Homo sapiens Protein: RYR1 | |||||||||||||||||||||||||||||||||||
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Summary | |||||||||||||||||||||||||||||||||||
InnateDB Protein | IDBP-48911.7 | ||||||||||||||||||||||||||||||||||
Last Modified | 2014-10-13 [Report errors or provide feedback] | ||||||||||||||||||||||||||||||||||
Gene Symbol | RYR1 | ||||||||||||||||||||||||||||||||||
Protein Name | ryanodine receptor 1 (skeletal) | ||||||||||||||||||||||||||||||||||
Synonyms | CCO; MHS; MHS1; PPP1R137; RYDR; RYR; RYR-1; SKRR; | ||||||||||||||||||||||||||||||||||
Species | Homo sapiens | ||||||||||||||||||||||||||||||||||
Ensembl Protein | ENSP00000347667 | ||||||||||||||||||||||||||||||||||
InnateDB Gene | IDBG-48907 (RYR1) | ||||||||||||||||||||||||||||||||||
Protein Structure | |||||||||||||||||||||||||||||||||||
UniProt Annotation | |||||||||||||||||||||||||||||||||||
Function | Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity). {ECO:0000250}. | ||||||||||||||||||||||||||||||||||
Subcellular Localization | Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C- terminus seem to be cytoplasmic. | ||||||||||||||||||||||||||||||||||
Disease Associations | Malignant hyperthermia 1 (MHS1) [MIM:145600]: Autosomal dominant pharmacogenetic disorder of skeletal muscle and is one of the main causes of death due to anesthesia. In susceptible people, an MH episode can be triggered by all commonly used inhalational anesthetics such as halothane and by depolarizing muscle relaxants such as succinylcholine. The clinical features of the myopathy are hyperthermia, accelerated muscle metabolism, contractures, metabolic acidosis, tachycardia and death, if not treated with the postsynaptic muscle relaxant, dantrolene. Susceptibility to MH can be determined with the 'in vitro' contracture test (IVCT): observing the magnitude of contractures induced in strips of muscle tissue by caffeine alone and halothane alone. Patients with normal response are MH normal (MHN), those with abnormal response to caffeine alone or halothane alone are MH equivocal (MHE(C) and MHE(H) respectively). {ECO:0000269PubMed:10051009, ECO:0000269PubMed:10484775, ECO:0000269PubMed:10612851, ECO:0000269PubMed:10823104, ECO:0000269PubMed:10888602, ECO:0000269PubMed:11241852, ECO:0000269PubMed:11389482, ECO:0000269PubMed:11525881, ECO:0000269PubMed:11575529, ECO:0000269PubMed:11928716, ECO:0000269PubMed:12059893, ECO:0000269PubMed:12066726, ECO:0000269PubMed:12123492, ECO:0000269PubMed:12208234, ECO:0000269PubMed:12411788, ECO:0000269PubMed:12709367, ECO:0000269PubMed:12883402, ECO:0000269PubMed:1354642, ECO:0000269PubMed:14732627, ECO:0000269PubMed:14985404, ECO:0000269PubMed:15221887, ECO:0000269PubMed:15448513, ECO:0000269PubMed:16163667, ECO:0000269PubMed:1774074, ECO:0000269PubMed:19191329, ECO:0000269PubMed:20142353, ECO:0000269PubMed:7751854, ECO:0000269PubMed:7849712, ECO:0000269PubMed:7881417, ECO:0000269PubMed:8012359, ECO:0000269PubMed:9066328, ECO:0000269PubMed:9138151, ECO:0000269PubMed:9389851, ECO:0000269PubMed:9450902, ECO:0000269PubMed:9497245}. Note=The disease is caused by mutations affecting the gene represented in this entry.Central core disease of muscle (CCD) [MIM:117000]: Autosomal dominant congenital myopathy, but a severe autosomal recessive form also exists. Both clinical and histological variability is observed. Affected individuals typically display hypotonia and proximal muscle weakness in infancy, leading to the delay of motor milestones. The clinical course of the disorder is usually slow or nonprogressive in adulthood, and the severity of the symptoms may vary from normal to significant muscle weakness. Microscopic examination of CCD-affected skeletal muscle reveals a predominance of type I fibers containing amorphous-looking areas (cores) that do not stain with oxidative and phosphorylase histochemical techniques. {ECO:0000269PubMed:10051009, ECO:0000269PubMed:10097181, ECO:0000269PubMed:11113224, ECO:0000269PubMed:11709545, ECO:0000269PubMed:11741831, ECO:0000269PubMed:12112081, ECO:0000269PubMed:12136074, ECO:0000269PubMed:12565913, ECO:0000269PubMed:12566385, ECO:0000269PubMed:12937085, ECO:0000269PubMed:14670767, ECO:0000269PubMed:14985404, ECO:0000269PubMed:17204054, ECO:0000269PubMed:17226826, ECO:0000269PubMed:18253926, ECO:0000269PubMed:18312400, ECO:0000269PubMed:20142353, ECO:0000269PubMed:21674524, ECO:0000269PubMed:7829078, ECO:0000269PubMed:8220422, ECO:0000269PubMed:8220423, ECO:0000269PubMed:9497245}. Note=The disease is caused by mutations affecting the gene represented in this entry.Multiminicore disease with external ophthalmoplegia (MMDO) [MIM:255320]: Clinically heterogeneous neuromuscular disorder. General features include neonatal hypotonia, delayed motor development, and generalized muscle weakness and amyotrophy, which may progress slowly or remain stable. Muscle biopsy shows multiple, poorly circumscribed, short areas of sarcomere disorganization and mitochondria depletion (areas termed minicores) in most muscle fibers. Typically, no dystrophic signs, such as muscle fiber necrosis or regeneration or significant endomysial fibrosis, are present in multiminicore disease. {ECO:0000269PubMed:12719381, ECO:0000269PubMed:16380615}. Note=The disease is caused by mutations affecting the gene represented in this entry.Myopathy, congenital, with fiber-type disproportion (CFTD) [MIM:255310]: A genetically heterogeneous disorder in which there is relative hypotrophy of type 1 muscle fibers compared to type 2 fibers on skeletal muscle biopsy. However, these findings are not specific and can be found in many different myopathic and neuropathic conditions. {ECO:0000269PubMed:20583297}. Note=The disease is caused by mutations affecting the gene represented in this entry.Note=Defects in RYR1 may be a cause of Samaritan myopathy, a congenital myopathy with benign course. Patients display severe hypotonia and respiratory distress at birth. Unlike other congenital myopathies, the health status constantly improves and patients are minimally affected at adulthood. | ||||||||||||||||||||||||||||||||||
Tissue Specificity | Skeletal muscle and brain (cerebellum and hippocampus). {ECO:0000269PubMed:9607712}. | ||||||||||||||||||||||||||||||||||
Comments | |||||||||||||||||||||||||||||||||||
Interactions | |||||||||||||||||||||||||||||||||||
Number of Interactions |
This gene and/or its encoded proteins are associated with 18 experimentally validated interaction(s) in this database.
They are also associated with 16 interaction(s) predicted by orthology.
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Gene Ontology | |||||||||||||||||||||||||||||||||||
Molecular Function |
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Biological Process |
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Cellular Component |
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Protein Structure and Domains | |||||||||||||||||||||||||||||||||||
PDB ID | |||||||||||||||||||||||||||||||||||
InterPro |
IPR000699
RIH (RyR and IP3R Homology) domain IPR001870 B30.2/SPRY domain IPR003032 Ryanodine receptor Ryr IPR003877 SPRY domain IPR005821 Ion transport domain IPR008985 Concanavalin A-like lectin/glucanases superfamily IPR009066 Alpha-2-macroglobulin receptor-associated protein, domain 1 IPR009460 Ryanodine Receptor TM 4-6 IPR013333 Ryanodine receptor IPR013662 RyR/IP3R Homology associated domain IPR014821 Inositol 1,4,5-trisphosphate/ryanodine receptor IPR016093 MIR motif |
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PFAM |
PF01365
PF02026 PF00622 PF00520 PF06400 PF06459 PF08454 PF08709 PF02815 |
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PRINTS |
PR00795
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PIRSF | |||||||||||||||||||||||||||||||||||
SMART |
SM00449
SM00472 |
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TIGRFAMs | |||||||||||||||||||||||||||||||||||
Post-translational Modifications | |||||||||||||||||||||||||||||||||||
Modification | |||||||||||||||||||||||||||||||||||
Cross-References | |||||||||||||||||||||||||||||||||||
SwissProt | P21817 | ||||||||||||||||||||||||||||||||||
PhosphoSite | PhosphoSite-P21817 | ||||||||||||||||||||||||||||||||||
TrEMBL | O75591 | ||||||||||||||||||||||||||||||||||
UniProt Splice Variant | |||||||||||||||||||||||||||||||||||
Entrez Gene | 6261 | ||||||||||||||||||||||||||||||||||
UniGene | Hs.466664 | ||||||||||||||||||||||||||||||||||
RefSeq | NP_001036188 | ||||||||||||||||||||||||||||||||||
HUGO | HGNC:10483 | ||||||||||||||||||||||||||||||||||
OMIM | 180901 | ||||||||||||||||||||||||||||||||||
CCDS | CCDS42563 | ||||||||||||||||||||||||||||||||||
HPRD | 01618 | ||||||||||||||||||||||||||||||||||
IMGT | |||||||||||||||||||||||||||||||||||
EMBL | AC005933 AC011469 AC067969 AF075460 J05200 M91455 S77392 S78717 U48449 U48450 U48451 U48452 U48453 U48454 U48455 U48456 U48457 U48458 U48459 U48460 U48461 U48462 U48463 U48464 U48465 U48466 U48467 U48468 U48469 U48470 U48471 U48472 U48473 U48474 U48475 U48476 U48477 U48478 U48479 U48480 U48481 U48482 U48483 U48484 U48485 U48486 U48487 U48488 U48489 U48490 U48491 U48492 U48493 U48494 U48495 U48496 U48497 U48498 U48499 U48500 U48501 U48502 U48503 U48504 U48505 U48506 U48507 U48508 | ||||||||||||||||||||||||||||||||||
GenPept | AAA60294 AAA60295 AAB21245 AAB34356 AAC26798 AAC51191 AAC71651 AAF66076 | ||||||||||||||||||||||||||||||||||