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ryanodine receptor 1; RYR-1; RyR1; skeletal muscle-type ryanodine receptor; skeletal muscle Ca+2 release channel (RYR1, RYDR)

Function: - communication between transverse-tubules & sarcoplasmic reticulum - contraction of skeletal muscle is triggered by release of Ca+2 from SR following depolarization of T-tubules - mechanically coupled to plasma membrane Ca+2 channel in skeletal muscle - Ca+2 release channel is modulated by Ca+2, Mg+2, ATP & calmodulin Structure: - homotetramer (putative) - belongs to the ryanodine receptor family - homologous to IP3 receptor sarcoplasmic reticulum Ca+2 release channel - contains 3 B30.2/SPRY domains - contains 5 MIR domains - Ca+2 release channel activity resides in the C-terminal region while the remaining part of the protein constitutes the 'foot' structure spanning the junctional gap between the SR & the T-tubule; it is possible that the foot structure interacts with the cytoplasmic region of the dihydropyridine receptor Compartment: membrane Alternative splicing: named isoforms=3 Expression: - skeletal muscle & brain (cerebellum & hippocampus) Pathology: - defects in RYR1 are the cause of a) malignant hyperthermia susceptibility type 1 b) central core disease of muscle c) multiminicore disease with external ophthalmoplegia

Related

ryanodine RYR1 gene mutation

General

glycoprotein phosphoprotein ryanodine receptor (RyR)

Properties

SIZE: entity length = 5038 aa MW = 565 kD COMPARTMENT: cellular membrane MOTIF: cytoplasmic domain {1-3123} MOTIF: MIR 1 {97-152} MIR 2 {159-204} MIR 3 {210-264} MIR 4 {270-327} MIR 5 {335-392} B30.2/SPRY 1 {581-797} 6 X approximate repeats {841-2959} consensus repeat {841-954} consensus repeat {955-1068} B30.2/SPRY 2 {1013-1208} consensus repeat {1344-1359} B30.2/SPRY 3 {1356-1570} consensus repeat {1372-1387} glutamate-rich region {1873-1924} MOTIF: glutamate residue (SEVERAL) consensus repeat {2726-2845} Ser phosphorylation site {S2843} consensus repeat {2846-2959} transmembrane domain {3124-3144} exoplasmic loop {3145-3187} transmembrane domain {3188-3206} cytoplasmic loop {3207-3983} MOTIF: N-glycosylation site {N3466} N-glycosylation site {N3474} N-glycosylation site {N3908} N-glycosylation site {N3949} Ser phosphorylation site {S3951} transmembrane domain {3984-4003} exoplasmic loop {4004-4021} transmembrane domain {4022-4040} cytoplasmic loop {4041-4277} MOTIF: N-glycosylation site {N4148} transmembrane domain {4278-4301} exoplasmic loop {4302-4342} MOTIF: Thr phosphorylation site {T4324} transmembrane domain {4343-4363} cytoplasmic loop {4364-4559} MOTIF: proline-rich region SITE: 4462-4532 MOTIF: proline residue (SEVERAL) transmembrane domain {4560-4581} exoplasmic loop {4582-4648} transmembrane domain {4649-4672} cytoplasmic loop {4673-4789} transmembrane domain {4790-4810} exoplasmic loop {4811-4837} transmembrane domain {4838-4857} cytoplasmic loop {4858-4879} MOTIF: Tyr phosphorylation site {Y4864} N-glycosylation site {N4865} Ser phosphorylation site {S4867} transmembrane domain {4880-4899} exoplasmic loop {4900-4923} transmembrane domain {4924-4938} cytoplasmic domain {4937-5038} ION-PERMEABILITY: Ca+2

Database Correlations

OMIM correlations MORBIDMAP 180901 UniProt P21817 PFAM correlations Entrez Gene 6261 Kegg hsa:6261

References

  1. Mignery GA, Sdhof TC. The ligand binding site and transduction mechanism in the inositol-1,4,5-triphosphate receptor. EMBO J. 1990 Dec;9(12):3893-8. PMID: 2174351
  2. Taylor CW, Marshall IC. Calcium and inositol 1,4,5-trisphosphate receptors: a complex relationship. Trends Biochem Sci. 1992 Oct;17(10):403-7. Review. Erratum in: Trends Biochem Sci 1992 Dec;17(12):493. PMID: 1333657
  3. Sorrentino V, Volpe P. Ryanodine receptors: how many, where and why? Trends Pharmacol Sci. 1993 Mar;14(3):98-103. Review. PMID: 8387707
  4. UniProt :accession P21817
  5. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=RYR1
  6. Wikipedia; Note: Ryanodine receptor entry http://en.wikipedia.org/wiki/Ryanodine_receptor
  7. Wikipedia; Note: RYR1 entry http://en.wikipedia.org/wiki/RYR1