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edit Ryanodine receptor 1 (skeletal) PDB rendering based on 2bcx. Available structures PDB 2bcx Identifiers Symbols RYR1; CCO; MHS; MHS1; RYDR; RYR; SKRR External IDs OMIM: 180901 MGI: 99659 HomoloGene: 68069 GeneCards: RYR1 Gene Gene Ontology Molecular function • receptor activity • ion channel activity • ryanodine-sensitive calcium-release channel activity • calcium ion binding • calcium-release channel activity Cellular component • smooth endoplasmic reticulum • integral to plasma membrane • membrane Biological process • ion transport • calcium ion transport • cellular calcium ion homeostasis • muscle contraction Sources: Amigo / QuickGO RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 6261 20190 Ensembl ENSG00000196218 ENSMUSG00000030592 UniProt P21817 P70272 RefSeq (mRNA) NM_000540 NM_009109 RefSeq (protein) NP_000531 NP_033135 Location (UCSC) Chr 19: 43.62 - 43.77 Mb Chr 7: 28.71 - 28.83 Mb PubMed search [1] [2] Ryanodine receptor 1 (RYR-1) also known as skeletal muscle calcium release channel or skeletal muscle-type ryanodine receptor is a protein primarily found in skeletal muscle. In humans, it is encoded by the RYR1 gene.[1][2] Contents 1 Function 2 Clinical significance 3 Interactions 4 See also 5 References 6 Further reading 7 External links Function RYR1 functions as a calcium release channel in the sarcoplasmic reticulum, as well as a connection between the sarcoplasmic reticulum and the transverse tubule.[3] Clinical significance Mutations in the RYR1 gene are associated with malignant hyperthermia susceptibility, central core disease, and minicore myopathy with external ophthalmoplegia. Alternatively spliced transcripts encoding different isoforms have been described.[3] Interactions RYR1 has been shown to interact with: calmodulin,[4][5] FKBP1A,[6][7][8] HOMER1,[9][10] HOMER2,[10] HOMER3,[10] and TRDN.[11][12][13][14] See also Ryanodine receptor References ^ Fujii J, Otsu K, Zorzato F, de Leon S, Khanna VK, Weiler JE, O'Brien PJ, MacLennan DH (Aug 1991). "Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia". Science 253 (5018): 448–51. doi:10.1126/science.1862346. PMID 1862346.  ^ Wu S, Ibarra MC, Malicdan MC, Murayama K, Ichihara Y, Kikuchi H, Nonaka I, Noguchi S, Hayashi YK, Nishino I (Jun 2006). "Central core disease is due to RYR1 mutations in more than 90% of patients". Brain 129 (Pt 6): 1470–80. doi:10.1093/brain/awl077. PMID 16621918.  ^ a b "Entrez Gene: RYR1 ryanodine receptor 1 (skeletal)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6261.  ^ Fruen BR, Balog EM, Schafer J, Nitu FR, Thomas DD, Cornea RL (January 2005). "Direct detection of calmodulin tuning by ryanodine receptor channel targets using a Ca2+-sensitive acrylodan-labeled calmodulin". Biochemistry 44 (1): 278–84. doi:10.1021/bi048246u. PMID 15628869.  ^ Cornea RL, Nitu F, Gruber S, Kohler K, Satzer M, Thomas DD, Fruen BR (April 2009). "FRET-based mapping of calmodulin bound to the RyR1 Ca2+ release channel". Proc. Natl. Acad. Sci. U.S.A. 106 (15): 6128–33. doi:10.1073/pnas.0813010106. PMC 2662960. PMID 19332786.  ^ Avila, Guillermo; Lee Eun Hui, Perez Claudio F, Allen P D, Dirksen Robert T (Jun. 2003). "FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes". J. Biol. Chem. (United States) 278 (25): 22600–8. doi:10.1074/jbc.M205866200. ISSN 0021-9258. PMID 12704193.  ^ Bultynck, G; De Smet P, Rossi D, Callewaert G, Missiaen L, Sorrentino V, De Smedt H, Parys J B (Mar. 2001). "Characterization and mapping of the 12 kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor". Biochem. J. (England) 354 (Pt 2): 413–22. doi:10.1042/0264-6021:3540413. ISSN 0264-6021. PMC 1221670. PMID 11171121.  ^ Gaburjakova, M; Gaburjakova J, Reiken S, Huang F, Marx S O, Rosemblit N, Marks A R (May. 2001). "FKBP12 binding modulates ryanodine receptor channel gating". J. Biol. Chem. (United States) 276 (20): 16931–5. doi:10.1074/jbc.M100856200. ISSN 0021-9258. PMID 11279144.  ^ Hwang SY, Wei J, Westhoff JH, Duncan RS, Ozawa F, Volpe P, Inokuchi K, Koulen P (August 2003). "Differential functional interaction of two Vesl/Homer protein isoforms with ryanodine receptor type 1: a novel mechanism for control of intracellular calcium signaling". Cell Calcium 34 (2): 177–84. doi:10.1016/S0143-4160(03)00082-4. PMID 12810060.  ^ a b c Feng W, Tu J, Yang T, Vernon PS, Allen PD, Worley PF, Pessah IN (November 2002). "Homer regulates gain of ryanodine receptor type 1 channel complex". J. Biol. Chem. 277 (47): 44722–30. doi:10.1074/jbc.M207675200. PMID 12223488.  ^ Lee JM, Rho SH, Shin DW, Cho C, Park WJ, Eom SH, Ma J, Kim DH (February 2004). "Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin". J. Biol. Chem. 279 (8): 6994–7000. doi:10.1074/jbc.M312446200. PMID 14638677.  ^ Caswell AH, Motoike HK, Fan H, Brandt NR (January 1999). "Location of ryanodine receptor binding site on skeletal muscle triadin". Biochemistry 38 (1): 90–7. doi:10.1021/bi981306. PMID 9890886.  ^ Guo W, Campbell KP (April 1995). "Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum". J. Biol. Chem. 270 (16): 9027–30. doi:10.1074/jbc.270.16.9027. PMID 7721813.  ^ Groh S, Marty I, Ottolia M, Prestipino G, Chapel A, Villaz M, Ronjat M (April 1999). "Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor". J. Biol. Chem. 274 (18): 12278–83. doi:10.1074/jbc.274.18.12278. PMID 10212196.  Further reading Treves S, Anderson AA, Ducreux S, et al. (2005). "Ryanodine receptor 1 mutations, dysregulation of calcium homeostasis and neuromuscular disorders.". Neuromuscul. Disord. 15 (9-10): 577–87. doi:10.1016/j.nmd.2005.06.008. PMID 16084090.  External links MeSH RYR1+protein,+human GeneReviews/NIH/UW entry on Multiminicore Disease GeneReviews/NCBI/NIH/UW entry on Malignant Hyperthermia Susceptibility RYR1 Variation Database v · d · ePDB gallery 2bcx: Crystal structure of calmodulin in complex with a ryanodine receptor peptide   v · d · eMembrane transport protein: ion channels (TC 1A)  Ca2+: Calcium channel Voltage-gated L-type/Cavα (1.1, 1.2, 1.3, 1.4) · N-type/Cavα2.2 · P-type/Cavα(2.1) · Q-type/Cavα2.1 · R-type/Cavα2.3 · T-type/Cavα(3.1, 3.2, 3.3) α2δ-subunits (1, 2) · β-subunits (β1, β2, β3, β4) · γ-subunits (γ1, γ2, γ3, γ4) Cation channels of sperm (1, 2, 3, 4) · Two-pore channel (1, 2) Ligand-gated Inositol trisphosphate receptor (1, 2, 3) · Ryanodine receptor (1, 2, 3)  Na+: Sodium channel Voltage-gated Navα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) · Navβ (1, 2, 3, 4) Constitutively active Epithelial sodium channel (α, β, γ, δ)  K+: Potassium channel Voltage-gated Kvα1-6 (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8) · (2.1, 2.2) · (3.1, 3.2, 3.3, 3.4) · (4.1, 4.2, 4.3) · (5.1) · (6.1, 6.2, 6.3, 6.4) Kvα7-12 (7.1, 7.2, 7.3, 7.4, 7.5) · (8.1, 8.2) · (9.1, 9.2, 9.3) · (10.1, 10.2) · (11.1/hERG, 11.2, 11.3) · (12.1, 12.2, 12.3) Kvβ (1, 2, 3) · KCNIP (1, 2, 3, 4) · minK/ISK · minK/ISK-like · MiRP (1, 2, 3) · Shaker gene Calcium-activated BK channel (α1, β1, β2, β3, β4) · SK channel (SK1, SK2, SK3, SK4) · KCa (1.1, 2.1, 2.2, 2.3, 3.1, 4.1, 4.2, 5.1) Inward-rectifier KATP · Kir (1.1, 2.1, 2.2, 2.3, 2.4, 2.6) · GIRK/Kir (3.1, 3.2, 3.3, 3.4) · Kir (4.1, 4.2, 5.1, 6.1, 6.2, 7.1) Tandem pore domain K2P (1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)  Other M+: TRP cation channel TRPA (1) · TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) · TRPM (1, 2, 3, 4, 5, 6, 7, 8) · TRPML (1, 2, 3) · TRPP (1, 2) · TRPV (1, 2, 3, 4, 5, 6) Cl-: Chloride channel ANO1 · Bestrophin (1, 2) · CFTR · CLCA (1, 2, 3, 4) · CLCN (1, 2, 3, 4, 5, 6, 7, KA, KB) · CLIC (1, 2, 3, 4, 5, 6, L1) · CLNS (1A, 1B) Cyclic nucleotide-gated (FC) α (1, 2, 3, 4) · β (1, 2, 3) · HCN (1, 2, 3, 4) Porin Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) · Voltage-dependent anion channel (1, 2, 3) · General bacterial porin family Gap junction Connexin: A (GJA1, GJA3, GJA4, GJA5, GJA8, GJA9, GJA10) · B (GJB1, GJB2, GJB3, GJB4, GJB5, GJB6, GJB7) · C (GJC1, GJC2, GJC3) · D (GJD2, GJD3, GJD4) · E (GJE1) Innexin General Ligand-gated ion channel · Voltage-gated ion channel · Stretch-activated ion channel see also disorders B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr This article incorporates text from the United States National Library of Medicine, which is in the public domain. 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