular response to vascular endothelial growth factor stimulus / female pregnancy / G-protein coupled receptor signaling pathway / heart development / intracellular protein transport / negative regulation of endothelial cell apoptotic process / negative regulation of vascular permeability / positive regulation of angiogenesis / positive regulation of cAMP biosynthetic process / positive regulation of gene expression / positive regulation of vasculogenesis / protein localization to plasma membrane / protein transport / receptor internalization / regulation of blood pressure / regulation of G-protein coupled receptor protein signaling pathway / response to estradiol / response to hypoxia / response to progesterone / sprouting angiogenesis / vascular smooth muscle cell development / vasculogenesisComponentscell surface / coated pit / cytoplasm / integral component of plasma membrane / lysosome / plasma membrane / receptor complex
- General Function
- Protein transporter activity
- Specific Function
- Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL.
- Pfam Domain Function
- RAMP (PF04901)
- Transmembrane Regions
- 146-166
- Cellular Location
- Membrane
- Gene sequence
>lcl|BSEQ0010608|Receptor activity-modifying protein 2 (RAMP2) ATGGCCTCGCTCCGGGTGGAGCGCGCCGGCGGCCCGCGTCTCCCTAGGACCCGAGTCGGG CGGCCGGCAGCGCTCCGCCTCCTCCTCCTGCTGGGCGCTGTCCTGAATCCCCACGAGGCC CTGGCTCAGCCTCTTCCCACCACAGGCACACCAGGGTCAGAAGGGGGGACGGTGAAGAAC TATGAGACAGCTGTCCAATTTTGCTGGAATCATTATAAGGATCAAATGGATCCTATCGAA AAGGATTGGTGCGACTGGGCCATGATTAGCAGGCCTTATAGCACCCTGCGAGATTGCCTG GAGCACTTTGCAGAGTTGTTTGACCTGGGCTTCCCCAATCCCTTGGCAGAGAGGATCATC TTTGAGACTCACCAGATCCACTTTGCCAACTGCTCCCTGGTGCAGCCCACCTTCTCTGAC CCCCCAGAGGATGTACTCCTGGCCATGATCATAGCCCCCATCTGCCTCATCCCCTTCCTC ATCACTCTTGTAGTATGGAGGAGTAAAGACAGTGAGGCCCAGGCCTAG
- Chromosome Location
- 17
- Locus
- 17q12-q21.1
- External Identifiers
Resource Link UniProtKB ID O60895 UniProtKB Entry Name RAMP2_HUMAN GenBank Protein ID 3171912 GenBank Gene ID AJ001015 GenAtlas ID RAMP2 HGNC ID HGNC:9844 - General References
- 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. 1998 May 28;393(6683):333-9. [Article]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Kusano S, Kukimoto-Niino M, Hino N, Ohsawa N, Okuda K, Sakamoto K, Shirouzu M, Shindo T, Yokoyama S: Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding. Protein Sci. 2012 Feb;21(2):199-210. doi: 10.1002/pro.2003. Epub 2011 Dec 28. [Article]