Receptor activity-modifying protein 1

Details

Name
Receptor activity-modifying protein 1
Kind
protein
Synonyms
  • Calcitonin-receptor-like receptor activity-modifying protein 1
  • CRLR activity-modifying protein 1
Gene Name
RAMP1
UniProtKB Entry
O60894Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0010607|Receptor activity-modifying protein 1
MARALCRLPRRGLWLLLAHHLFMTTACQEANYGALLRELCLTQFQVDMEAVGETLWCDWG
RTIRSYRELADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVRDPPGSILY
PFIVVPITVTLLVTALVVWQSKRTEGIV
Number of residues
148
Molecular Weight
16987.765
Theoretical pI
8.29
GO Classification
Functions
amylin receptor activity / calcitonin gene-related peptide binding / calcitonin gene-related peptide receptor activity
Processes
adenylate cyclase-activating G protein-coupled receptor signaling pathway / amylin receptor signaling pathway / calcitonin gene-related peptide receptor signaling pathway / G protein-coupled receptor signaling pathway / regulation of G protein-coupled receptor signaling pathway
Components
CGRP receptor complex
General Function
Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL
Specific Function
amylin receptor activity
Pfam Domain Function
Signal Regions
1-26
Transmembrane Regions
118-138
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0001711|447 bp
ATGGCCCGGGCCCTGTGCCGCCTCCCGCGGCGCGGCCTCTGGCTGCTCCTGGCCCATCAC
CTCTTCATGACCACTGCCTGCCAGGAGGCTAACTACGGTGCCCTCCTCCGGGAGCTCTGC
CTCACCCAGTTCCAGGTAGACATGGAGGCCGTCGGGGAGACGCTGTGGTGTGACTGGGGC
AGGACCATCAGGAGCTACAGGGAGCTGGCCGACTGCACCTGGCACATGGCGGAGAAGCTG
GGCTGCTTCTGGCCCAATGCAGAGGTGGACAGGTTCTTCCTGGCAGTGCATGGCCGCTAC
TTCAGGAGCTGCCCCATCTCAGGCAGGGCCGTGCGGGACCCGCCCGGCAGCATCCTCTAC
CCCTTCATCGTGGTCCCCATCACGGTGACCCTGCTGGTGACGGCACTGGTGGTCTGGCAG
AGCAAGCGCACTGAGGGCATTGTGTAG
Chromosome Location
2
Locus
2q37.3
External Identifiers
ResourceLink
UniProtKB IDO60894
UniProtKB Entry NameRAMP1_HUMAN
GenBank Protein ID3171910
GenBank Gene IDAJ001014
GeneCard IDRAMP1
GenAtlas IDRAMP1
HGNC IDHGNC:9843
PDB ID(s)2YX8, 3N7P, 3N7R, 3N7S, 4RWG, 5V6Y, 6D1U, 6E3Y, 6UMG, 6ZHO, 6ZIS, 7KNT, 7KNU, 7P0F, 7P0I, 7TYF, 7TYW, 8AX5, 8AX6, 8AX7, 9AUC
KEGG IDhsa:10267
IUPHAR/Guide To Pharmacology ID51
NCBI Gene ID10267
General References
  1. 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]
  2. 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]
  3. Kusano S, Kukimoto-Niino M, Akasaka R, Toyama M, Terada T, Shirouzu M, Shindo T, Yokoyama S: Crystal structure of the human receptor activity-modifying protein 1 extracellular domain. Protein Sci. 2008 Nov;17(11):1907-14. doi: 10.1110/ps.036012.108. Epub 2008 Aug 25. [Article]
  4. ter Haar E, Koth CM, Abdul-Manan N, Swenson L, Coll JT, Lippke JA, Lepre CA, Garcia-Guzman M, Moore JM: Crystal structure of the ectodomain complex of the CGRP receptor, a class-B GPCR, reveals the site of drug antagonism. Structure. 2010 Sep 8;18(9):1083-93. doi: 10.1016/j.str.2010.05.014. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Pramlintideapproved, investigationalyestargetagonistDetails