RYR1_MOUSE
ID RYR1_MOUSE Reviewed; 5035 AA.
AC E9PZQ0; Q60834; Q61779; Q61780; Q62173; Q62196; Q62235; Q78EJ6; Q7TNG1;
AC Q80UQ5; Q80X16; Q99JF9;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ryanodine receptor 1;
DE Short=RYR-1;
DE Short=RyR1;
DE AltName: Full=Skeletal muscle calcium release channel;
DE AltName: Full=Skeletal muscle ryanodine receptor;
DE AltName: Full=Skeletal muscle-type ryanodine receptor;
DE AltName: Full=Type 1 ryanodine receptor;
GN Name=Ryr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ILE-4895.
RC STRAIN=BALB/c X CD-1;
RX PubMed=18003898; DOI=10.1073/pnas.0709312104;
RA Zvaritch E., Depreux F., Kraeva N., Loy R.E., Goonasekera S.A.,
RA Boncompagni S., Kraev A., Gramolini A.O., Dirksen R.T.,
RA Franzini-Armstrong C., Seidman C.E., Seidman J.G., MacLennan D.H.;
RT "An Ryr1I4895T mutation abolishes Ca2+ release channel function and delays
RT development in homozygous offspring of a mutant mouse line.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18537-18542(2007).
RN [2]
RP ERRATUM OF PUBMED:18003898.
RA Zvaritch E., Depreux F., Kraeva N., Loy R.E., Goonasekera S.A.,
RA Boncompagni S., Kraev A., Gramolini A.O., Dirksen R.T.,
RA Franzini-Armstrong C., Seidman C.E., Seidman J.G., MacLennan D.H.;
RL Proc. Natl. Acad. Sci. U.S.A. 105:825-825(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-27, FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=129/J, and BALB/cJ; TISSUE=Skeletal muscle;
RX PubMed=7515481; DOI=10.1038/369556a0;
RA Takeshima H., Iino M., Takekura H., Nishi M., Kuno J., Minowa O.,
RA Takano H., Noda T.;
RT "Excitation-contraction uncoupling and muscular degeneration in mice
RT lacking functional skeletal muscle ryanodine-receptor gene.";
RL Nature 369:556-559(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 483-861.
RC STRAIN=129;
RA Kathirvel P.;
RT "Characterisation of the murine Ryr1 gene.";
RL Thesis (2000), University of Edinburgh, United Kingdom.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4500-5035.
RC STRAIN=FVB/N-3; TISSUE=Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4537-5035, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=7876312; DOI=10.1083/jcb.128.5.893;
RA Giannini G., Conti A., Mammarella S., Scrobogna M., Sorrentino V.;
RT "The ryanodine receptor/calcium channel genes are widely and differentially
RT expressed in murine brain and peripheral tissues.";
RL J. Cell Biol. 128:893-904(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4762-5013.
RC TISSUE=Brain;
RX PubMed=7635066; DOI=10.1242/dev.121.7.2233;
RA Ayabe T., Kopf G.S., Schultz R.M.;
RT "Regulation of mouse egg activation: presence of ryanodine receptors and
RT effects of microinjected ryanodine and cyclic ADP ribose on uninseminated
RT and inseminated eggs.";
RL Development 121:2233-2244(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4913-5035, FUNCTION, SUBCELLULAR LOCATION,
RP DOMAIN, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX PubMed=7621815; DOI=10.1002/j.1460-2075.1995.tb07302.x;
RA Takeshima H., Yamazawa T., Ikemoto T., Takekura H., Nishi M., Noda T.,
RA Iino M.;
RT "Ca(2+)-induced Ca2+ release in myocytes from dyspedic mice lacking the
RT type-1 ryanodine receptor.";
RL EMBO J. 14:2999-3006(1995).
RN [10]
RP SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, AND DOMAIN.
RX PubMed=7724570; DOI=10.1073/pnas.92.8.3381;
RA Takekura H., Nishi M., Noda T., Takeshima H., Franzini-Armstrong C.;
RT "Abnormal junctions between surface membrane and sarcoplasmic reticulum in
RT skeletal muscle with a mutation targeted to the ryanodine receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3381-3385(1995).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT SER-2844, S-NITROSYLATION, AND IDENTIFICATION
RP IN A COMPLEX WITH PDE4D; PKA; FKBP1A AND PROTEIN PHOSPHATASE 1.
RX PubMed=18268335; DOI=10.1073/pnas.0711074105;
RA Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W.,
RA Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.;
RT "Remodeling of ryanodine receptor complex causes 'leaky' channels: a
RT molecular mechanism for decreased exercise capacity.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2844, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION IN BRAIN, S-NITROSYLATION, ACTIVITY REGULATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22036948; DOI=10.1038/emboj.2011.386;
RA Kakizawa S., Yamazawa T., Chen Y., Ito A., Murayama T., Oyamada H.,
RA Kurebayashi N., Sato O., Watanabe M., Mori N., Oguchi K., Sakurai T.,
RA Takeshima H., Saito N., Iino M.;
RT "Nitric oxide-induced calcium release via ryanodine receptors regulates
RT neuronal function.";
RL EMBO J. 31:417-428(2012).
RN [14]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF ARG-165, AND PHOSPHORYLATION AT SER-2844.
RX PubMed=21156754; DOI=10.1124/mol.110.067959;
RA Feng W., Barrientos G.C., Cherednichenko G., Yang T., Padilla I.T.,
RA Truong K., Allen P.D., Lopez J.R., Pessah I.N.;
RT "Functional and biochemical properties of ryanodine receptor type 1
RT channels from heterozygous R163C malignant hyperthermia-susceptible mice.";
RL Mol. Pharmacol. 79:420-431(2011).
RN [15]
RP REVIEW.
RX PubMed=20214899; DOI=10.1016/j.febslet.2010.03.005;
RA Kushnir A., Betzenhauser M.J., Marks A.R.;
RT "Ryanodine receptor studies using genetically engineered mice.";
RL FEBS Lett. 584:1956-1965(2010).
CC -!- FUNCTION: Calcium channel that mediates the release of Ca(2+) from the
CC sarcoplasmic reticulum into the cytoplasm and thereby plays a key role
CC in triggering muscle contraction following depolarization of T-tubules
CC (PubMed:18003898, PubMed:7515481, PubMed:7621815, PubMed:21156754).
CC Repeated very high-level exercise increases the open probability of the
CC channel and leads to Ca(2+) leaking into the cytoplasm
CC (PubMed:18268335). Can also mediate the release of Ca(2+) from
CC intracellular stores in neurons, and may thereby promote prolonged
CC Ca(2+) signaling in the brain (PubMed:22036948). Required for normal
CC embryonic development of muscle fibers and skeletal muscle
CC (PubMed:7515481). Required for normal heart morphogenesis, skin
CC development and ossification during embryogenesis (PubMed:18003898,
CC PubMed:7515481). {ECO:0000269|PubMed:18003898,
CC ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754,
CC ECO:0000269|PubMed:22036948, ECO:0000269|PubMed:7515481,
CC ECO:0000269|PubMed:7621815}.
CC -!- ACTIVITY REGULATION: Channel activity is modulated by the alkaloid
CC ryanodine that binds to the open Ca-release channel with high affinity.
CC At low concentrations, ryanodine maintains the channel in an open
CC conformation. High ryanodine concentrations inhibit channel activity
CC (PubMed:7621815). Channel activity is regulated by calmodulin (CALM).
CC The calcium release is activated by increased cytoplasmic calcium
CC levels, by nitric oxyde (NO), caffeine and ATP (PubMed:7621815,
CC PubMed:22036948, PubMed:21156754). Channel activity is inhibited by
CC magnesium ions, possibly by competition for calcium binding sites.
CC {ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:7621815}.
CC -!- SUBUNIT: Homotetramer (PubMed:18003898). Can also form heterotetramers
CC with RYR2 (By similarity). Identified in a complex composed of RYR1,
CC PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) (PubMed:18268335).
CC Repeated very high-level exercise decreases interaction with PDE4D and
CC protein phosphatase 1 (PP1) (PubMed:18268335). Interacts with CALM;
CC CALM with bound calcium inhibits the RYR1 channel activity (By
CC similarity). Interacts with S100A1 (By similarity). Interacts with
CC FKBP1A; this stabilizes the closed conformation of the channel.
CC Interacts with CACNA1S; interaction with CACNA1S is important for
CC activation of the RYR1 channel. Interacts with CACNB1. Interacts with
CC TRDN and ASPH; these interactions stimulate RYR1 channel activity.
CC Interacts with SELENON (By similarity). Interacts with scorpion calcins
CC (AC P0DPT1; AC P0DM30; AC A0A1L4BJ42; AC P59868; AC P60254; AC B8QG00;
CC AC L0GBR1; AC P60252; AC P60253) (By similarity).
CC {ECO:0000250|UniProtKB:P11716, ECO:0000250|UniProtKB:P21817,
CC ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:18268335}.
CC -!- INTERACTION:
CC E9PZQ0; O55108: Bsg; NbExp=3; IntAct=EBI-642079, EBI-643315;
CC E9PZQ0; P49070: Camlg; NbExp=3; IntAct=EBI-642079, EBI-309114;
CC E9PZQ0; P26883: Fkbp1a; NbExp=2; IntAct=EBI-642079, EBI-6379901;
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:7621815}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:18003898}. Membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Sarcoplasmic reticulum
CC {ECO:0000250|UniProtKB:P11716}. Note=The number of predicted
CC transmembrane domains varies between orthologs, but the 3D-structures
CC show the presence of six transmembrane regions. Both N-terminus and C-
CC terminus are cytoplasmic. {ECO:0000250|UniProtKB:P11716}.
CC -!- TISSUE SPECIFICITY: Detected in muscle and myotubes (at protein level)
CC (PubMed:18003898). Ubiquitous. Detected in diaphragm, skeletal muscle,
CC esophagus, spleen, submaxillary gland, adrenal gland, cerebellum, brain
CC and in testis germ cells. {ECO:0000269|PubMed:18003898,
CC ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:22036948,
CC ECO:0000269|PubMed:7621815, ECO:0000269|PubMed:7876312}.
CC -!- DOMAIN: The calcium release channel activity resides in the C-terminal
CC region while the remaining part of the protein constitutes the 'foot'
CC structure spanning the junctional gap between the sarcoplasmic
CC reticulum (SR) and the T-tubule (PubMed:7621815, PubMed:7724570). Pore
CC opening is mediated via the cytoplasmic calcium-binding domains that
CC mediate a small rotation of the channel-forming transmembrane regions
CC that then leads to channel opening (By similarity).
CC {ECO:0000250|UniProtKB:P11716, ECO:0000269|PubMed:7621815,
CC ECO:0000269|PubMed:7724570}.
CC -!- PTM: Channel activity is modulated by phosphorylation. Phosphorylation
CC at Ser-2844 may increase channel activity. Repeated very high-level
CC exercise increases phosphorylation at Ser-2844.
CC {ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754}.
CC -!- PTM: Activated by reversible S-nitrosylation (PubMed:22036948).
CC Repeated very high-level exercise increases S-nitrosylation.
CC {ECO:0000250, ECO:0000269|PubMed:18268335,
CC ECO:0000269|PubMed:22036948}.
CC -!- DISRUPTION PHENOTYPE: Perinatal lethality, due to severe defects in
CC skeletal muscle development. Neonates do not breathe and do not move.
CC Mutant mice show defects in muscle fiber development. Their muscles do
CC not show a contractile response to electrical stimulation. In addition,
CC mice display abnormal curvature of the spine, thin limbs, and an
CC abnormal rib cage. {ECO:0000269|PubMed:7515481}.
CC -!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR1
CC subfamily. {ECO:0000305}.
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DR EMBL; AY268935; AAP29981.1; -; mRNA.
DR EMBL; AC164564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D21798; BAA21010.1; -; Genomic_DNA.
DR EMBL; D21796; BAA04821.1; -; mRNA.
DR EMBL; D21797; BAA04822.1; -; Genomic_DNA.
DR EMBL; AJ308737; CAC34624.1; -; Genomic_DNA.
DR EMBL; BC051248; AAH51248.1; -; mRNA.
DR EMBL; BC055487; AAH55487.1; -; mRNA.
DR EMBL; X83932; CAA58784.1; -; mRNA.
DR EMBL; U23754; AAA64955.1; -; mRNA.
DR EMBL; D38216; BAA07391.1; -; mRNA.
DR CCDS; CCDS39866.1; -.
DR PIR; I48741; I48741.
DR PIR; I58087; I58087.
DR PIR; I78376; I78376.
DR PIR; I78377; I78377.
DR PIR; S56105; S56105.
DR RefSeq; NP_033135.2; NM_009109.2.
DR SMR; E9PZQ0; -.
DR BioGRID; 203045; 10.
DR ComplexPortal; CPX-3092; Ryanodine 1 complex.
DR DIP; DIP-29705N; -.
DR IntAct; E9PZQ0; 29.
DR MINT; E9PZQ0; -.
DR STRING; 10090.ENSMUSP00000137123; -.
DR BindingDB; E9PZQ0; -.
DR ChEMBL; CHEMBL2133; -.
DR iPTMnet; E9PZQ0; -.
DR PhosphoSitePlus; E9PZQ0; -.
DR MaxQB; E9PZQ0; -.
DR PaxDb; E9PZQ0; -.
DR PeptideAtlas; E9PZQ0; -.
DR PRIDE; E9PZQ0; -.
DR ProteomicsDB; 256854; -.
DR Antibodypedia; 44914; 174 antibodies from 24 providers.
DR DNASU; 20190; -.
DR Ensembl; ENSMUST00000179893; ENSMUSP00000137123; ENSMUSG00000030592.
DR GeneID; 20190; -.
DR KEGG; mmu:20190; -.
DR UCSC; uc009gao.1; mouse.
DR CTD; 6261; -.
DR MGI; MGI:99659; Ryr1.
DR VEuPathDB; HostDB:ENSMUSG00000030592; -.
DR eggNOG; KOG2243; Eukaryota.
DR GeneTree; ENSGT00940000155288; -.
DR InParanoid; E9PZQ0; -.
DR PhylomeDB; E9PZQ0; -.
DR TreeFam; TF315244; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 20190; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ryr1; mouse.
DR PRO; PR:E9PZQ0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9PZQ0; protein.
DR Bgee; ENSMUSG00000030592; Expressed in triceps brachii and 115 other tissues.
DR ExpressionAtlas; E9PZQ0; baseline and differential.
DR Genevisible; E9PZQ0; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0031674; C:I band; ISO:MGI.
DR GO; GO:0031301; C:integral component of organelle membrane; ISS:UniProtKB.
DR GO; GO:0030314; C:junctional membrane complex; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI.
DR GO; GO:0030315; C:T-tubule; IDA:MGI.
DR GO; GO:0014802; C:terminal cisterna; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IMP:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048763; F:calcium-induced calcium release activity; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IMP:UniProtKB.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0071318; P:cellular response to ATP; ISO:MGI.
DR GO; GO:0071313; P:cellular response to caffeine; IMP:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IDA:MGI.
DR GO; GO:0043931; P:ossification involved in bone maturation; IMP:UniProtKB.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0006937; P:regulation of muscle contraction; TAS:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:UniProtKB.
DR GO; GO:0031000; P:response to caffeine; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; ISO:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:UniProtKB.
DR GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR CDD; cd12877; SPRY1_RyR; 1.
DR CDD; cd12878; SPRY2_RyR; 1.
DR CDD; cd12879; SPRY3_RyR; 1.
DR Gene3D; 2.60.120.920; -; 3.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014821; Ins145_P3_rcpt.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR013662; RIH_assoc-dom.
DR InterPro; IPR000699; RIH_dom.
DR InterPro; IPR013333; Ryan_recept.
DR InterPro; IPR003032; Ryanodine_rcpt.
DR InterPro; IPR009460; Ryanrecept_TM4-6.
DR InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR InterPro; IPR033215; RyR1.
DR InterPro; IPR035761; SPRY1_RyR.
DR InterPro; IPR035764; SPRY2_RyR.
DR InterPro; IPR035762; SPRY3_RyR.
DR InterPro; IPR003877; SPRY_dom.
DR PANTHER; PTHR13715:SF15; PTHR13715:SF15; 1.
DR Pfam; PF08709; Ins145_P3_rec; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF08454; RIH_assoc; 1.
DR Pfam; PF06459; RR_TM4-6; 1.
DR Pfam; PF01365; RYDR_ITPR; 2.
DR Pfam; PF02026; RyR; 4.
DR Pfam; PF00622; SPRY; 3.
DR PRINTS; PR00795; RYANODINER.
DR SMART; SM00472; MIR; 4.
DR SMART; SM00449; SPRY; 3.
DR SUPFAM; SSF100909; SSF100909; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49899; SSF49899; 3.
DR SUPFAM; SSF82109; SSF82109; 2.
DR PROSITE; PS50188; B302_SPRY; 3.
DR PROSITE; PS50919; MIR; 5.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Developmental protein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; S-nitrosylation;
KW Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..5035
FT /note="Ryanodine receptor 1"
FT /id="PRO_0000415566"
FT TOPO_DOM 1..4556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TRANSMEM 4557..4577
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TOPO_DOM 4578..4638
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TRANSMEM 4639..4659
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TOPO_DOM 4660..4777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TRANSMEM 4778..4800
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TOPO_DOM 4801
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TRANSMEM 4802..4818
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TOPO_DOM 4819..4833
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TRANSMEM 4834..4854
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TOPO_DOM 4855..4877
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT INTRAMEM 4878..4897
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TOPO_DOM 4898..4917
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TRANSMEM 4918..4938
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT TOPO_DOM 4939..5035
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT DOMAIN 99..154
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 161..206
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 212..266
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 272..329
FT /note="MIR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 337..394
FT /note="MIR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 583..799
FT /note="B30.2/SPRY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REPEAT 843..956
FT /note="1"
FT REPEAT 957..1070
FT /note="2"
FT DOMAIN 1015..1210
FT /note="B30.2/SPRY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REPEAT 1346..1361
FT /note="3; truncated"
FT DOMAIN 1359..1572
FT /note="B30.2/SPRY 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REPEAT 1374..1389
FT /note="4; truncated"
FT REPEAT 2727..2846
FT /note="5"
FT REPEAT 2847..2960
FT /note="6"
FT DOMAIN 4078..4106
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 671..682
FT /note="Interaction with FKBP1A"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT REGION 843..2960
FT /note="6 X approximate repeats"
FT REGION 1309..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2391..2414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2828..2859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3479..3502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3615..3644
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250"
FT REGION 4255..4283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4378..4531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4586..4618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4892..4898
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT COMPBIAS 1372..1387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1874..1923
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2828..2844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4257..4274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4402..4418
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4482..4496
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4497..4513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4514..4528
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3896
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT BINDING 3970
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT BINDING 4214..4218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT BINDING 4714
FT /ligand="caffeine"
FT /ligand_id="ChEBI:CHEBI:27732"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT BINDING 4952..4957
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT BINDING 4977..4983
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT BINDING 4999
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1LMY4"
FT MOD_RES 2346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1LMY4"
FT MOD_RES 2844
FT /note="Phosphoserine; by PKA and PKG"
FT /evidence="ECO:0000269|PubMed:18268335,
FT ECO:0000269|PubMed:21156754, ECO:0007744|PubMed:21183079"
FT MOD_RES 3636
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P11716"
FT MOD_RES 4464
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:F1LMY4"
FT MOD_RES 4468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1LMY4"
FT MOD_RES 4861
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21817"
FT MOD_RES 4864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21817"
FT MUTAGEN 165
FT /note="R->C: Increased channel activity, leading to
FT permanently increased cytoplasmic Ca(2+) levels. Increased
FT activation by calcium, and increased ryanodine binding."
FT /evidence="ECO:0000269|PubMed:21156754"
FT MUTAGEN 4895
FT /note="I->T: Causes paralysis and perinatal death in
FT homozygous mice, apparently due to asphyxia. Mutant mice
FT have greatly reduced and amorphous skeletal muscle."
FT /evidence="ECO:0000269|PubMed:18003898"
FT CONFLICT 616
FT /note="R -> C (in Ref. 5; CAC34624)"
FT /evidence="ECO:0000305"
FT CONFLICT 1380
FT /note="A -> S (in Ref. 1; AAP29981)"
FT /evidence="ECO:0000305"
FT CONFLICT 3484
FT /note="D -> V (in Ref. 1; AAP29981)"
FT /evidence="ECO:0000305"
FT CONFLICT 4766
FT /note="I -> L (in Ref. 8; AAA64955)"
FT /evidence="ECO:0000305"
FT CONFLICT 4821
FT /note="L -> V (in Ref. 7; CAA58784)"
FT /evidence="ECO:0000305"
FT CONFLICT 4888
FT /note="G -> A (in Ref. 7; CAA58784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5035 AA; 565039 MW; D15D2E764B445573 CRC64;
MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL EPTSNAQNVP
PDLAICCFIL EQSLSVRALQ EMLANTVEAG VESSQGGGHR TLLYGHAILL RHAHSRMYLS
CLTTSRSMTD KLAFDVGLQE DATGEACWWT MHPASKQRSE GEKVRVGDDL ILVSVSSERY
LHLSTASGEL QVDASFMQTL WNMNPICSGC EEGFVTGGHV LRLFHGHMDE CLTISPSDSD
DQRRLVYYEG GPVCTHARSL WRLEPLRISW SGSHLRWGQP LRIRHVTTGR YLGLTEDQGL
VVVDASKAHT KATSFCFRIS KEKLDVAPKR DVEGMGPPEI KYGESLCFVQ HVASGLWLTY
AAPDPKALRL GVLKKKAMLH QEGHMDDALS LTRCQQEESQ AARMIYSTAG LYNQFIKGLD
SFSGKPRGSG PPAGSALPIE GVILSLQDLI GYFEPPSEEL QHEEKQTKLR SLRNRQSLFQ
EEGMLSLVLN CIDRLNVYTT AAHFAEFAGE EAAESWKEIV NLLYELLASL IRGNRTNCAL
FSTNLDWLVS KLDRLEASSG ILEVLYCVLI ESPEVLNIIQ ENHIKSIISL LDKHGRNHKV
LDVLCSLCVC NGVAVRSNQD LITENLLPGR ELLLQTNLIN YVTSIRPNIF VGRAEGSTQY
GKWYFEVMVD EVAPFLTAQA THLRVGWALS EGYSPYPGGG EGWGGNGVGD DLYSYGFDGL
HLWTGHVARP VTSPGQHLLA PEDVVSCCLD LSVPSISFRI NGCPVQGVFE SFNLDGLFFP
VVSFSAGIKV RFLLGGRHGE FKFLPPPGYA PCHEAVLPRE RLHLQPIKEY RREGPRGPHL
VGPSRCLSHL DFVPCPVDTI QIVLPPHLER IREKLAENIH ELWALTRIEQ GWTYGPVRDD
NKRLHPCLVN FHSLPEPERN YNLQMSGETL KTLLALGCHV GMADEKAEDN LKKTKLPKTY
MMSNGYKPAP LDLSHVRLTP AQTTLVDRLA ENGHNVWARD RVAQGWSYSA VQDIPARRNP
RLVPYRLLDE ATKRSNRDSL CQAVRTLLGY GYNIEPPDQE PSQVDSQSRG DRARIFRAEK
SYAVQSGRWY FEFEAVTTGE MRVGWARPEL RPDVELGADD LAYVFNGHRG QRWHLGSEPF
GRPWQSGDVV GCMIDLTENT IIFTLNGEVL MSDSGSETAF RDIEIGDGFL PVCSLGPGQV
GHLNLGQDVS SLRFFAICGL QEGFEPFAIN MQRPVTTWFS KSLPQFEPVP LEHPHYEVAR
MDGTVDTPPC LRLTHRTWGS QNSLVEMLFL RLSLPVQFHQ HFRCTAGATP LASPGLQPPA
EDEARAAEPD TDYENLRRSA GGWGEAEGGK DGTAKEGTPG GTAQAGVEAQ PARAENEKDA
TTEKNKKRGF LFKAKKVAMM TQPPSTPALP RLPRDVVPAD NRDDPEIILN TTTYYYSVRV
FAGQEPSCVW VGWVTPDYHQ HDMSFDLSKV RAVTVTMGDE QGNVHSSLKC SNCYMVWGGD
FVSPGQQGRI SHTDLVIGCL VDLATGLMTF TANGKESNTF FQVEPNTKLF PAVFVLPTHQ
NVVQFELGKQ KNIMPLSAAM FLSERKNPAP QCPPRLEVQM LMPVSWSRMP NHFLQVDTRR
AGERLGWAVQ CQEPLMMMAL HIPEENRCMD ILELSERLDL QRFHSHTLSL YRSVCALGNN
RVAHALCSHV DQAQLLHALE DARLPGPLRA GYYDLLISIH LESACRSRRS MLSEYIVPLT
PETRAITLFP PGRSAEDGPR RHGLPGVGVT TSLRPPHHFS PPCFVVALPA AGATEAPARL
SPAIPLEALR DKALRMLGEA VRDGGQHARD PVGGSVEFQF VPVLKLVSTL LVMGVFSDED
VKQILKMIEP EVFREEEEVE EEGEEEEEDE EEKEEDEEEE AHEKEDEEKE EAEDAAEEEK
EELEEGLLQM KLPESVKLQM CHLLEYFCDQ ELQHRVESLA AFAECYVDKM QGNQRGRYGL
LMKAFTMSAA ETARRTREFR SPPQEQINML LHFKNGADEE ECPLPEEIRQ ELVNFHQDLL
AHCGIQLEGE EEEPEEESTL GSRLMSLLEK VKLVKKTEEK PEEEPAPEEH KPQSLQELVS
HTVVRWAQED FVQSPELVRA MFSLLHRQYD GLGELLRALP RAYTISVSSV EDTMSLLECL
GQIRSLLIVQ MGPQEENLMI QSIGNIMNNK VFYQHPNLMR ALGMHETVME VMVNVLGGGE
SKEIRFPKMV TSCCRFLCYF CRISRQNQRS MFDHLSYLLE NSGIGLGMQG STPLDVAAAS
VIDNNELALA LQEQDLEKVV SYLAGCGLQS CPMLLAKGYP DIGWNPCGGE RYLDFLRFAV
FVNGESVEEN ANVVVRLLIR KPECFGPALR GEGGSGLLAA IEEAIRISED PARDGPGVRR
DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE THLIQAGKGE ALRIRAILRS
LVPLDDLVGI ISLPLQIPTL GKDGALVQPK MSASFVPDHK ASMVLFLDRV YGIENQDFLL
HVLDVGFLPD MRAAASLDTA TFSTTEMALA LNRYLCLAVL PLITKCAPLF AGTEHRAIMV
DSMLHTVYRL SRGRSLTKAQ RDVIEDCLMA LCRYIRPSML QHLLRRLVFD VPILNEFAKM
PLKLLTNHYE RCWKYYCLPT GWANFGVTSE EELHLTRKLF WGIFDSLAHK KYDQELYRIA
MPCLCAIAGA LPPDYVDASY SSKTEKKATV DAEGNFDPRP VETLNVIIPE KLDSFINKFA
EYTHEKWAFD KIQNNWSYGE NIDEELKTHP MLRPYKTFSE KDKEIYRWPI KESLKAMIAW
EWTVEKAREG EEEKTEKKKT RKISQTAQTY DPREGYNPQP PDLSVVTLSR ELQAMAEQLA
ENYHNTWGRK KKQELEAKGG GSHPLLVPYD TLTAKEKARD REKAQELLKF LQMNGYAVTR
GLKDMELDTS SIEKRFAFGF LQQLLRWMDI SQEFIAHLEA VVSSGRVEKS PHEQEIKFFA
KILLPLINQY FTNHCLYFLS TPAKVLGSGG HASNKEKEMI TSLFCKLAAL VRHRVSLFGT
DAPAVVNCLH ILARSLDART VMKSGPEIVK AGLRSFFESA SEDIEKMVEN LRLGKVSQAR
TQVKGVGQNL TYTTVALLPV LTTLFQHIAQ HQFGDDVILD DVQVSCYRTL CSIYSLGTTR
NPYVEKLRPA LGECLARLAA AMPVAFLEPE LNEYNACSVY TTKSPRERAI LGLPNSVEEM
CPDIPVLERL MAEIGGLAES GARYTEMPHV IEITLPMLCS YLPRWWERGP EAPPPALPAG
APPPCTAVTS DHLNSLLGNI LRIIVNNLGI DEASWMKRLA VFAQPIVSRA RPELLRSHFI
PTIGRLRKRA GKVVAEEEQL RLEAKAEAEE GELLVRDEFS VLCRDLYALY PLLIRYVDNN
RAHWLTEPNP NAEELFRMVG EIFIYWSKSH NFKREEQNFV VQNEINNMSF LTADNKSKMA
KAGDVQSGGS DQERTKKKRR GDRYSVQTSL IVATLKKMLP IGLNMCAPTD QDLIVLAKAR
YALKDTDEEV REFLQNNLNL QGKVEGSPSL RWQMALYRGV PGREEDADDP EKIVRRVQEV
SAVLYHLDQT EHPYKSKKAV WHKLLSKQRR RAVVACFRMT PLYNLPTHRA CNMFLESYKA
SWILTEDHSF EDRMIDDLSK AGEQEEEEEE VEEKKPDPLH QLVLHFSRTA LTEKSKLDED
YLYMAYADIM AKSCHLEEGG ENGEEGGEEE EVEVSFEEKE MEKQRLLYQQ SRLHNRGAAE
MVLQMISACK GETGAMVSST LKLGISILNG GNAEVQQKML DYLKDKKEVG FFQSIQALMQ
TCSVLDLNAF ERQNKAEGLG MVNEDGTVIN RQNGEKVMAD DEFTQDLFRF LQLLCEGHNN
DFQNYLRTQT GNTTTINIII CTVDYLLRLQ ESISDFYWYY SGKDVIEEQG KRNFSKAMSV
AKQVFNSLTE YIQGPCTGNQ QSLAHSRLWD AVVGFLHVFA HMMMKLAQDS SQIELLKELL
DLQKDMVVML LSLLEGNVVN GMIARQMVDM LVESSSNVEM ILKFFDMFLK LKDIVGSEAF
QDYVTDPRGL ISKKDFQKAM DSQKQFTGPE IQFLLSCSEA DENEMINCEE FANRFQEPAR
DIGFNVAVLL TNLSEHVPHD PRLRNFLELA ESILEYFRPY LGRIEIMGAS RRIERIYFEI
SETNRAQWEM PQVKESKRQF IFDVVNEGGE SEKMEMFVSF CEDTIFEMQI AAQISEPEGE
PEEDEDEGAE EAEEGAAGSD GSGSAAAAGV WVWLAATAGR TLRGLSYRSL RRRVRRLRRL
TAREAATAVA ALLWALVTRA GGAGAGAAAG ALRLLWGSLF GGGLVDSAKK VTVTELLAGM
PDPTGDEVHG QQPSGAGSDA EGEGEGEGEG DAADGAGDEE AAADQAGTGG ADGAVAVADG
SPFRPEGAGG LGDMGDTTPV EPPTPEGSPI LKRKLGVDGE EEEPPPEPEP EPEPEPEKAD
TENGEKEVPE PPPEPPKKTP PPPPPKKEEA GGAGLEEFWG ELEVQRVKFL NYLSRNFYTL
RFLALFLAFA INFILLFYKV SDSPPGEDDI EGSGAGDMSG AGSGDGSGWG SRAGEEVEGD
EDENMVYYFL EESTGYMEPA LRCLSLLHTL VAFLCIIGYN CLKVPLVIFK REKELARKLE
FDGLYITEQP EDDDVKGQWD RLVLNTPSFP SNYWDKFVKR KVLDKHGDIF GRERIAELLG
MDLASLEITA HNERKPDPPP GLLTWIMSID VKYQIWKFGV IFTDNSFLYL GWYMVMSLLG
HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT VVAFNFFRKF
YNKSEDEDEP DMKCDDMMTC YLFHMYVGVR AGGGIGDEIE DPAGDEYELY RVVFDITFFF
FVIVILLAII QGLIIDAFGE LRDQQEQVKE DMETKCFICG IGSDYFDTTP HGFETHTLEE
HNLANYMFFL MYLINKDETE HTGQESYVWK MYQERCWDFF PAGDCFRKQY EDQLS
