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Database: UniProt
Entry: RYR1_MOUSE
LinkDB: RYR1_MOUSE
Original site: RYR1_MOUSE 
ID   RYR1_MOUSE              Reviewed;        5035 AA.
AC   E9PZQ0; Q60834; Q61779; Q61780; Q62173; Q62196; Q62235; Q78EJ6;
AC   Q7TNG1; Q80UQ5; Q80X16; Q99JF9;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-APR-2018, entry version 69.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
RP   TISSUE 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
RT   delays 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.
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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, NUCLEOTIDE SEQUENCE [MRNA]
RP   OF 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
RT   project: 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
RT   differentially 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;
RA   Ayabe T., Kopf G.S., Schultz R.M.;
RT   "Regulation of mouse egg activation: presence of ryanodine receptors
RT   and effects of microinjected ryanodine and cyclic ADP ribose on
RT   uninseminated and inseminated eggs.";
RL   Development 121:2233-2244(1995).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4913-5035, FUNCTION, SUBCELLULAR
RP   LOCATION, DOMAIN, ENZYME REGULATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX   PubMed=7621815;
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
RT   the 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
RT   reticulum in skeletal muscle with a mutation targeted to the ryanodine
RT   receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3381-3385(1995).
RN   [11]
RP   FUNCTION, PHOSPHORYLATION AT SER-2844, S-NITROSYLATION, AND
RP   IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; FKBP1A AND PROTEIN
RP   PHOSPHATASE 1.
RX   PubMed=18268335; DOI=10.1073/pnas.0711074105;
RA   Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X.,
RA   Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A.,
RA   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
RP   BY 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [13]
RP   FUNCTION IN BRAIN, S-NITROSYLATION, ENZYME 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
RT   regulates neuronal function.";
RL   EMBO J. 31:417-428(2012).
RN   [14]
RP   FUNCTION, ENZYME 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
RT   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
CC       the sarcoplasmic reticulum into the cytoplasm and thereby plays a
CC       key role in triggering muscle contraction following depolarization
CC       of T-tubules (PubMed:18003898, PubMed:7515481, PubMed:7621815,
CC       PubMed:21156754). Repeated very high-level exercise increases the
CC       open probability of the channel and leads to Ca(2+) leaking into
CC       the cytoplasm (PubMed:18268335). Can also mediate the release of
CC       Ca(2+) from intracellular stores in neurons, and may thereby
CC       promote prolonged Ca(2+) signaling in the brain (PubMed:22036948).
CC       Required for normal embryonic development of muscle fibers and
CC       skeletal muscle (PubMed:7515481). Required for normal heart
CC       morphogenesis, skin development and ossification during
CC       embryogenesis (PubMed:18003898, PubMed:7515481).
CC       {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:18268335,
CC       ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:22036948,
CC       ECO:0000269|PubMed:7515481, ECO:0000269|PubMed:7621815}.
CC   -!- ENZYME REGULATION: Channel activity is modulated by the alkaloid
CC       ryanodine that binds to the open Ca-release channel with high
CC       affinity. At low concentrations, ryanodine maintains the channel
CC       in an open conformation. High ryanodine concentrations inhibit
CC       channel activity (PubMed:7621815). Channel activity is regulated
CC       by calmodulin (CALM). The calcium release is activated by
CC       increased cytoplasmic calcium levels, by nitric oxyde (NO),
CC       caffeine and ATP (PubMed:7621815, PubMed:22036948,
CC       PubMed:21156754). Channel activity is inhibited by magnesium ions,
CC       possibly by competition for calcium binding sites.
CC       {ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:7621815}.
CC   -!- SUBUNIT: Homotetramer (PubMed:18003898). Can also form
CC       heterotetramers with RYR2 (By similarity). Identified in a complex
CC       composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1
CC       (PP1) (PubMed:18268335). Repeated very high-level exercise
CC       decreases interaction with PDE4D and protein phosphatase 1 (PP1)
CC       (PubMed:18268335). Interacts with CALM; CALM with bound calcium
CC       inhibits the RYR1 channel activity (By similarity). Interacts with
CC       S100A1 (By similarity). Interacts with FKBP1A; this stabilizes the
CC       closed conformation of the channel. Interacts with CACNA1S;
CC       interaction with CACNA1S is important for activation of the RYR1
CC       channel. Interacts with CACNB1. Interacts with TRDN and ASPH;
CC       these interactions stimulate RYR1 channel activity. Interacts with
CC       SELENON (By similarity). {ECO:0000250|UniProtKB:P11716,
CC       ECO:0000250|UniProtKB:P21817, ECO:0000269|PubMed:18003898,
CC       ECO:0000269|PubMed:18268335}.
CC   -!- INTERACTION:
CC       O55108:Bsg; NbExp=3; IntAct=EBI-642079, EBI-643315;
CC       P49070:Camlg; NbExp=3; IntAct=EBI-642079, EBI-309114;
CC       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-
CC       pass membrane protein {ECO:0000269|PubMed:18003898}. Membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC       Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P11716}. Note=The
CC       number of predicted transmembrane domains varies between
CC       orthologs, but the 3D-structures show the presence of six
CC       transmembrane regions. Both N-terminus and C-terminus are
CC       cytoplasmic. {ECO:0000250|UniProtKB:P11716}.
CC   -!- TISSUE SPECIFICITY: Detected in muscle and myotubes (at protein
CC       level) (PubMed:18003898). Ubiquitous. Detected in diaphragm,
CC       skeletal muscle, esophagus, spleen, submaxillary gland, adrenal
CC       gland, cerebellum, brain and in testis germ cells.
CC       {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:21156754,
CC       ECO:0000269|PubMed:22036948, ECO:0000269|PubMed:7621815,
CC       ECO:0000269|PubMed:7876312}.
CC   -!- DOMAIN: The calcium release channel activity resides in the C-
CC       terminal region while the remaining part of the protein
CC       constitutes the 'foot' structure spanning the junctional gap
CC       between the sarcoplasmic reticulum (SR) and the T-tubule
CC       (PubMed:7621815, PubMed:7724570). Pore opening is mediated via the
CC       cytoplasmic calcium-binding domains that mediate a small rotation
CC       of the channel-forming transmembrane regions that then leads to
CC       channel opening (By similarity). {ECO:0000250|UniProtKB:P11716,
CC       ECO:0000269|PubMed:7621815, ECO:0000269|PubMed:7724570}.
CC   -!- PTM: Channel activity is modulated by phosphorylation.
CC       Phosphorylation at Ser-2844 may increase channel activity.
CC       Repeated very high-level exercise increases phosphorylation at
CC       Ser-2844. {ECO:0000269|PubMed:18268335,
CC       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
CC       in skeletal muscle development. Neonates do not breathe and do not
CC       move. Mutant mice show defects in muscle fiber development. Their
CC       muscles do not show a contractile response to electrical
CC       stimulation. In addition, mice display abnormal curvature of the
CC       spine, thin limbs, and an abnormal rib cage.
CC       {ECO:0000269|PubMed:7515481}.
CC   -!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family.
CC       RYR1 subfamily. {ECO:0000305}.
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   UniGene; Mm.439745; -.
DR   ProteinModelPortal; E9PZQ0; -.
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   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   eggNOG; KOG2243; Eukaryota.
DR   eggNOG; ENOG410YCNW; LUCA.
DR   GeneTree; ENSGT00760000119152; -.
DR   HOGENOM; HOG000231428; -.
DR   HOVERGEN; HBG102939; -.
DR   InParanoid; E9PZQ0; -.
DR   KO; K04961; -.
DR   OMA; DIPARRN; -.
DR   OrthoDB; EOG091G00T0; -.
DR   TreeFam; TF315244; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   PRO; PR:E9PZQ0; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000030592; -.
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: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: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: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: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: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:0001666; P:response to hypoxia; 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   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
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; IPR015925; Ryanodine_recept-rel.
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; PTHR13715; 1.
DR   PANTHER; PTHR13715:SF15; PTHR13715:SF15; 1.
DR   Pfam; PF13833; EF-hand_8; 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; Complete proteome; Developmental protein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; S-nitrosylation; Sarcoplasmic reticulum;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   5035       Ryanodine receptor 1.
FT                                /FTId=PRO_0000415566.
FT   TOPO_DOM      1   4556       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4557   4577       Helical; Name=1.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4578   4638       Lumenal. {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4639   4659       Helical; Name=2.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4660   4777       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4778   4800       Helical; Name=3.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4801   4801       Lumenal. {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4802   4818       Helical; Name=4.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4819   4833       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4834   4854       Helical; Name=5.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4855   4877       Lumenal. {ECO:0000250|UniProtKB:P11716}.
FT   INTRAMEM   4878   4897       Pore-forming.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4898   4917       Lumenal. {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4918   4938       Helical; Name=6.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4939   5035       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   DOMAIN       99    154       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      161    206       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      212    266       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      272    329       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      337    394       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      583    799       B30.2/SPRY 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT      843    956       1.
FT   REPEAT      957   1070       2.
FT   DOMAIN     1015   1210       B30.2/SPRY 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT     1346   1361       3; truncated.
FT   DOMAIN     1359   1572       B30.2/SPRY 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT     1374   1389       4; truncated.
FT   REPEAT     2727   2846       5.
FT   REPEAT     2847   2960       6.
FT   DOMAIN     4078   4106       EF-hand. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   NP_BIND    4214   4218       ATP. {ECO:0000250|UniProtKB:P11716}.
FT   NP_BIND    4952   4957       ATP. {ECO:0000250|UniProtKB:P11716}.
FT   NP_BIND    4977   4983       ATP. {ECO:0000250|UniProtKB:P11716}.
FT   REGION      671    682       Interaction with FKBP1A.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   REGION      843   2960       6 X approximate repeats.
FT   REGION     3615   3644       Interaction with CALM. {ECO:0000250}.
FT   MOTIF      4892   4898       Selectivity filter.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   COMPBIAS   1869   2089       Glu-rich.
FT   COMPBIAS   3683   3762       Glu-rich.
FT   COMPBIAS   4459   4525       Pro-rich.
FT   METAL      3896   3896       Calcium. {ECO:0000250|UniProtKB:P11716}.
FT   METAL      3970   3970       Calcium. {ECO:0000250|UniProtKB:P11716}.
FT   METAL      4999   4999       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   BINDING    4714   4714       Caffeine. {ECO:0000250|UniProtKB:P11716}.
FT   MOD_RES    1339   1339       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    2346   2346       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    2844   2844       Phosphoserine; by PKA and PKG.
FT                                {ECO:0000244|PubMed:21183079,
FT                                ECO:0000269|PubMed:18268335,
FT                                ECO:0000269|PubMed:21156754}.
FT   MOD_RES    3636   3636       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   MOD_RES    4464   4464       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    4468   4468       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    4861   4861       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P21817}.
FT   MOD_RES    4864   4864       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P21817}.
FT   MUTAGEN     165    165       R->C: Increased channel activity, leading
FT                                to permanently increased cytoplasmic
FT                                Ca(2+) levels. Increased activation by
FT                                calcium, and increased ryanodine binding.
FT                                {ECO:0000269|PubMed:21156754}.
FT   MUTAGEN    4895   4895       I->T: Causes paralysis and perinatal
FT                                death in homozygous mice, apparently due
FT                                to asphyxia. Mutant mice have greatly
FT                                reduced and amorphous skeletal muscle.
FT                                {ECO:0000269|PubMed:18003898}.
FT   CONFLICT    616    616       R -> C (in Ref. 5; CAC34624).
FT                                {ECO:0000305}.
FT   CONFLICT   1380   1380       A -> S (in Ref. 1; AAP29981).
FT                                {ECO:0000305}.
FT   CONFLICT   3484   3484       D -> V (in Ref. 1; AAP29981).
FT                                {ECO:0000305}.
FT   CONFLICT   4766   4766       I -> L (in Ref. 8; AAA64955).
FT                                {ECO:0000305}.
FT   CONFLICT   4821   4821       L -> V (in Ref. 7; CAA58784).
FT                                {ECO:0000305}.
FT   CONFLICT   4888   4888       G -> A (in Ref. 7; CAA58784).
FT                                {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
//
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