Receptor activity-modifying protein 1

Details

Name
Receptor activity-modifying protein 1
Synonyms
  • Calcitonin-receptor-like receptor activity-modifying protein 1
  • CRLR activity-modifying protein 1
Gene Name
RAMP1
Organism
Humans
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
calcitonin receptor activity / calcitonin receptor binding / coreceptor activity / protein transporter activity / receptor activity
Processes
angiogenesis / calcium ion transport / cellular response to hormone stimulus / intracellular protein transport / positive regulation of cAMP biosynthetic process / positive regulation of protein glycosylation / protein localization to plasma membrane / protein transport / receptor internalization / regulation of G-protein coupled receptor protein signaling pathway
Components
cell surface / extracellular space / integral component of plasma membrane / intracellular / plasma membrane / receptor complex
General Function
Receptor activity
Specific 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.
Pfam Domain Function
Transmembrane Regions
118-138
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0001711|447 bp
ATGGCCCGGGCCCTGTGCCGCCTCCCGCGGCGCGGCCTCTGGCTGCTCCTGGCCCATCAC
CTCTTCATGACCACTGCCTGCCAGGAGGCTAACTACGGTGCCCTCCTCCGGGAGCTCTGC
CTCACCCAGTTCCAGGTAGACATGGAGGCCGTCGGGGAGACGCTGTGGTGTGACTGGGGC
AGGACCATCAGGAGCTACAGGGAGCTGGCCGACTGCACCTGGCACATGGCGGAGAAGCTG
GGCTGCTTCTGGCCCAATGCAGAGGTGGACAGGTTCTTCCTGGCAGTGCATGGCCGCTAC
TTCAGGAGCTGCCCCATCTCAGGCAGGGCCGTGCGGGACCCGCCCGGCAGCATCCTCTAC
CCCTTCATCGTGGTCCCCATCACGGTGACCCTGCTGGTGACGGCACTGGTGGTCTGGCAG
AGCAAGCGCACTGAGGGCATTGTGTAG
Chromosome Location
Not Available
Locus
2q36-q37.1
External Identifiers
ResourceLink
UniProtKB IDO60894
UniProtKB Entry NameRAMP1_HUMAN
GenBank Protein ID3171910
GenBank Gene IDAJ001014
GenAtlas IDRAMP1
HGNC IDHGNC:9843
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. [PubMed:9620797]
  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. [PubMed:15489334]
  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. [PubMed:18725456]
  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. [PubMed:20826335]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01278Pramlintideapproved, investigationalyesagonistDetails