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E9PZQ0

- RYR1_MOUSE

UniProt

E9PZQ0 - RYR1_MOUSE

Protein

Ryanodine receptor 1

Gene

Ryr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (05 Apr 2011)
      Previous versions | rss
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    Functioni

    Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca2+ leaking into the cytoplasm. Can also mediate the release of Ca2+ from intracellular stores in neurons, and may thereby promote prolonged Ca2+ signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis.6 Publications

    GO - Molecular functioni

    1. calcium channel activity Source: UniProtKB
    2. calcium ion binding Source: InterPro
    3. enzyme binding Source: BHF-UCL
    4. protease binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. ryanodine-sensitive calcium-release channel activity Source: UniProtKB
    7. voltage-gated calcium channel activity Source: UniProtKB

    GO - Biological processi

    1. calcium ion transport Source: MGI
    2. cellular response to caffeine Source: UniProtKB
    3. muscle contraction Source: UniProtKB
    4. ossification involved in bone maturation Source: UniProtKB
    5. outflow tract morphogenesis Source: UniProtKB
    6. regulation of muscle contraction Source: MGI
    7. release of sequestered calcium ion into cytosol Source: MGI
    8. release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: UniProtKB
    9. response to hypoxia Source: Ensembl
    10. skeletal muscle fiber development Source: UniProtKB
    11. skin development Source: UniProtKB

    Keywords - Molecular functioni

    Calcium channel, Developmental protein, Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium, Calmodulin-binding

    Enzyme and pathway databases

    ReactomeiREACT_196640. Stimuli-sensing channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ryanodine receptor 1
    Short name:
    RYR-1
    Short name:
    RyR1
    Alternative name(s):
    Skeletal muscle calcium release channel
    Skeletal muscle ryanodine receptor
    Skeletal muscle-type ryanodine receptor
    Type 1 ryanodine receptor
    Gene namesi
    Name:Ryr1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:99659. Ryr1.

    Subcellular locationi

    Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Membrane Curated; Multi-pass membrane protein Curated
    Note: The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic.

    GO - Cellular componenti

    1. cell cortex Source: Ensembl
    2. I band Source: Ensembl
    3. integral component of membrane Source: UniProtKB-KW
    4. junctional membrane complex Source: MGI
    5. membrane Source: MGI
    6. protein complex Source: UniProtKB
    7. sarcoplasmic reticulum Source: MGI
    8. sarcoplasmic reticulum membrane Source: UniProtKB
    9. smooth endoplasmic reticulum Source: MGI
    10. T-tubule Source: MGI

    Keywords - Cellular componenti

    Membrane, Sarcoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    Perinatal lethality, due to severe defects in skeletal muscle development. Neonates do not breathe and do not move. Mutant mice show defects in muscle fiber development. Their muscles do not show a contractile response to electrical stimulation. In addition, mice display abnormal curvature of the spine, thin limbs, and an abnormal rib cage.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi165 – 1651R → C: Increased channel activity, leading to permanently increased cytoplasmic Ca(2+) levels. Increased activation by calcium, and increased ryanodine binding. 1 Publication
    Mutagenesisi4895 – 48951I → T: Causes paralysis and perinatal death in homozygous mice, apparently due to asphyxia. Mutant mice have greatly reduced and amorphous skeletal muscle. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 50355035Ryanodine receptor 1PRO_0000415566Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2844 – 28441Phosphoserine; by PKA and PKG2 Publications
    Modified residuei3636 – 36361S-nitrosocysteineBy similarity
    Modified residuei4861 – 48611PhosphotyrosineBy similarity
    Modified residuei4864 – 48641PhosphoserineBy similarity

    Post-translational modificationi

    Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2844 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2844.2 Publications
    Activated by reversible S-nitrosylation By similarity. Repeated very high-level exercise increases S-nitrosylation.By similarity1 Publication

    Keywords - PTMi

    Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiE9PZQ0.
    PRIDEiE9PZQ0.

    PTM databases

    PhosphoSiteiE9PZQ0.

    Expressioni

    Tissue specificityi

    Detected in muscle and myotubes (at protein level). Ubiquitous. Detected in diaphragm, skeletal muscle, esophagus, spleen, submaxillary gland, adrenal gland, cerebellum, brain and in testis germ cells.4 Publications

    Gene expression databases

    ArrayExpressiE9PZQ0.
    BgeeiE9PZQ0.
    GenevestigatoriQ62235.

    Interactioni

    Subunit structurei

    Homotetramer. Can also form heterotetramers with RYR2. Interacts with CALM; CALM with bound calcium inhibits the RYR1 channel activity. Interacts with S100A1. Interacts with FKBP1A; this stabilizes the closed conformation of the channel. Interacts with CACNA1S; interaction with CACNA1S is important for activation of the RYR1 channel. Interacts with CACNB1. Interacts with TRDN and ASPH; these interactions stimulate RYR1 channel activity By similarity. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Repeated very high-level exercise decreases interaction with PDE4D and protein phosphatase 1 (PP1).By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BsgO551083EBI-642079,EBI-643315
    CamlgP490703EBI-642079,EBI-309114

    Protein-protein interaction databases

    DIPiDIP-29705N.
    IntActiE9PZQ0. 27 interactions.
    STRINGi10090.ENSMUSP00000032813.

    Structurei

    3D structure databases

    ProteinModelPortaliE9PZQ0.
    SMRiE9PZQ0. Positions 13-535, 2735-2941, 3615-3641.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 43234323CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini4939 – 503597CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei4888 – 489710Pore-formingBy similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4324 – 434421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4345 – 436521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4557 – 457721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4649 – 466921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4778 – 479821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4805 – 482521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4837 – 485721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4918 – 493821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini99 – 15456MIR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini161 – 20646MIR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini212 – 26655MIR 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini272 – 32958MIR 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini337 – 39458MIR 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini583 – 799217B30.2/SPRY 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati843 – 9561141Add
    BLAST
    Repeati957 – 10701142Add
    BLAST
    Domaini1015 – 1210196B30.2/SPRY 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati1346 – 1361163; truncatedAdd
    BLAST
    Domaini1359 – 1572214B30.2/SPRY 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati1374 – 1389164; truncatedAdd
    BLAST
    Repeati2727 – 28461205Add
    BLAST
    Repeati2847 – 29601146Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni843 – 296021186 X approximate repeatsAdd
    BLAST
    Regioni3615 – 364430Interaction with CALMBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1869 – 2089221Glu-richAdd
    BLAST
    Compositional biasi3683 – 376280Glu-richAdd
    BLAST
    Compositional biasi4459 – 452567Pro-richAdd
    BLAST

    Domaini

    The calcium release channel activity resides in the C-terminal region while the remaining part of the protein constitutes the 'foot' structure spanning the junctional gap between the sarcoplasmic reticulum (SR) and the T-tubule.1 Publication

    Sequence similaritiesi

    Contains 3 B30.2/SPRY domains.PROSITE-ProRule annotation
    Contains 5 MIR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00690000101961.
    HOGENOMiHOG000231428.
    HOVERGENiHBG102939.
    KOiK04961.
    OMAiQCSATVL.
    OrthoDBiEOG71K622.
    TreeFamiTF315244.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.25.10.30. 1 hit.
    InterProiIPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR011992. EF-hand-dom_pair.
    IPR014821. Ins145_P3_rcpt.
    IPR005821. Ion_trans_dom.
    IPR016093. MIR_motif.
    IPR013662. RIH_assoc-dom.
    IPR000699. RIH_dom.
    IPR013333. Ryan_recept.
    IPR003032. Ryanodine_rcpt.
    IPR015925. Ryanodine_recept-rel.
    IPR009460. Ryanrecept_TM4-6.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view]
    PANTHERiPTHR13715. PTHR13715. 1 hit.
    PfamiPF08709. Ins145_P3_rec. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF02815. MIR. 1 hit.
    PF08454. RIH_assoc. 1 hit.
    PF06459. RR_TM4-6. 1 hit.
    PF01365. RYDR_ITPR. 2 hits.
    PF02026. RyR. 4 hits.
    PF00622. SPRY. 3 hits.
    [Graphical view]
    PRINTSiPR00795. RYANODINER.
    SMARTiSM00472. MIR. 4 hits.
    SM00449. SPRY. 3 hits.
    [Graphical view]
    SUPFAMiSSF100909. SSF100909. 2 hits.
    SSF49899. SSF49899. 3 hits.
    SSF82109. SSF82109. 2 hits.
    PROSITEiPS50188. B302_SPRY. 3 hits.
    PS50919. MIR. 5 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    E9PZQ0-1 [UniParc]FASTAAdd to Basket

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    MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL     50
    EPTSNAQNVP PDLAICCFIL EQSLSVRALQ EMLANTVEAG VESSQGGGHR 100
    TLLYGHAILL RHAHSRMYLS CLTTSRSMTD KLAFDVGLQE DATGEACWWT 150
    MHPASKQRSE GEKVRVGDDL ILVSVSSERY LHLSTASGEL QVDASFMQTL 200
    WNMNPICSGC EEGFVTGGHV LRLFHGHMDE CLTISPSDSD DQRRLVYYEG 250
    GPVCTHARSL WRLEPLRISW SGSHLRWGQP LRIRHVTTGR YLGLTEDQGL 300
    VVVDASKAHT KATSFCFRIS KEKLDVAPKR DVEGMGPPEI KYGESLCFVQ 350
    HVASGLWLTY AAPDPKALRL GVLKKKAMLH QEGHMDDALS LTRCQQEESQ 400
    AARMIYSTAG LYNQFIKGLD SFSGKPRGSG PPAGSALPIE GVILSLQDLI 450
    GYFEPPSEEL QHEEKQTKLR SLRNRQSLFQ EEGMLSLVLN CIDRLNVYTT 500
    AAHFAEFAGE EAAESWKEIV NLLYELLASL IRGNRTNCAL FSTNLDWLVS 550
    KLDRLEASSG ILEVLYCVLI ESPEVLNIIQ ENHIKSIISL LDKHGRNHKV 600
    LDVLCSLCVC NGVAVRSNQD LITENLLPGR ELLLQTNLIN YVTSIRPNIF 650
    VGRAEGSTQY GKWYFEVMVD EVAPFLTAQA THLRVGWALS EGYSPYPGGG 700
    EGWGGNGVGD DLYSYGFDGL HLWTGHVARP VTSPGQHLLA PEDVVSCCLD 750
    LSVPSISFRI NGCPVQGVFE SFNLDGLFFP VVSFSAGIKV RFLLGGRHGE 800
    FKFLPPPGYA PCHEAVLPRE RLHLQPIKEY RREGPRGPHL VGPSRCLSHL 850
    DFVPCPVDTI QIVLPPHLER IREKLAENIH ELWALTRIEQ GWTYGPVRDD 900
    NKRLHPCLVN FHSLPEPERN YNLQMSGETL KTLLALGCHV GMADEKAEDN 950
    LKKTKLPKTY MMSNGYKPAP LDLSHVRLTP AQTTLVDRLA ENGHNVWARD 1000
    RVAQGWSYSA VQDIPARRNP RLVPYRLLDE ATKRSNRDSL CQAVRTLLGY 1050
    GYNIEPPDQE PSQVDSQSRG DRARIFRAEK SYAVQSGRWY FEFEAVTTGE 1100
    MRVGWARPEL RPDVELGADD LAYVFNGHRG QRWHLGSEPF GRPWQSGDVV 1150
    GCMIDLTENT IIFTLNGEVL MSDSGSETAF RDIEIGDGFL PVCSLGPGQV 1200
    GHLNLGQDVS SLRFFAICGL QEGFEPFAIN MQRPVTTWFS KSLPQFEPVP 1250
    LEHPHYEVAR MDGTVDTPPC LRLTHRTWGS QNSLVEMLFL RLSLPVQFHQ 1300
    HFRCTAGATP LASPGLQPPA EDEARAAEPD TDYENLRRSA GGWGEAEGGK 1350
    DGTAKEGTPG GTAQAGVEAQ PARAENEKDA TTEKNKKRGF LFKAKKVAMM 1400
    TQPPSTPALP RLPRDVVPAD NRDDPEIILN TTTYYYSVRV FAGQEPSCVW 1450
    VGWVTPDYHQ HDMSFDLSKV RAVTVTMGDE QGNVHSSLKC SNCYMVWGGD 1500
    FVSPGQQGRI SHTDLVIGCL VDLATGLMTF TANGKESNTF FQVEPNTKLF 1550
    PAVFVLPTHQ NVVQFELGKQ KNIMPLSAAM FLSERKNPAP QCPPRLEVQM 1600
    LMPVSWSRMP NHFLQVDTRR AGERLGWAVQ CQEPLMMMAL HIPEENRCMD 1650
    ILELSERLDL QRFHSHTLSL YRSVCALGNN RVAHALCSHV DQAQLLHALE 1700
    DARLPGPLRA GYYDLLISIH LESACRSRRS MLSEYIVPLT PETRAITLFP 1750
    PGRSAEDGPR RHGLPGVGVT TSLRPPHHFS PPCFVVALPA AGATEAPARL 1800
    SPAIPLEALR DKALRMLGEA VRDGGQHARD PVGGSVEFQF VPVLKLVSTL 1850
    LVMGVFSDED VKQILKMIEP EVFREEEEVE EEGEEEEEDE EEKEEDEEEE 1900
    AHEKEDEEKE EAEDAAEEEK EELEEGLLQM KLPESVKLQM CHLLEYFCDQ 1950
    ELQHRVESLA AFAECYVDKM QGNQRGRYGL LMKAFTMSAA ETARRTREFR 2000
    SPPQEQINML LHFKNGADEE ECPLPEEIRQ ELVNFHQDLL AHCGIQLEGE 2050
    EEEPEEESTL GSRLMSLLEK VKLVKKTEEK PEEEPAPEEH KPQSLQELVS 2100
    HTVVRWAQED FVQSPELVRA MFSLLHRQYD GLGELLRALP RAYTISVSSV 2150
    EDTMSLLECL GQIRSLLIVQ MGPQEENLMI QSIGNIMNNK VFYQHPNLMR 2200
    ALGMHETVME VMVNVLGGGE SKEIRFPKMV TSCCRFLCYF CRISRQNQRS 2250
    MFDHLSYLLE NSGIGLGMQG STPLDVAAAS VIDNNELALA LQEQDLEKVV 2300
    SYLAGCGLQS CPMLLAKGYP DIGWNPCGGE RYLDFLRFAV FVNGESVEEN 2350
    ANVVVRLLIR KPECFGPALR GEGGSGLLAA IEEAIRISED PARDGPGVRR 2400
    DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE THLIQAGKGE 2450
    ALRIRAILRS LVPLDDLVGI ISLPLQIPTL GKDGALVQPK MSASFVPDHK 2500
    ASMVLFLDRV YGIENQDFLL HVLDVGFLPD MRAAASLDTA TFSTTEMALA 2550
    LNRYLCLAVL PLITKCAPLF AGTEHRAIMV DSMLHTVYRL SRGRSLTKAQ 2600
    RDVIEDCLMA LCRYIRPSML QHLLRRLVFD VPILNEFAKM PLKLLTNHYE 2650
    RCWKYYCLPT GWANFGVTSE EELHLTRKLF WGIFDSLAHK KYDQELYRIA 2700
    MPCLCAIAGA LPPDYVDASY SSKTEKKATV DAEGNFDPRP VETLNVIIPE 2750
    KLDSFINKFA EYTHEKWAFD KIQNNWSYGE NIDEELKTHP MLRPYKTFSE 2800
    KDKEIYRWPI KESLKAMIAW EWTVEKAREG EEEKTEKKKT RKISQTAQTY 2850
    DPREGYNPQP PDLSVVTLSR ELQAMAEQLA ENYHNTWGRK KKQELEAKGG 2900
    GSHPLLVPYD TLTAKEKARD REKAQELLKF LQMNGYAVTR GLKDMELDTS 2950
    SIEKRFAFGF LQQLLRWMDI SQEFIAHLEA VVSSGRVEKS PHEQEIKFFA 3000
    KILLPLINQY FTNHCLYFLS TPAKVLGSGG HASNKEKEMI TSLFCKLAAL 3050
    VRHRVSLFGT DAPAVVNCLH ILARSLDART VMKSGPEIVK AGLRSFFESA 3100
    SEDIEKMVEN LRLGKVSQAR TQVKGVGQNL TYTTVALLPV LTTLFQHIAQ 3150
    HQFGDDVILD DVQVSCYRTL CSIYSLGTTR NPYVEKLRPA LGECLARLAA 3200
    AMPVAFLEPE LNEYNACSVY TTKSPRERAI LGLPNSVEEM CPDIPVLERL 3250
    MAEIGGLAES GARYTEMPHV IEITLPMLCS YLPRWWERGP EAPPPALPAG 3300
    APPPCTAVTS DHLNSLLGNI LRIIVNNLGI DEASWMKRLA VFAQPIVSRA 3350
    RPELLRSHFI PTIGRLRKRA GKVVAEEEQL RLEAKAEAEE GELLVRDEFS 3400
    VLCRDLYALY PLLIRYVDNN RAHWLTEPNP NAEELFRMVG EIFIYWSKSH 3450
    NFKREEQNFV VQNEINNMSF LTADNKSKMA KAGDVQSGGS DQERTKKKRR 3500
    GDRYSVQTSL IVATLKKMLP IGLNMCAPTD QDLIVLAKAR YALKDTDEEV 3550
    REFLQNNLNL QGKVEGSPSL RWQMALYRGV PGREEDADDP EKIVRRVQEV 3600
    SAVLYHLDQT EHPYKSKKAV WHKLLSKQRR RAVVACFRMT PLYNLPTHRA 3650
    CNMFLESYKA SWILTEDHSF EDRMIDDLSK AGEQEEEEEE VEEKKPDPLH 3700
    QLVLHFSRTA LTEKSKLDED YLYMAYADIM AKSCHLEEGG ENGEEGGEEE 3750
    EVEVSFEEKE MEKQRLLYQQ SRLHNRGAAE MVLQMISACK GETGAMVSST 3800
    LKLGISILNG GNAEVQQKML DYLKDKKEVG FFQSIQALMQ TCSVLDLNAF 3850
    ERQNKAEGLG MVNEDGTVIN RQNGEKVMAD DEFTQDLFRF LQLLCEGHNN 3900
    DFQNYLRTQT GNTTTINIII CTVDYLLRLQ ESISDFYWYY SGKDVIEEQG 3950
    KRNFSKAMSV AKQVFNSLTE YIQGPCTGNQ QSLAHSRLWD AVVGFLHVFA 4000
    HMMMKLAQDS SQIELLKELL DLQKDMVVML LSLLEGNVVN GMIARQMVDM 4050
    LVESSSNVEM ILKFFDMFLK LKDIVGSEAF QDYVTDPRGL ISKKDFQKAM 4100
    DSQKQFTGPE IQFLLSCSEA DENEMINCEE FANRFQEPAR DIGFNVAVLL 4150
    TNLSEHVPHD PRLRNFLELA ESILEYFRPY LGRIEIMGAS RRIERIYFEI 4200
    SETNRAQWEM PQVKESKRQF IFDVVNEGGE SEKMEMFVSF CEDTIFEMQI 4250
    AAQISEPEGE PEEDEDEGAE EAEEGAAGSD GSGSAAAAGV WVWLAATAGR 4300
    TLRGLSYRSL RRRVRRLRRL TAREAATAVA ALLWALVTRA GGAGAGAAAG 4350
    ALRLLWGSLF GGGLVDSAKK VTVTELLAGM PDPTGDEVHG QQPSGAGSDA 4400
    EGEGEGEGEG DAADGAGDEE AAADQAGTGG ADGAVAVADG SPFRPEGAGG 4450
    LGDMGDTTPV EPPTPEGSPI LKRKLGVDGE EEEPPPEPEP EPEPEPEKAD 4500
    TENGEKEVPE PPPEPPKKTP PPPPPKKEEA GGAGLEEFWG ELEVQRVKFL 4550
    NYLSRNFYTL RFLALFLAFA INFILLFYKV SDSPPGEDDI EGSGAGDMSG 4600
    AGSGDGSGWG SRAGEEVEGD EDENMVYYFL EESTGYMEPA LRCLSLLHTL 4650
    VAFLCIIGYN CLKVPLVIFK REKELARKLE FDGLYITEQP EDDDVKGQWD 4700
    RLVLNTPSFP SNYWDKFVKR KVLDKHGDIF GRERIAELLG MDLASLEITA 4750
    HNERKPDPPP GLLTWIMSID VKYQIWKFGV IFTDNSFLYL GWYMVMSLLG 4800
    HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT 4850
    VVAFNFFRKF YNKSEDEDEP DMKCDDMMTC YLFHMYVGVR AGGGIGDEIE 4900
    DPAGDEYELY RVVFDITFFF FVIVILLAII QGLIIDAFGE LRDQQEQVKE 4950
    DMETKCFICG IGSDYFDTTP HGFETHTLEE HNLANYMFFL MYLINKDETE 5000
    HTGQESYVWK MYQERCWDFF PAGDCFRKQY EDQLS 5035
    Length:5,035
    Mass (Da):565,039
    Last modified:April 5, 2011 - v1
    Checksum:iD15D2E764B445573
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti616 – 6161R → C in CAC34624. 1 PublicationCurated
    Sequence conflicti1380 – 13801A → S in AAP29981. (PubMed:18003898)Curated
    Sequence conflicti3484 – 34841D → V in AAP29981. (PubMed:18003898)Curated
    Sequence conflicti4766 – 47661I → L in AAA64955. (PubMed:7635066)Curated
    Sequence conflicti4821 – 48211L → V in CAA58784. (PubMed:7876312)Curated
    Sequence conflicti4888 – 48881G → A in CAA58784. (PubMed:7876312)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY268935 mRNA. Translation: AAP29981.1.
    AC164564 Genomic DNA. No translation available.
    AC165142 Genomic DNA. No translation available.
    D21798 Genomic DNA. Translation: BAA21010.1.
    D21796 mRNA. Translation: BAA04821.1.
    D21797 Genomic DNA. Translation: BAA04822.1.
    AJ308737 Genomic DNA. Translation: CAC34624.1.
    BC051248 mRNA. Translation: AAH51248.1.
    BC055487 mRNA. Translation: AAH55487.1.
    X83932 mRNA. Translation: CAA58784.1.
    U23754 mRNA. Translation: AAA64955.1.
    D38216 mRNA. Translation: BAA07391.1.
    CCDSiCCDS39866.1.
    PIRiI48741.
    I58087.
    I78376.
    I78377.
    S56105.
    RefSeqiNP_033135.2. NM_009109.2.
    UniGeneiMm.439745.

    Genome annotation databases

    EnsembliENSMUST00000179893; ENSMUSP00000137123; ENSMUSG00000030592.
    GeneIDi20190.
    KEGGimmu:20190.
    UCSCiuc009gao.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY268935 mRNA. Translation: AAP29981.1 .
    AC164564 Genomic DNA. No translation available.
    AC165142 Genomic DNA. No translation available.
    D21798 Genomic DNA. Translation: BAA21010.1 .
    D21796 mRNA. Translation: BAA04821.1 .
    D21797 Genomic DNA. Translation: BAA04822.1 .
    AJ308737 Genomic DNA. Translation: CAC34624.1 .
    BC051248 mRNA. Translation: AAH51248.1 .
    BC055487 mRNA. Translation: AAH55487.1 .
    X83932 mRNA. Translation: CAA58784.1 .
    U23754 mRNA. Translation: AAA64955.1 .
    D38216 mRNA. Translation: BAA07391.1 .
    CCDSi CCDS39866.1.
    PIRi I48741.
    I58087.
    I78376.
    I78377.
    S56105.
    RefSeqi NP_033135.2. NM_009109.2.
    UniGenei Mm.439745.

    3D structure databases

    ProteinModelPortali E9PZQ0.
    SMRi E9PZQ0. Positions 13-535, 2735-2941, 3615-3641.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29705N.
    IntActi E9PZQ0. 27 interactions.
    STRINGi 10090.ENSMUSP00000032813.

    Chemistry

    BindingDBi E9PZQ0.
    ChEMBLi CHEMBL2133.

    PTM databases

    PhosphoSitei E9PZQ0.

    Proteomic databases

    MaxQBi E9PZQ0.
    PRIDEi E9PZQ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000179893 ; ENSMUSP00000137123 ; ENSMUSG00000030592 .
    GeneIDi 20190.
    KEGGi mmu:20190.
    UCSCi uc009gao.1. mouse.

    Organism-specific databases

    CTDi 6261.
    MGIi MGI:99659. Ryr1.

    Phylogenomic databases

    GeneTreei ENSGT00690000101961.
    HOGENOMi HOG000231428.
    HOVERGENi HBG102939.
    KOi K04961.
    OMAi QCSATVL.
    OrthoDBi EOG71K622.
    TreeFami TF315244.

    Enzyme and pathway databases

    Reactomei REACT_196640. Stimuli-sensing channels.

    Miscellaneous databases

    NextBioi 297735.
    PROi E9PZQ0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi E9PZQ0.
    Bgeei E9PZQ0.
    Genevestigatori Q62235.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.25.10.30. 1 hit.
    InterProi IPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR011992. EF-hand-dom_pair.
    IPR014821. Ins145_P3_rcpt.
    IPR005821. Ion_trans_dom.
    IPR016093. MIR_motif.
    IPR013662. RIH_assoc-dom.
    IPR000699. RIH_dom.
    IPR013333. Ryan_recept.
    IPR003032. Ryanodine_rcpt.
    IPR015925. Ryanodine_recept-rel.
    IPR009460. Ryanrecept_TM4-6.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view ]
    PANTHERi PTHR13715. PTHR13715. 1 hit.
    Pfami PF08709. Ins145_P3_rec. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF02815. MIR. 1 hit.
    PF08454. RIH_assoc. 1 hit.
    PF06459. RR_TM4-6. 1 hit.
    PF01365. RYDR_ITPR. 2 hits.
    PF02026. RyR. 4 hits.
    PF00622. SPRY. 3 hits.
    [Graphical view ]
    PRINTSi PR00795. RYANODINER.
    SMARTi SM00472. MIR. 4 hits.
    SM00449. SPRY. 3 hits.
    [Graphical view ]
    SUPFAMi SSF100909. SSF100909. 2 hits.
    SSF49899. SSF49899. 3 hits.
    SSF82109. SSF82109. 2 hits.
    PROSITEi PS50188. B302_SPRY. 3 hits.
    PS50919. MIR. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "An Ryr1I4895T mutation abolishes Ca2+ release channel function and delays development in homozygous offspring of a mutant mouse line."
      Zvaritch E., Depreux F., Kraeva N., Loy R.E., Goonasekera S.A., Boncompagni S., Kraev A., Gramolini A.O., Dirksen R.T., Franzini-Armstrong C., Seidman C.E., Seidman J.G., MacLennan D.H.
      Proc. Natl. Acad. Sci. U.S.A. 104:18537-18542(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ILE-4895.
      Strain: BALB/c X CD-1.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene."
      Takeshima H., Iino M., Takekura H., Nishi M., Kuno J., Minowa O., Takano H., Noda T.
      Nature 369:556-559(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, NUCLEOTIDE SEQUENCE [MRNA] OF 1-27, FUNCTION, DISRUPTION PHENOTYPE.
      Strain: 129/J and BALB/c.
      Tissue: Skeletal muscle.
    4. "Characterisation of the murine Ryr1 gene."
      Kathirvel P.
      Thesis (2000), University of Edinburgh, United Kingdom
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 483-861.
      Strain: 129.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4500-5035.
      Strain: FVB/N-3.
      Tissue: Eye and Mammary tumor.
    6. "The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues."
      Giannini G., Conti A., Mammarella S., Scrobogna M., Sorrentino V.
      J. Cell Biol. 128:893-904(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4537-5035, TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Brain.
    7. "Regulation of mouse egg activation: presence of ryanodine receptors and effects of microinjected ryanodine and cyclic ADP ribose on uninseminated and inseminated eggs."
      Ayabe T., Kopf G.S., Schultz R.M.
      Development 121:2233-2244(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4762-5013.
      Tissue: Brain.
    8. "Ca(2+)-induced Ca2+ release in myocytes from dyspedic mice lacking the type-1 ryanodine receptor."
      Takeshima H., Yamazawa T., Ikemoto T., Takekura H., Nishi M., Noda T., Iino M.
      EMBO J. 14:2999-3006(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4913-5035, FUNCTION, TISSUE SPECIFICITY.
      Strain: C57BL/6J.
      Tissue: Skeletal muscle.
    9. "Abnormal junctions between surface membrane and sarcoplasmic reticulum in skeletal muscle with a mutation targeted to the ryanodine receptor."
      Takekura H., Nishi M., Noda T., Takeshima H., Franzini-Armstrong C.
      Proc. Natl. Acad. Sci. U.S.A. 92:3381-3385(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, DOMAIN.
    10. "Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity."
      Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.
      Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-2844, S-NITROSYLATION, IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; FKBP1A AND PROTEIN PHOSPHATASE 1.
    11. "Nitric oxide-induced calcium release via ryanodine receptors regulates neuronal function."
      Kakizawa S., Yamazawa T., Chen Y., Ito A., Murayama T., Oyamada H., Kurebayashi N., Sato O., Watanabe M., Mori N., Oguchi K., Sakurai T., Takeshima H., Saito N., Iino M.
      EMBO J. 31:417-428(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BRAIN, TISSUE SPECIFICITY.
    12. "Functional and biochemical properties of ryanodine receptor type 1 channels from heterozygous R163C malignant hyperthermia-susceptible mice."
      Feng W., Barrientos G.C., Cherednichenko G., Yang T., Padilla I.T., Truong K., Allen P.D., Lopez J.R., Pessah I.N.
      Mol. Pharmacol. 79:420-431(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-165, PHOSPHORYLATION AT SER-2844.
    13. "Ryanodine receptor studies using genetically engineered mice."
      Kushnir A., Betzenhauser M.J., Marks A.R.
      FEBS Lett. 584:1956-1965(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiRYR1_MOUSE
    AccessioniPrimary (citable) accession number: E9PZQ0
    Secondary accession number(s): Q60834
    , Q61779, Q61780, Q62173, Q62196, Q62235, Q78EJ6, Q7TNG1, Q80UQ5, Q80X16, Q99JF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: April 5, 2011
    Last modified: October 1, 2014
    This is version 36 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    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. Channel activity is regulated by calmodulin (CALM). The calcium release is activated by increased cytoplasmic calcium levels, by nitric oxyde (NO), caffeine and ATP. Channel activity is inhibited by magnesium ions, possibly by competition for calcium binding sites.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3