| IED ID | IndEnz0002001658 |
| Enzyme Type ID | protease001658 |
| Protein Name |
Ryanodine receptor 1 RYR-1 RyR1 Skeletal muscle calcium release channel Skeletal muscle ryanodine receptor Skeletal muscle-type ryanodine receptor Type 1 ryanodine receptor |
| Gene Name | Ryr1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MGDGGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFILEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSGCEEGFVTGGHVLRLFHGHMDECLTISPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLGLTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAMLHQEGHMDDALSLTRCQQEESQAARMIYSTAGLYNQFIKGLDSFSGKPRGSGPPAGSALPIEGVILSLQDLIGYFEPPSEELQHEEKQTKLRSLRNRQSLFQEEGMLSLVLNCIDRLNVYTTAAHFAEFAGEEAAESWKEIVNLLYELLASLIRGNRTNCALFSTNLDWLVSKLDRLEASSGILEVLYCVLIESPEVLNIIQENHIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGSTQYGKWYFEVMVDEVAPFLTAQATHLRVGWALSEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGIKVRFLLGGRHGEFKFLPPPGYAPCHEAVLPRERLHLQPIKEYRREGPRGPHLVGPSRCLSHLDFVPCPVDTIQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVNFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVDSQSRGDRARIFRAEKSYAVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADDLAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFRDIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKSLPQFEPVPLEHPHYEVARMDGTVDTPPCLRLTHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLASPGLQPPAEDEARAAEPDTDYENLRRSAGGWGEAEGGKDGTAKEGTPGGTAQAGVEAQPARAENEKDATTEKNKKRGFLFKAKKVAMMTQPPSTPALPRLPRDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMSFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVVQFELGKQKNIMPLSAAMFLSERKNPAPQCPPRLEVQMLMPVSWSRMPNHFLQVDTRRAGERLGWAVQCQEPLMMMALHIPEENRCMDILELSERLDLQRFHSHTLSLYRSVCALGNNRVAHALCSHVDQAQLLHALEDARLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTPETRAITLFPPGRSAEDGPRRHGLPGVGVTTSLRPPHHFSPPCFVVALPAAGATEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGVFSDEDVKQILKMIEPEVFREEEEVEEEGEEEEEDEEEKEEDEEEEAHEKEDEEKEEAEDAAEEEKEELEEGLLQMKLPESVKLQMCHLLEYFCDQELQHRVESLAAFAECYVDKMQGNQRGRYGLLMKAFTMSAAETARRTREFRSPPQEQINMLLHFKNGADEEECPLPEEIRQELVNFHQDLLAHCGIQLEGEEEEPEEESTLGSRLMSLLEKVKLVKKTEEKPEEEPAPEEHKPQSLQELVSHTVVRWAQEDFVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISVSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLLAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGVRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPETHLIQAGKGEALRIRAILRSLVPLDDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSTTEMALALNRYLCLAVLPLITKCAPLFAGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMALCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDQELYRIAMPCLCAIAGALPPDYVDASYSSKTEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTVEKAREGEEEKTEKKKTRKISQTAQTYDPREGYNPQPPDLSVVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGSHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDTSSIEKRFAFGFLQQLLRWMDISQEFIAHLEAVVSSGRVEKSPHEQEIKFFAKILLPLINQYFTNHCLYFLSTPAKVLGSGGHASNKEKEMITSLFCKLAALVRHRVSLFGTDAPAVVNCLHILARSLDARTVMKSGPEIVKAGLRSFFESASEDIEKMVENLRLGKVSQARTQVKGVGQNLTYTTVALLPVLTTLFQHIAQHQFGDDVILDDVQVSCYRTLCSIYSLGTTRNPYVEKLRPALGECLARLAAAMPVAFLEPELNEYNACSVYTTKSPRERAILGLPNSVEEMCPDIPVLERLMAEIGGLAESGARYTEMPHVIEITLPMLCSYLPRWWERGPEAPPPALPAGAPPPCTAVTSDHLNSLLGNILRIIVNNLGIDEASWMKRLAVFAQPIVSRARPELLRSHFIPTIGRLRKRAGKVVAEEEQLRLEAKAEAEEGELLVRDEFSVLCRDLYALYPLLIRYVDNNRAHWLTEPNPNAEELFRMVGEIFIYWSKSHNFKREEQNFVVQNEINNMSFLTADNKSKMAKAGDVQSGGSDQERTKKKRRGDRYSVQTSLIVATLKKMLPIGLNMCAPTDQDLIVLAKARYALKDTDEEVREFLQNNLNLQGKVEGSPSLRWQMALYRGVPGREEDADDPEKIVRRVQEVSAVLYHLDQTEHPYKSKKAVWHKLLSKQRRRAVVACFRMTPLYNLPTHRACNMFLESYKASWILTEDHSFEDRMIDDLSKAGEQEEEEEEVEEKKPDPLHQLVLHFSRTALTEKSKLDEDYLYMAYADIMAKSCHLEEGGENGEEGGEEEEVEVSFEEKEMEKQRLLYQQSRLHNRGAAEMVLQMISACKGETGAMVSSTLKLGISILNGGNAEVQQKMLDYLKDKKEVGFFQSIQALMQTCSVLDLNAFERQNKAEGLGMVNEDGTVINRQNGEKVMADDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISDFYWYYSGKDVIEEQGKRNFSKAMSVAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMMMKLAQDSSQIELLKELLDLQKDMVVMLLSLLEGNVVNGMIARQMVDMLVESSSNVEMILKFFDMFLKLKDIVGSEAFQDYVTDPRGLISKKDFQKAMDSQKQFTGPEIQFLLSCSEADENEMINCEEFANRFQEPARDIGFNVAVLLTNLSEHVPHDPRLRNFLELAESILEYFRPYLGRIEIMGASRRIERIYFEISETNRAQWEMPQVKESKRQFIFDVVNEGGESEKMEMFVSFCEDTIFEMQIAAQISEPEGEPEEDEDEGAEEAEEGAAGSDGSGSAAAAGVWVWLAATAGRTLRGLSYRSLRRRVRRLRRLTAREAATAVAALLWALVTRAGGAGAGAAAGALRLLWGSLFGGGLVDSAKKVTVTELLAGMPDPTGDEVHGQQPSGAGSDAEGEGEGEGEGDAADGAGDEEAAADQAGTGGADGAVAVADGSPFRPEGAGGLGDMGDTTPVEPPTPEGSPILKRKLGVDGEEEEPPPEPEPEPEPEPEKADTENGEKEVPEPPPEPPKKTPPPPPPKKEEAGGAGLEEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDIEGSGAGDMSGAGSGDGSGWGSRAGEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVIFKREKELARKLEFDGLYITEQPEDDDVKGQWDRLVLNTPSFPSNYWDKFVKRKVLDKHGDIFGRERIAELLGMDLASLEITAHNERKPDPPPGLLTWIMSIDVKYQIWKFGVIFTDNSFLYLGWYMVMSLLGHYNNFFFAAHLLDIAMGVKTLRTILSSVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDEYELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGSDYFDTTPHGFETHTLEEHNLANYMFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLS |
| Enzyme Length | 5035 |
| Uniprot Accession Number | E9PZQ0 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Channel activity is modulated by the alkaloid ryanodine that binds to the open Ca-release channel with high affinity. At low concentrations, ryanodine maintains the channel in an open conformation. High ryanodine concentrations inhibit channel activity (PubMed:7621815). Channel activity is regulated by calmodulin (CALM). The calcium release is activated by increased cytoplasmic calcium levels, by nitric oxyde (NO), caffeine and ATP (PubMed:7621815, PubMed:22036948, PubMed:21156754). Channel activity is inhibited by magnesium ions, possibly by competition for calcium binding sites. {ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:7621815}. |
| Binding Site | BINDING 4714; /note=Caffeine; /evidence=ECO:0000250|UniProtKB:P11716 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:18003898, PubMed:7515481, PubMed:7621815, PubMed:21156754). Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm (PubMed:18268335). Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain (PubMed:22036948). Required for normal embryonic development of muscle fibers and skeletal muscle (PubMed:7515481). Required for normal heart morphogenesis, skin development and ossification during embryogenesis (PubMed:18003898, PubMed:7515481). {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754, ECO:0000269|PubMed:22036948, ECO:0000269|PubMed:7515481, ECO:0000269|PubMed:7621815}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 4214..4218; /note=ATP; /evidence=ECO:0000250|UniProtKB:P11716; NP_BIND 4952..4957; /note=ATP; /evidence=ECO:0000250|UniProtKB:P11716; NP_BIND 4977..4983; /note=ATP; /evidence=ECO:0000250|UniProtKB:P11716 |
| Features | Binding site (1); Chain (1); Compositional bias (8); Domain (9); Intramembrane (1); Metal binding (3); Modified residue (8); Motif (1); Mutagenesis (2); Nucleotide binding (3); Region (11); Repeat (6); Sequence conflict (6); Topological domain (8); Transmembrane (6) |
| Keywords | ATP-binding;Calcium;Calcium channel;Calcium transport;Calmodulin-binding;Developmental protein;Ion channel;Ion transport;Ligand-gated ion channel;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Receptor;Reference proteome;Repeat;S-nitrosylation;Sarcoplasmic reticulum;Transmembrane;Transmembrane helix;Transport |
| Interact With | O55108; P49070; P26883 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:18003898, ECO:0000269|PubMed:7621815}; Multi-pass membrane protein {ECO:0000269|PubMed:18003898}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P11716}. Note=The number of predicted transmembrane domains varies between orthologs, but the 3D-structures show the presence of six transmembrane regions. Both N-terminus and C-terminus are cytoplasmic. {ECO:0000250|UniProtKB:P11716}. |
| Modified Residue | MOD_RES 1339; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:F1LMY4"; MOD_RES 2346; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:F1LMY4"; MOD_RES 2844; /note="Phosphoserine; by PKA and PKG"; /evidence="ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754, ECO:0007744|PubMed:21183079"; MOD_RES 3636; /note="S-nitrosocysteine"; /evidence="ECO:0000250|UniProtKB:P11716"; MOD_RES 4464; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:F1LMY4"; MOD_RES 4468; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:F1LMY4"; MOD_RES 4861; /note="Phosphotyrosine"; /evidence="ECO:0000250|UniProtKB:P21817"; MOD_RES 4864; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P21817" |
| Post Translational Modification | PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2844 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2844. {ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:21156754}.; PTM: Activated by reversible S-nitrosylation (PubMed:22036948). Repeated very high-level exercise increases S-nitrosylation. {ECO:0000250, ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:22036948}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10213392; 10444070; 10473538; 10736313; 10788707; 11159936; 11500519; 11784029; 11818962; 11852053; 11860456; 12023238; 12364321; 12376096; 12414688; 12640042; 12642598; 12654335; 12704193; 12732639; 12954602; 1315127; 14592808; 14592949; 14610273; 14660561; 14672973; 15033925; 15102471; 15280431; 15289441; 15313613; 15381065; 15469935; 15536090; 15619962; 15894801; 15972723; 16141072; 16246297; 16284304; 16357209; 16484216; 16602821; 16737973; 16762927; 16844763; 16920191; 17074386; 17118445; 17122579; 17158949; 1774073; 17925380; 17942409; 18089560; 18206662; 18215135; 18313230; 18322139; 18394989; 18403125; 18434328; 18434746; 18488020; 18556650; 18643873; 18650434; 18663468; 18676612; 18772199; 18927079; 19011160; 19033399; 19131108; 19198614; 19246389; 19398467; 19549818; 1967823; 1970795; 19802526; 19959667; 19966218; 20207743; 20427316; 20479108; 20479110; 20519450; 20576841; 20926377; 20961389; 20978128; 21150295; 21262876; 21267068; 21289290; 21441923; 21575570; 21646399; 21784520; 21803290; 21803293; 21825032; 21858002; 21896730; 21933672; 21969454; 22131268; 22139840; 22203976; 22231556; 22355118; 22411552; 22504960; 22505613; 22853897; 22939628; 22962299; 2300206; 23070698; 23071115; 23152933; 23159934; 23247505; 23278119; 23308296; 23413940; 23454728; 23463619; 23482488; 23509717; 23695157; 23785297; 23798496; 23818578; 23917616; 23918386; 23992453; 24123915; 24143248; 24194600; 2421615; 24325401; 24509862; 24703692; 24962901; 25239916; 25384984; 25548159; 25564733; 25619131; 25640239; 25874477; 26025922; 26114725; 26134413; 26462735; 26494785; 26575622; 26831464; 26910427; 27150455; 27382027; 27621462; 27655403; 27802169; 28465322; 28724790; 29130937; 29543863; 29593014; 29701772; 29949772; 30071129; 30236258; 30420428; 30563862; 30689883; 30770808; 30786075; 30870432; 31044239; 31107960; 31199454; 31607937; 3161450; 31804576; 32242214; 32499372; 32506037; 32693782; 32826313; 32883967; 32994313; 33037202; 33065384; 33176865; 34893614; 4600883; 7832748; 7931345; 7959768; 8288260; 8598910; 8618963; 8626432; 8812484; 8910220; 8943043; 9054435; 9124414; 9192302; 9204703; 9242641; 9384575; 9461216; 9472036; 9480761; 9489997; 9799464; 9817784; 9986730; |
| Motif | MOTIF 4892..4898; /note=Selectivity filter; /evidence=ECO:0000250|UniProtKB:P11716 |
| Gene Encoded By | |
| Mass | 565,039 |
| Kinetics | |
| Metal Binding | METAL 3896; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P11716; METAL 3970; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P11716; METAL 4999; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P11716 |
| Rhea ID | |
| Cross Reference Brenda |