ID   RYR3_MOUSE              Reviewed;        4863 AA.
AC   A2AGL3; P70184; P70185; Q3V1H0; Q4JFC4; Q60836; Q62175; Q62198; Q9QY91;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   04-NOV-2026, entry version 137.
DE   RecName: Full=Ryanodine receptor 3 {ECO:0000305|PubMed:8702664};
DE            Short=RYR-3;
DE            Short=RyR3;
DE   AltName: Full=Brain ryanodine receptor-calcium release channel;
DE   AltName: Full=Brain-type ryanodine receptor;
DE   AltName: Full=Type 3 ryanodine receptor;
GN   Name=Ryr3 {ECO:0000312|MGI:MGI:99684};
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-67, FUNCTION, TRANSPORTER ACTIVITY, AND
RP   DISRUPTION PHENOTYPE.
RC   TISSUE=Brain;
RX   PubMed=8702664; DOI=10.1074/jbc.271.33.19649;
RA   Takeshima H., Ikemoto T., Nishi M., Nishiyama N., Shimuta M., Sugitani Y.,
RA   Kuno J., Saito I., Saito H., Endo M., Iino M., Noda T.;
RT   "Generation and characterization of mutant mice lacking ryanodine receptor
RT   type 3.";
RL   J. Biol. Chem. 271:19649-19652(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4088-4541 (ISOFORM 1).
RC   STRAIN=SWR/J; TISSUE=Brain;
RA   Chameau P., Van de Vrede Y., Lucas-Meunier E., Fossier P., Denizot J.-P.,
RA   Shimahara T., Tauc L., Baux G.;
RT   "Calcium-induced calcium release dependent on ryanodine receptor type 3
RT   (RyR3) modulates both neuronal excitability and transmitter release.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4220-4863 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4405-4692 (ISOFORM 1), AND TISSUE
RP   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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4598-4841, SUBUNIT, AND TISSUE SPECIFICITY.
RC   TISSUE=Egg;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4741-4863, FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [8]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=9582272; DOI=10.1093/emboj/17.10.2790;
RA   Sonnleitner A., Conti A., Bertocchini F., Schindler H., Sorrentino V.;
RT   "Functional properties of the ryanodine receptor type 3 (RyR3) Ca2+ release
RT   channel.";
RL   EMBO J. 17:2790-2798(1998).
RN   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11717163; DOI=10.1161/hh2301.100250;
RA   Lohn M., Jessner W., Furstenau M., Wellner M., Sorrentino V., Haller H.,
RA   Luft F.C., Gollasch M.;
RT   "Regulation of calcium sparks and spontaneous transient outward currents by
RT   RyR3 in arterial vascular smooth muscle cells.";
RL   Circ. Res. 89:1051-1057(2001).
RN   [10]
RP   FUNCTION.
RX   PubMed=11500519; DOI=10.1074/jbc.m106944200;
RA   Yang D., Pan Z., Takeshima H., Wu C., Nagaraj R.Y., Ma J., Cheng H.;
RT   "RyR3 amplifies RyR1-mediated Ca(2+)-induced Ca(2+) release in neonatal
RT   mammalian skeletal muscle.";
RL   J. Biol. Chem. 276:40210-40214(2001).
RN   [11]
RP   FUNCTION, CHARACTERIZATION OF ISOFORM 2, ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17596299; DOI=10.1152/ajpcell.00069.2007;
RA   Dabertrand F., Fritz N., Mironneau J., Macrez N., Morel J.L.;
RT   "Role of RYR3 splice variants in calcium signaling in mouse nonpregnant and
RT   pregnant myometrium.";
RL   Am. J. Physiol. 293:C848-C854(2007).
RN   [12]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19503748; DOI=10.3389/neuro.08.003.2009;
RA   Matsuo N., Tanda K., Nakanishi K., Yamasaki N., Toyama K., Takao K.,
RA   Takeshima H., Miyakawa T.;
RT   "Comprehensive behavioral phenotyping of ryanodine receptor type 3 (RyR3)
RT   knockout mice: decreased social contact duration in two social interaction
RT   tests.";
RL   Front. Behav. Neurosci. 3:3-3(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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   [14]
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: Cytosolic calcium-activated calcium channel that mediates the
CC       release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in
CC       muscle and thereby plays a role in triggering muscle contraction. May
CC       regulate Ca(2+) release by other calcium channels. Calcium channel that
CC       mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum
CC       in non-muscle cells. Plays a role in cellular calcium signaling.
CC       Contributes to cellular calcium ion homeostasis. Isoform 2 lacks a
CC       predicted transmembrane segment and does not form functional calcium
CC       channels by itself; however, it can form tetramers with isoforms that
CC       contain the full complement of transmembrane segments and modulate
CC       their activity. {ECO:0000269|PubMed:11500519,
CC       ECO:0000269|PubMed:11717163, ECO:0000269|PubMed:17596299,
CC       ECO:0000269|PubMed:7621815, ECO:0000269|PubMed:8702664,
CC       ECO:0000269|PubMed:9582272}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC         ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:8702664,
CC         ECO:0000269|PubMed:9582272};
CC   -!- ACTIVITY REGULATION: Channel activity is modulated by the alkaloid
CC       ryanodine that binds to the open calcium-release channel with high
CC       affinity. At low concentrations, ryanodine maintains the channel in an
CC       open conformation. High ryanodine concentrations inhibit channel
CC       activity. Channel activity is regulated by calmodulin (CALM). The
CC       calcium release is activated by elevated cytoplasmic calcium levels in
CC       the micromolar range, by caffeine and adenine nucleotides, such as AMP
CC       and ATP. Inhibited by Mg(2+) and ruthenium red.
CC       {ECO:0000250|UniProtKB:Q9TS33}.
CC   -!- SUBUNIT: Homotetramer. Isoform 2 can form tetramers with isoform 1.
CC       Heterotetramer with RYR2. Interacts with FKBP1A. Interacts with CALM.
CC       Interacts with SELENON (By similarity). {ECO:0000250|UniProtKB:Q9TS33}.
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:9582272}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=RYR3L;
CC         IsoId=A2AGL3-1; Sequence=Displayed;
CC       Name=2; Synonyms=RYR3S;
CC         IsoId=A2AGL3-2; Sequence=VSP_042304;
CC   -!- TISSUE SPECIFICITY: Detected in hippocampus, cerebellum, striatum,
CC       frontal brain cortex and parietal brain cortex. Detected in skeletal
CC       muscle, diaphragm muscle and myometrium (at protein level). Detected in
CC       egg cells. Detected in heart, diaphragm, stomach, spleen, ovary, testis
CC       germ cells, brain and cerebellum. Detected in cerebral artery smooth
CC       muscle cells. {ECO:0000269|PubMed:11717163,
CC       ECO:0000269|PubMed:17596299, ECO:0000269|PubMed:7621815,
CC       ECO:0000269|PubMed:7635066, ECO:0000269|PubMed:7876312,
CC       ECO:0000269|PubMed:9582272}.
CC   -!- DOMAIN: The calcium release channel activity resides in the C-terminal
CC       region while the remaining part of the protein resides in the
CC       cytoplasm. {ECO:0000250|UniProtKB:P11716}.
CC   -!- DISRUPTION PHENOTYPE: No apparent phenotype. Mice are born at the
CC       expected Mendelian rate and are fertile. They appear normal, except for
CC       increased locomotor activity and decreased social contact duration in
CC       social interaction tests. {ECO:0000269|PubMed:19503748,
CC       ECO:0000269|PubMed:8702664}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Lacks a predicted transmembrane segment and
CC       is not expected to form functional calcium channels. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL929348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL672250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL691423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL732316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX649564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; D84237; BAA12286.1; -; mRNA.
DR   EMBL; AF111166; AAF21940.1; -; mRNA.
DR   EMBL; AK132464; BAE21181.1; -; mRNA.
DR   EMBL; X83934; CAA58786.1; -; mRNA.
DR   EMBL; U23756; AAA64957.1; -; mRNA.
DR   EMBL; D38218; BAA07393.1; -; mRNA.
DR   PIR; I48743; I48743.
DR   PIR; S56107; S56107.
DR   RefSeq; XP_017172194.1; XM_017316705.3. [A2AGL3-1]
DR   SMR; A2AGL3; -.
DR   ComplexPortal; CPX-3161; Ryanodine 3 complex.
DR   FunCoup; A2AGL3; 945.
DR   IntAct; A2AGL3; 1.
DR   STRING; 10090.ENSMUSP00000147250; -.
DR   BindingDB; A2AGL3; -.
DR   ChEMBL; CHEMBL2365; -.
DR   iPTMnet; A2AGL3; -.
DR   PhosphoSitePlus; A2AGL3; -.
DR   SwissPalm; A2AGL3; -.
DR   jPOST; A2AGL3; -.
DR   PaxDb; 10090-ENSMUSP00000147250; -.
DR   PeptideAtlas; A2AGL3; -.
DR   ProteomicsDB; 256855; -. [A2AGL3-1]
DR   ProteomicsDB; 256856; -. [A2AGL3-2]
DR   Antibodypedia; 41923; 46 antibodies from 18 providers.
DR   DNASU; 20192; -.
DR   Ensembl; ENSMPUT00000008119; ENSMPUP00000007994; ENSMPUG00000008052.
DR   Ensembl; ENSMUST00000080673.13; ENSMUSP00000079503.6; ENSMUSG00000057378.16. [A2AGL3-1]
DR   Ensembl; ENSMUST00000208151.2; ENSMUSP00000146449.2; ENSMUSG00000057378.16. [A2AGL3-2]
DR   GeneID; 20192; -.
DR   AGR; MGI:99684; -.
DR   CTD; 6263; -.
DR   MGI; MGI:99684; Ryr3.
DR   VEuPathDB; HostDB:ENSMUSG00000057378; -.
DR   eggNOG; KOG2243; Eukaryota.
DR   GeneTree; ENSGT00940000155507; -.
DR   HOGENOM; CLU_000040_2_0_1; -.
DR   InParanoid; A2AGL3; -.
DR   PhylomeDB; A2AGL3; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   BioGRID-ORCS; 20192; 1 hit in 61 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:A2AGL3; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A2AGL3; protein.
DR   Bgee; ENSMUSG00000057378; Expressed in caudate-putamen and 150 other cell types or tissues.
DR   ExpressionAtlas; A2AGL3; baseline and differential.
DR   GO; GO:0034704; C:calcium channel complex; IBA:GO_Central.
DR   GO; GO:0030314; C:junctional membrane complex; IDA:MGI.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0005790; C:smooth endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0015278; F:intracellularly gated calcium channel activity; ISO:GO_Central.
DR   GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IDA:UniProtKB.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; ISO:GO_Central.
DR   GO; GO:0071318; P:cellular response to ATP; ISS:UniProtKB.
DR   GO; GO:0071313; P:cellular response to caffeine; ISS:UniProtKB.
DR   GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR   GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0006941; P:striated muscle contraction; IMP:MGI.
DR   CDD; cd23292; beta-trefoil_MIR_RyR3; 1.
DR   CDD; cd12877; SPRY1_RyR; 1.
DR   CDD; cd12878; SPRY2_RyR; 1.
DR   CDD; cd12879; SPRY3_RyR; 1.
DR   FunFam; 2.80.10.50:FF:000009; Ryanodine receptor 1 (skeletal); 1.
DR   FunFam; 1.10.238.10:FF:000040; Ryanodine receptor 2; 1.
DR   FunFam; 1.10.490.160:FF:000001; Ryanodine receptor 2 (Cardiac); 1.
DR   FunFam; 2.80.10.50:FF:000006; Ryanodine receptor 2 (Cardiac); 1.
DR   FunFam; 2.60.120.920:FF:000024; Ryanodine receptor 3; 1.
DR   FunFam; 1.10.287.70:FF:000017; ryanodine receptor isoform X2; 1.
DR   FunFam; 1.25.10.30:FF:000002; ryanodine receptor isoform X2; 1.
DR   FunFam; 2.60.120.920:FF:000002; ryanodine receptor isoform X2; 1.
DR   FunFam; 2.60.120.920:FF:000003; ryanodine receptor isoform X2; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.10.490.160; -; 2.
DR   Gene3D; 2.60.120.920; -; 3.
DR   Gene3D; 2.80.10.50; -; 2.
DR   Gene3D; 6.20.350.10; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.25.10.30; IP3 receptor type 1 binding core, RIH domain; 1.
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; 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; IPR015925; Ryanodine_IP3_receptor.
DR   InterPro; IPR003032; Ryanodine_rcpt.
DR   InterPro; IPR009460; Ryanrecept_TM4-6.
DR   InterPro; IPR048581; RYDR_Jsol.
DR   InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR   InterPro; IPR035761; SPRY1_RyR.
DR   InterPro; IPR035764; SPRY2_RyR.
DR   InterPro; IPR035762; SPRY3_RyR.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR46399; B30.2/SPRY DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46399:SF9; RYANODINE RECEPTOR 3; 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; PF21119; RYDR_Jsol; 1.
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; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF100909; IP3 receptor type 1 binding core, domain 2; 2.
DR   SUPFAM; SSF82109; MIR domain; 2.
DR   PROSITE; PS50188; B302_SPRY; 3.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Calmodulin-binding; Ion channel; Ion transport; Ligand-gated ion channel;
KW   Membrane; Receptor; Reference proteome; Repeat; Sarcoplasmic reticulum;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..4863
FT                   /note="Ryanodine receptor 3"
FT                   /id="PRO_0000415648"
FT   TOPO_DOM        1..4179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4180..4200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4403..4423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4478..4498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4603..4623
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4626..4646
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4665..4685
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        4716..4725
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        4746..4766
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        4767..4863
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          100..155
FT                   /note="MIR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          162..207
FT                   /note="MIR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          215..269
FT                   /note="MIR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          275..333
FT                   /note="MIR 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          343..400
FT                   /note="MIR 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          585..796
FT                   /note="B30.2/SPRY 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REPEAT          840..953
FT                   /note="1"
FT   REPEAT          954..1068
FT                   /note="2"
FT   DOMAIN          1012..1208
FT                   /note="B30.2/SPRY 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   DOMAIN          1254..1466
FT                   /note="B30.2/SPRY 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REPEAT          2587..2705
FT                   /note="3"
FT   REPEAT          2706..2818
FT                   /note="4"
FT   REGION          840..2818
FT                   /note="4 X approximate repeats"
FT   REGION          2320..2333
FT                   /note="Interaction with FKBP1A"
FT                   /evidence="ECO:0000250"
FT   REGION          3329..3348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3462..3491
FT                   /note="Interaction with CALM"
FT                   /evidence="ECO:0000250"
FT   REGION          3576..3604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4095..4126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          4326..4347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3593..3604
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4104..4126
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        4326..4347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            3876
FT                   /note="Important for activation by Ca(2+)"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         4397..4425
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_042304"
FT   CONFLICT        4169
FT                   /note="S -> I (in Ref. 3; AAF21940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4214
FT                   /note="E -> Q (in Ref. 3; AAF21940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4427
FT                   /note="T -> A (in Ref. 3; AAF21940)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4450
FT                   /note="E -> V (in Ref. 4; BAE21181)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4457
FT                   /note="F -> L (in Ref. 5; CAA58786)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4469
FT                   /note="T -> N (in Ref. 5; CAA58786)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        4602
FT                   /note="H -> N (in Ref. 6; AAA64957)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   4863 AA;  551328 MW;  D2B086935E99D40B CRC64;
     MAEAGEGGED EIQFLRTEDE VVLQCIANIH KEQRKFCLAA EGLGNRLCFL EPTSEAKYIP
     PDLCVCNFVL EQSLSVRALQ EMLANTVENG GEGAAQGGGH RTLLYGHAIL LRHSFSGMYL
     TCLTTSRSQT DKLAFDVGLR EHATGEACWW TIHPASKQRS EGEKVRIGDD LILVSVSSER
     YLHLSISNGS IQVDASFMQT LWNVHPTCSG SSIEEGYLLG GHVVRLFHGH DECLTIPSTD
     QNDSQHRRVF YEAGGAGTRA RSLWRVEPLR ISWSGSNIRW GQAFRLRHLT TGHYLALTED
     QGLLLQDRGK SDTKSTAFSF RASKEIKEKL DSSHKRDMEG MGVPEIKYGD SVCFVQHVAS
     GLWVTYKAQD AKTSRLGPLK RKVILHQEGH MDDGLTLQRC QQEESQAARI IRNTTALFSQ
     FVSGNNRTTA PVALPTEEVL QTLQDLIAYF QPPEDEMQHE DKQNKLRSLK NRQNLFKEEG
     MLALVLNCID RLNIYNSVAH FAGIVREESG MAWKEILNLL YKLLAALIRG NRNNCAQFSN
     NLDWLISKLD RLESSSGILE VLHCILIESP EALNLIAEGH IKSIISLLDK HGRNHKVLDV
     LCSLCLCNGV AVRANQNLIC DNLLPRRNLL LQTRLINDVT SIRPNIFLGV AEGSPQYKKW
     YFELIIDQVE PFLTAEPTHL RVGWASSSGY APYPGGGEGW GGNGVGDDLY SYGFDGLHLW
     SGRIPRAVAS INQHLLKSDD VVSCCLDLGV PSISFRINGQ PVQGMFENFN TDGLFFPVMS
     FSAGVKVRFL MGGRHGEFKF LPPSGYAPCY EALLPKEKMR LEPVKEYKRD ADGVRDLLGT
     TQFLSQASFI PCPIDTSQVV LPLHLEKIRD RLAENIHELW GMNKIELGWT YGKVRDDNKR
     QHPCLVEFSK LPETEKNYNL QMSTETLKTL LALGCHIAHV NPAAEEDLKK VKLPKNYMMS
     NGYKPAPLDL SDVKLLPPQE ILVDKLAENA HNVWAKDRIK QGWTYGIQQD LKNKRNPRLV
     PYALLDERTK KSNRDSLREA VRTFVGYGYN IEPSDQELAD PTVEKVSIDK IRFFRVERSY
     AVKSGKWYFE FEVVTGGDMR VGWARPGCRP DIELGADDQA FVFEGSRGQR WHQGSGYFGR
     TWQPGDVVGC MINLDDASMV FTLNGELLIT NKGSELAFAD YEIENGFVPI CSLGLSQIGR
     MNLGTDASTF KFYTMCGLQE GFEPFAVNMN RDVAVWFSKR LPTFVNVPKD HPHIEVVRID
     GTMDSPPCLK VTHKTFGTQN SNANMIYCRL SMPVECHSSF SHSPCLDSEA FQKRKQMQEI
     LSHTTTQCYY AIRIFAGQDP SCVWVGWVTP DYHLYSEKFD LNKNCTVTVT LGDERGRVHE
     SVKRSNCYMV WGGDIVASSQ RSSRSNVDLE IGCLLDLAMG MLSFSANGKE LGTCYQVEPN
     TKVFPAVFLQ PTSTSLFQFE LGKLKNAMPL SAAIFKSEEK NPTPQCPPRL DVQTIQPVLW
     SRMPSSFLKV ETERVSERHG WVVQCLEPLQ MMALHIPEEN RCVDILELCE QEDLMQFHYH
     TLRLYSAVCA LGNSRVASAL CSHVDLSQLF YAIDNKYLPG LLRSGFYDLL ISIHLANAKE
     RKLMMKNEYI IPITSATRNI RLYPDESKRH GLPGVGLRTC LKPGFRFSTP CFVVTSEDHQ
     KQSPEIPLQI LKTKALSMLT EAVHCSGAHI RDPVGGSVEF QFVPVLKLIG TLLVMGVFDD
     DDVRQILLLI DPSVFGEHSG ETEEGVEKEV THAEEKAVEA GEKACKEAPV KGLLQTRLPE
     SVKLQMCELL SYLCDCELQH RVEAIVAFGD IYVSKLQANQ KFRYNELMQA LNMSAALTAR
     KTREFRSPPQ EQINMLLNFH LGENCPCPEE IREELYDFHE DLLVHCGVPL EEEEEEEEDT
     SWTGKLCALV YKIKGPPKPE KEQPTEEEKP YPTTLKELVS QTMIRWAQEN QIQDAELVRM
     MFNLLRRQYD SIGELLQALR KTYTISQASV NDTINLLAAL GQIRSLLSVR MGREEELLMI
     NGLGDIMNNK VFYQHPNLMR VLGMHETVME VMVNVLGTEK SQIAFPKMVA SCCRFLCYFC
     RISRQNQKAM FEHLSYLLEN SSVGLASPSM RGSTPLDVAA SSVMDNNELA LGLEEPDLEK
     VVTYLAGCGL QSCPMLLARG YPDVGWNPIE GERYLSFLRF AVFVNSESVE ENASVVVKLL
     IRRPECFGPA LRGEGGNGLL AAMQGAIKIS ENPALDLPSQ GYKTEVTQDD GEEEEIVHMG
     NAIMSFYSAL IDLLGRCAPE MHLIQTGKGE AIRIRSILRS LVPTEDLVGI ISIPLKLPSL
     NKDGSVSEPD MAANFCPDHK APMVLFLDRV YGIKDQTFLL HLLEVGFLPD LRASASLDTV
     SLSTTEAALA LNRYLCSAVL PLLTRCAPLF SGTEHCTSLI DSTLQTIYRL SKGRSLTKAQ
     RDTIEECLLA ICNHLRPSML QQLLRRLVFD VPQLSEYCKM PLKLLTNHYE QCWKYYCLPS
     GWGSYGLAVE EELHLTEKLF WGIFDSLSHK KYDLDLFRMA LPCLSAIAGA LPPDYLDTRI
     TATLEKQVSV DADGNFDPKP INTMNFSLPE KLEYIVTKYA EHSHDKWACD KSHSGWKYGI
     SLDENVKTHP LIRPFKTLTE KEKEIYRWPA RESLKTMLAV GWTVERTKEG EALVQQRENE
     KLRCVSQTNQ GNSYSPAPLD LSNVVLSREL QGMVEVVAEN YHNIWAKKKK LELESKGGGS
     HPLLVPYDTL TAKEKFRDRE KAQDLFKFLQ VNGILVSRGM KDLELDASSM EKRFAYKFLK
     KILKYVDAAQ EFIAHLEAIV SSGKTEKSPH DQEIKFFAKV LLPLVDQYFT NHRLYFLSSP
     LKPLSSSGYA SHKEKEMVAS LFCKLAALVR HRISLFGSDS TTMVSCLHIL AQTLDTRTVM
     KSGSELVKAG LRAFFENAAE DLEKTSENLK LGKFTHSRTQ IKGVSQNINY TTVALLPILT
     SIFEHIAQHQ FGVDLLLSDV QVSCYHILCS LYSLGTGKNI YVERQRPALG ECLASLAAAI
     PVAFLEPSLN RHNPLSVFNT KTPRERSILG MPDKVEDMCP DIPQLEGLMK EINDLAESGA
     RYTEMPHVIE VILPMLCNYL SYWWERGPEN LPPSTGPCCT KVTSEHLSLI LGNILKIINN
     NLGIDEASWM KRIAVYAQPI ISKARPDLLR SHFIPTLEKL KKKAVKTVQE EEQLKTDGKG
     DTQEAELLIL DEFAVLCRDL YAFYPMLIRY VDNNRSNWLK SPDPDSDQLF RMVAEVFILW
     CKSHNFKREE QNFVIQNEIN NLAFLTGDSK SKMSKSGGQD QERKKTKRRG DLYSIQTSLI
     VAALKKMLPI GLNMCTPGDQ ELISLAKSRY SCRDTDEEVK EHLRNNLHLQ EKSDDPAVKW
     QLNLYKDVLR NDEPSNPEKT VERVQSISAA LFHLEQVEQP LRSKKAVWHK LLSKQRKRAV
     VACFRMAPLY NLPRHRSINL FLHGYQRFWI ETEAHFFEEK LVQDLAKSPR VEDEEEEETE
     RQPDPLHQII LHFSRNALTE RSKLEDDPLY TSYSSMMAKS CQSGEDEEEE EDKEKTFEEK
     EMEKQKTLYQ QARLHERGAA EMVLQMISAS KGEMSPMVVE TLKLGIAILN GGNAGVQQKM
     LDYLKEKKDA GFFQSLSGLM QSCSVLDLNA FERQNKAEGL GMVTEEGTLI VRERGEKVLQ
     NDEFTQDLFR FLQLLCEGHN SDFQNFLRTQ MGNTTTVNII ISTVDYLLRL QESISDFYWY
     YSGKDIIDES GQHNFSKALA VTKQIFNSLT EYIQGPCIGN QQSLAHSRLW DAVVGFLHVF
     ANMQMKLSQD SSQIELLKEL LDLLQDMVVM LLSLLEGNVV NGTIGKQMVD TLVESSTNVE
     MILKFFDMFL KLKDLTSSDT FKEYDPDGKG IISRKEFQKA MEGLKQYTQS EIDFLLSCTE
     ADENDMFNYV DFVERFHEPA KDIGFNVAVL LTNLSEHMPN DSRLKSLLDP AESVLNYFEP
     YLGRIEIMGG AKKIERVYFE ISESSRTQWE KPQVKESKRQ FIFDVVNEGG EQEKMELFVN
     FCEDTIFEMQ LASQISESDS TDRPEEEEEE DEDSAYSIET EGEEEEKSFE SASAFTMACV
     SVKRNVTKFL KRATLKNLRK QYRNVKKMSA KELVKVFFSF FWMLFVGLFQ LLFTIFGGIF
     QILWNTVFGG GLVEGAKNIR VTKILGDMPD PTQFGIHDDV IETDRAEVTE PGVTTELVHF
     VKGEAGDTDI MSDLFGIHSK KEGGLKQGPE VGLGDLSEII GKDEPPTLES TVRKKRKAQA
     AEMKAVHEAE GKAESEKADM EDREKEDKIK EEGQTDYLWA DVTVKKTRRR GQKAEKPEAF
     MANFFKGLEI YQTKLLHYLA RNFYNLRFLA LFVAFAINFI LLFYKVTEEP LEEETEDVAN
     LWNSFNDDDE EEAMVFFVLQ ESTGYMAPTL RALAIVHTII SLVCVVGYYC LKVPLVVFKR
     EKEIARKLEF DGLYITEQPS EDDIKGQWDR LVINTPSFPN NYWDKFVKRK VINKYGDLYG
     AERIAELLGL DKNALDFSPV EEAKAEAASL VSWLSSIDMK YHIWKLGVVF TDNSFLYLAW
     YTTMSVLGHY NNFFFAAHLL DIAMGFKTLR TILSSVTHNG KQLVLTVGLL AVVVYLYTVV
     AFNFFRKFYN KSEDDDEPDM KCDDMMTCYL FHMYVGVRAG GGIGDEIEDP AGDPYEMYRI
     VFDITFFFFV IVILLAIIQG LIIDAFGELR DQQEQVREDM ETKCFICGIG NDYFDTTPHG
     FETHTLQEHN LANYLFFLMY LINKDETEHT GQESYVWKMY QERCWDFFPA GDCFRKQYED
     QLG
//