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 24-JAN-2024, entry version 126.
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_017316705.1. [A2AGL3-1]
DR SMR; A2AGL3; -.
DR ComplexPortal; CPX-3161; Ryanodine 3 complex.
DR IntAct; A2AGL3; 1.
DR MINT; A2AGL3; -.
DR STRING; 10090.ENSMUSP00000147250; -.
DR BindingDB; A2AGL3; -.
DR ChEMBL; CHEMBL2365; -.
DR iPTMnet; A2AGL3; -.
DR PhosphoSitePlus; A2AGL3; -.
DR SwissPalm; A2AGL3; -.
DR EPD; A2AGL3; -.
DR MaxQB; A2AGL3; -.
DR PaxDb; 10090-ENSMUSP00000089426; -.
DR PeptideAtlas; A2AGL3; -.
DR ProteomicsDB; 256855; -. [A2AGL3-1]
DR ProteomicsDB; 256856; -. [A2AGL3-2]
DR Antibodypedia; 41923; 45 antibodies from 17 providers.
DR DNASU; 20192; -.
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 OrthoDB; 3144451at2759; -.
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 ChiTaRS; Ryr3; mouse.
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 Genevisible; A2AGL3; MM.
DR GO; GO:0034704; C:calcium channel complex; IBA:GO_Central.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0030314; C:junctional membrane complex; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
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:0048763; F:calcium-induced calcium release activity; ISO:MGI.
DR GO; GO:0015278; F:calcium-release channel activity; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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:MGI.
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:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO: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; cd12877; SPRY1_RyR; 1.
DR CDD; cd12878; SPRY2_RyR; 1.
DR CDD; cd12879; SPRY3_RyR; 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 4101..4126
FT /note="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
//
