Ryanodine receptor 3

Ryanodine receptor 3 is one of a class of ryanodine receptors and a protein that in humans is encoded by the RYR3 gene. The protein encoded by this gene is both a calcium channel and a receptor for the plant alkaloid ryanodine. RYR3 and RYR1 control the resting calcium ion concentration in skeletal muscle.

RYR3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4ERV
Identifiers
Aliases	RYR3, RYR-3, ryanodine receptor 3
External IDs	OMIM: 180903; MGI: 99684; HomoloGene: 68151; GeneCards: RYR3; OMA:RYR3 - orthologs
Gene location (Human) Chr. Chromosome 15 (human) Band 15q13.3-q14 Start 33,310,962 bp End 33,866,121 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 E3- E4 Start 112,461,700 bp End 113,047,441 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in thoracic diaphragm sural nerve right hemisphere of cerebellum caudate nucleus putamen right uterine tube nucleus accumbens right frontal lobe body of uterus gastrocnemius muscle Top expressed in olfactory tubercle lateral septal nucleus medial dorsal nucleus subiculum mammillary body nucleus accumbens motor neuron lateral geniculate nucleus globus pallidus substantia nigra More reference expression data BioGPS n/a
Gene ontology Molecular function ryanodine-sensitive calcium-release channel activity calcium channel activity calcium-release channel activity calmodulin binding ion channel activity calcium-induced calcium release activity calcium ion binding Cellular component organelle membrane integral component of membrane membrane intracellular membrane-bounded organelle sarcoplasmic reticulum sarcoplasmic reticulum membrane endoplasmic reticulum perinuclear region of cytoplasm plasma membrane smooth endoplasmic reticulum Z discdkac cytoplasmic vesicle membrane calcium channel complex sarcolemma Biological process cellular response to calcium ion cellular response to magnesium ion regulation of cardiac conduction cellular calcium ion homeostasis ion transport ion transmembrane transport calcium ion transmembrane transport cellular response to caffeine cellular response to ATP protein homotetramerization calcium ion transport negative regulation of cytosolic calcium ion concentration transmembrane transport release of sequestered calcium ion into cytosol Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6263 20192 Ensembl ENSG00000198838 ENSMUSG00000057378 UniProt Q15413 A2AGL3 RefSeq (mRNA) NM_001036 NM_001243996 NM_177652 NM_001319156 RefSeq (protein) NP_001027 NP_001230925 NP_001306085 Location (UCSC) Chr 15: 33.31 – 33.87 Mb Chr 2: 112.46 – 113.05 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

See also

• Ryanodine receptor

Further reading

• Bertocchini F, Ovitt CE, Conti A, et al. (1997). "Requirement for the ryanodine receptor type 3 for efficient contraction in neonatal skeletal muscles". EMBO J. 16 (23): 6956–63. doi:10.1093/emboj/16.23.6956. PMC 1170299. PMID 9384575.
• Bultynck G, De Smet P, Rossi D, et al. (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. 354 (Pt 2): 413–22. doi:10.1042/bj3540413. PMC 1221670. PMID 11171121.
• Schwarzmann N, Kunerth S, Weber K, et al. (2002). "Knock-down of the type 3 ryanodine receptor impairs sustained Ca2+ signaling via the T cell receptor/CD3 complex". J. Biol. Chem. 277 (52): 50636–42. doi:10.1074/jbc.M209061200. PMID 12354756.
• Nakashima Y, Nishimura S, Maeda A, et al. (1997). "Molecular cloning and characterization of a human brain ryanodine receptor". FEBS Lett. 417 (1): 157–62. doi:10.1016/S0014-5793(97)01275-1. PMID 9395096. S2CID 21591492.
• Xiao B, Masumiya H, Jiang D, et al. (2002). "Isoform-dependent formation of heteromeric Ca2+ release channels (ryanodine receptors)". J. Biol. Chem. 277 (44): 41778–85. doi:10.1074/jbc.M208210200. PMID 12213830.
• Davis MR, Haan E, Jungbluth H, et al. (2003). "Principal mutation hotspot for central core disease and related myopathies in the C-terminal transmembrane region of the RYR1 gene". Neuromuscul. Disord. 13 (2): 151–7. doi:10.1016/S0960-8966(02)00218-3. PMID 12565913. S2CID 30235519.
• Kitahara K, Kawa S, Katsuyama Y, et al. (2008). "Microsatellite scan identifies new candidate genes for susceptibility to alcoholic chronic pancreatitis in Japanese patients". Dis. Markers. 25 (3): 175–80. doi:10.1155/2008/426764. PMC 3827802. PMID 19096130.
• Tochigi M, Kato C, Ohashi J, et al. (2008). "No association between the ryanodine receptor 3 gene and autism in a Japanese population". Psychiatry Clin. Neurosci. 62 (3): 341–4. doi:10.1111/j.1440-1819.2008.01802.x. PMID 18588595.
• Masumiya H, Yamamoto H, Hemberger M, et al. (2003). "The mouse sino-atrial node expresses both the type 2 and type 3 Ca(2+) release channels/ryanodine receptors". FEBS Lett. 553 (1–2): 141–4. Bibcode:2003FEBSL.553..141M. doi:10.1016/S0014-5793(03)00999-2. PMID 14550562. S2CID 20575812.
• Jiang D, Xiao B, Li X, Chen SR (2003). "Smooth muscle tissues express a major dominant negative splice variant of the type 3 Ca2+ release channel (ryanodine receptor)". J. Biol. Chem. 278 (7): 4763–9. doi:10.1074/jbc.M210410200. PMID 12471029.
• Mohaupt MG, Karas RH, Babiychuk EB, et al. (2009). "Association between statin-associated myopathy and skeletal muscle damage". Canadian Medical Association Journal. 181 (1–2): E11–8. doi:10.1503/cmaj.081785. PMC 2704421. PMID 19581603.
• Balschun D, Wolfer DP, Bertocchini F, et al. (1999). "Deletion of the ryanodine receptor type 3 (RyR3) impairs forms of synaptic plasticity and spatial learning". EMBO J. 18 (19): 5264–73. doi:10.1093/emboj/18.19.5264. PMC 1171597. PMID 10508160.
• Martin C, Chapman KE, Seckl JR, Ashley RH (1998). "Partial cloning and differential expression of ryanodine receptor/calcium-release channel genes in human tissues including the hippocampus and cerebellum". Neuroscience. 85 (1): 205–16. doi:10.1016/S0306-4522(97)00612-X. PMID 9607712. S2CID 25634042.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Van Acker K, Bultynck G, Rossi D, et al. (2004). "The 12 kDa FK506-binding protein, FKBP12, modulates the Ca(2+)-flux properties of the type-3 ryanodine receptor". J. Cell Sci. 117 (Pt 7): 1129–37. doi:10.1242/jcs.00948. PMID 14970260.
• Bultynck G, Rossi D, Callewaert G, et al. (2001). "The conserved sites for the FK506-binding proteins in ryanodine receptors and inositol 1,4,5-trisphosphate receptors are structurally and functionally different". J. Biol. Chem. 276 (50): 47715–24. doi:10.1074/jbc.M106573200. PMID 11598113.
• Leeb T, Brenig B (1998). "cDNA cloning and sequencing of the human ryanodine receptor type 3 (RYR3) reveals a novel alternative splice site in the RYR3 gene". FEBS Lett. 423 (3): 367–70. Bibcode:1998FEBSL.423..367L. doi:10.1016/S0014-5793(98)00124-0. PMID 9515741. S2CID 19974365.
• Lynn S, Morgan JM, Lamb HK, et al. (1995). "Isolation and partial cloning of ryanodine-sensitive Ca2+ release channel protein isoforms from human myometrial smooth muscle". FEBS Lett. 372 (1): 6–12. Bibcode:1995FEBSL.372....6L. doi:10.1016/0014-5793(95)00924-X. PMID 7556644. S2CID 41319934.

External links

• RYR3+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)