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E9Q401

- RYR2_MOUSE

UniProt

E9Q401 - RYR2_MOUSE

Protein

Ryanodine receptor 2

Gene

Ryr2

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 cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca2+ levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development.4 Publications

    GO - Molecular functioni

    1. binding Source: MGI
    2. calcium channel activity Source: UniProtKB
    3. calcium-induced calcium release activity Source: Ensembl
    4. calcium ion binding Source: InterPro
    5. calmodulin binding Source: MGI
    6. enzyme binding Source: BHF-UCL
    7. intracellular ligand-gated calcium channel activity Source: UniProtKB
    8. protein binding Source: IntAct
    9. protein kinase binding Source: BHF-UCL
    10. protein self-association Source: UniProtKB
    11. ryanodine-sensitive calcium-release channel activity Source: MGI
    12. suramin binding Source: Ensembl

    GO - Biological processi

    1. BMP signaling pathway Source: MGI
    2. calcium ion transmembrane transport Source: MGI
    3. calcium ion transport Source: UniProtKB
    4. calcium-mediated signaling Source: UniProtKB
    5. calcium-mediated signaling using intracellular calcium source Source: Ensembl
    6. canonical Wnt signaling pathway Source: MGI
    7. cardiac muscle contraction Source: Ensembl
    8. cardiac muscle hypertrophy Source: MGI
    9. cellular calcium ion homeostasis Source: UniProtKB
    10. cellular response to caffeine Source: UniProtKB
    11. cytosolic calcium ion transport Source: MGI
    12. detection of calcium ion Source: Ensembl
    13. embryonic heart tube morphogenesis Source: UniProtKB
    14. establishment of protein localization to endoplasmic reticulum Source: Ensembl
    15. left ventricular cardiac muscle tissue morphogenesis Source: MGI
    16. positive regulation of calcium-transporting ATPase activity Source: Ensembl
    17. positive regulation of heart rate Source: MGI
    18. positive regulation of ryanodine-sensitive calcium-release channel activity by adrenergic receptor signaling pathway involved in positive regulation of cardiac muscle contraction Source: BHF-UCL
    19. positive regulation of sequestering of calcium ion Source: Ensembl
    20. Purkinje myocyte to ventricular cardiac muscle cell signaling Source: BHF-UCL
    21. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
    22. regulation of heart rate Source: BHF-UCL
    23. release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    24. response to caffeine Source: UniProtKB
    25. response to hypoxia Source: BHF-UCL
    26. response to redox state Source: Ensembl
    27. type B pancreatic cell apoptotic process Source: BHF-UCL
    28. ventricular cardiac muscle cell action potential Source: BHF-UCL

    Keywords - Molecular functioni

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

    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 2
    Short name:
    RYR-2
    Short name:
    RyR2
    Alternative name(s):
    Cardiac muscle ryanodine receptor
    Cardiac muscle ryanodine receptor-calcium release channel
    Type 2 ryanodine receptor
    Gene namesi
    Name:Ryr2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:99685. Ryr2.

    Subcellular locationi

    Sarcoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic.By similarity

    GO - Cellular componenti

    1. calcium channel complex Source: BHF-UCL
    2. integral component of membrane Source: MGI
    3. membrane Source: MGI
    4. protein complex Source: MGI
    5. sarcomere Source: BHF-UCL
    6. sarcoplasmic reticulum Source: BHF-UCL
    7. sarcoplasmic reticulum membrane Source: MGI
    8. smooth endoplasmic reticulum Source: MGI
    9. Z disc Source: MGI

    Keywords - Cellular componenti

    Membrane, Sarcoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    Embryonically lethal. Embryos die at about 10 dpc, due to defects in heart tube development. Cardiac myotubes display enlarged rough endoplasmic reticulum and cytoplasmic vesicles that contain high levels of Ca2+.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi77 – 771A → V: No change to global protein fold or protein stability. Alters local protein folding. 1 Publication
    Mutagenesisi186 – 1861V → M: No change to global protein fold or protein stability. Alters local protein folding. 1 Publication
    Mutagenesisi2813 – 28131S → A: Protects against tachycardia and subsequent death due to heart failure. 1 Publication
    Mutagenesisi2813 – 28131S → D: Abolishes phosphorylation by CaMK2D. Tendency to tachycardia and subsequent death due to heart failure. 1 Publication
    Mutagenesisi4819 – 48191G → A: Strongly reduced calcium channel activity. Abolishes ryanodine binding. 1 Publication
    Mutagenesisi4821 – 48211R → A: No effect on calcium channel activity. Abolishes ryanodine binding. 1 Publication
    Mutagenesisi4823 – 48231G → A: Reduced calcium channel activity. Reduces single channel conductance by 97%. No effect on ryaodine binding. 1 Publication
    Mutagenesisi4824 – 48241G → A: No effect on calcium channel activity. Abolishes ryanodine binding. 1 Publication
    Mutagenesisi4825 – 48251G → A: Strongly reduced calcium channel activity. Abolishes ryanodine binding. 1 Publication
    Mutagenesisi4827 – 48271G → A: No effect on calcium channel activity. Abolishes ryanodine binding. 1 Publication
    Mutagenesisi4828 – 48281D → A: No effect on calcium channel activity. Abolishes ryanodine binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 49664966Ryanodine receptor 2PRO_0000415582Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2030 – 20301Phosphoserine; by PKA1 Publication
    Modified residuei2807 – 28071Phosphoserine; by CaMK2D and PKA2 Publications
    Modified residuei2813 – 28131Phosphoserine; by CaMK2D1 Publication

    Post-translational modificationi

    Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2807 and Ser-2813 increases the open probability of the calcium channel. Phosphorylation is increased in failing heart, leading to calcium leaks and increased cytoplasmic Ca2+ levels.3 Publications
    Phosphorylation at Ser-2030 by PKA enhances the response to lumenal calcium.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiE9Q401.
    PRIDEiE9Q401.

    PTM databases

    PhosphoSiteiE9Q401.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, lung, cerebellum and brain. Detected at lower levels in adrenal gland, stomach, thymus, esophagus and ovary.2 Publications

    Gene expression databases

    ArrayExpressiE9Q401.
    BgeeiE9Q401.

    Interactioni

    Subunit structurei

    Homotetramer. Can also form heterotetramers with RYR1 and RYR3. Interacts with CALM and S100A1; these interactions regulate channel activity. Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1. Interacts directly with FKBP1B, PKA, PP1 and PP2A By similarity. Interacts with FKBP1A and FKBP1B; these interactions may stabilize the channel in its closed state and prevent Ca2+ leaks.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Fkbp1bQ9Z2I22EBI-643628,EBI-6379859

    Protein-protein interaction databases

    IntActiE9Q401. 6 interactions.
    MINTiMINT-4129173.

    Structurei

    Secondary structure

    1
    4966
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 173
    Beta strandi19 – 2810
    Beta strandi31 – 388
    Beta strandi41 – 433
    Beta strandi48 – 514
    Turni53 – 575
    Helixi62 – 643
    Beta strandi67 – 737
    Helixi75 – 8410
    Beta strandi97 – 1026
    Beta strandi118 – 1236
    Turni124 – 1263
    Beta strandi129 – 1324
    Beta strandi145 – 1517
    Beta strandi154 – 1563
    Beta strandi159 – 1679
    Beta strandi180 – 1856
    Turni186 – 1883
    Beta strandi191 – 1966
    Beta strandi198 – 20811
    Beta strandi212 – 2165
    Helixi220 – 2223
    Beta strandi233 – 2386
    Turni239 – 2424
    Beta strandi243 – 2464
    Helixi256 – 2583
    Beta strandi261 – 2644
    Helixi265 – 2695
    Helixi271 – 2733
    Beta strandi275 – 2806
    Turni283 – 2864
    Beta strandi294 – 2996
    Turni300 – 3023
    Beta strandi305 – 3084
    Beta strandi314 – 3174
    Helixi319 – 3213
    Helixi324 – 3274
    Beta strandi329 – 3335
    Turni356 – 3583
    Beta strandi360 – 3656
    Turni366 – 3683
    Beta strandi371 – 3744
    Beta strandi389 – 3968
    Beta strandi403 – 4075
    Helixi410 – 43627
    Helixi449 – 46214
    Helixi472 – 49120
    Helixi494 – 50512
    Beta strandi508 – 5103
    Helixi511 – 5188
    Helixi520 – 54122
    Helixi2714 – 27163
    Helixi2717 – 273721
    Turni2748 – 27514
    Helixi2759 – 27613
    Helixi2764 – 278320
    Beta strandi2787 – 27904
    Helixi2796 – 27994
    Helixi2817 – 28193
    Helixi2827 – 28293
    Helixi2834 – 286128
    Helixi2873 – 28753
    Helixi2878 – 289720
    Beta strandi2900 – 29034

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MC2NMR-A10-224[»]
    3IM5X-ray2.55A/B1-217[»]
    3IM6X-ray1.70A1-217[»]
    3IM7X-ray2.21A1-217[»]
    3QR5X-ray2.30A/B1-217[»]
    4ETVX-ray1.65A/B2699-2904[»]
    4KEIX-ray2.41A1-217[»]
    4KEJX-ray2.55A1-217[»]
    4KEKX-ray2.15A1-217[»]
    4L4HX-ray2.00A1-547[»]
    4L4IX-ray2.15A1-547[»]
    ProteinModelPortaliE9Q401.
    SMRiE9Q401. Positions 10-544, 2700-2904, 3580-3606.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ERN6.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 42314231CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini4870 – 496697CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei4819 – 482810Pore-formingCurated

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4232 – 425221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4278 – 429821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4502 – 452221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4579 – 459921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4729 – 474921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4768 – 478821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4849 – 486921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini110 – 16556MIR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini172 – 21746MIR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini225 – 28056MIR 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini286 – 34358MIR 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini351 – 40858MIR 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini599 – 809211B30.2/SPRY 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati853 – 9661141Add
    BLAST
    Repeati967 – 10801142Add
    BLAST
    Domaini1025 – 1222198B30.2/SPRY 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1357 – 1563207B30.2/SPRY 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati2691 – 28091193Add
    BLAST
    Repeati2811 – 29241144Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni853 – 292420724 X approximate repeatsAdd
    BLAST
    Regioni3580 – 360930Interaction with CALMBy similarityAdd
    BLAST

    Domaini

    The calcium release channel activity resides in the C-terminal region while the remaining part of the protein resides in the cytoplasm.Curated

    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

    eggNOGiNOG247670.
    GeneTreeiENSGT00690000101961.
    HOGENOMiHOG000231428.
    HOVERGENiHBG006699.
    KOiK04962.
    OMAiSKVQPLM.
    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.
    IPR002048. EF_hand_dom.
    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.
    SMARTiSM00054. EFh. 2 hits.
    SM00472. MIR. 4 hits.
    SM00449. SPRY. 3 hits.
    [Graphical view]
    SUPFAMiSSF100909. SSF100909. 2 hits.
    SSF49899. SSF49899. 2 hits.
    SSF82109. SSF82109. 2 hits.
    PROSITEiPS50188. B302_SPRY. 3 hits.
    PS50919. MIR. 5 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    E9Q401-1 [UniParc]FASTAAdd to Basket

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    MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE     50
    STSNSKNVPP DLSICTFVLE QSLSVRALQE MLANTVEKSE GQVDVEKWKF 100
    MMKTAQGGGH RTLLYGHAIL LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ 150
    EDTTGEACWW TIHPASKQRS EGEKVRVGDD LILVSVSSER YLHLSYGNSS 200
    WHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH MDECLTVPSG 250
    EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV 300
    TTGKYLSLME DKNLLLMDKE KADVKSTAFA FRSSKEKLDV GVRKEVDGMG 350
    TSEIKYGDSI CYIQHVDTGL WLTYQAVDVK SARMGSIQRK AIMHHEGHMD 400
    DGLNLSRSQH EESRTARVIR STVFLFNRFI RGLDALSKKV KLPTIDLPIE 450
    SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR ALKNRQNLFQ EEGMINLVLE 500
    CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL IRGNRKNCAQ 550
    FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL 600
    LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN 650
    HVSSMRPNIF LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST 700
    EGYSPYPGGG EEWGGNGVGD DLFSYGFDGL HLWSGCIART VSSPNQHLLR 750
    TDDVISCCLD LSAPSISFRI NGQPVQGMFE NFNIDGLFFP VVSFSAGIKV 800
    RFLLGGRHGE FKFLPPPGYA ACYEAVLPKE KLKVEHSREY KQERTYTRDL 850
    LGPTVSLTQA AFTPVPVDTS QIVLPPHLER IRERLAENIH ELWVMNKIEL 900
    GWQYGPVRDD NKRQHPCLVE FCKLPEQERN YNLQMSLETL KTLLALGCHV 950
    GIADEHAEEK VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA 1000
    ENAHNVWARD RIRQGWTYGI QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL 1050
    REAVRTLLGY GYHLEAPDQD HASRAEVCSG TGERFRIFRA EKTYAVKAGR 1100
    WYFEFEAVTA GDMRVGWSRP GCQPDLELGS DDRAFAFDGF KAQRWHQGNE 1150
    HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG 1200
    FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW 1250
    LSKRLPQFLQ VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNNNTDIM 1300
    FYRLSMPIEC AEVFSKSVAG GLPGAGFYGP KNDLEDFDVD SDFEVLMKTA 1350
    HGHLVPDRID KDKETPKPEF NNHKDYAQEK PSRLKQRFLL RRTKPDYSTG 1400
    HSARLTEDVL ADDRDDYEYL MQTSTYYYSV RIFPGQEPAN VWVGWITSDF 1450
    HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR 1500
    NNSNGLEIGC VVDAASGLLT FIANGKELST YYQVEPSTKL FPAVFAQATS 1550
    PNVFQFELGR IKNVMPLSAG LFKSEHKNPV PQCPPRLHVQ FLSHVLWSRM 1600
    PNQFLKVDVS RISERQGWLV QCLDPLQFMS LHIPEENRSV DILELTEQEE 1650
    LLQFHYHTLR LYSAVCALGN HRVAHALCSH VDEPQLLYAI ENKYMPGLLR 1700
    AGYYDLLIDI HLSSYATARL MMNNEFIVPM TEETKSITLF PDENKKHGLP 1750
    GIGLSTSLRP RMRFSSPSFV SISNDCYQYS PEFPLDILKA KTIQMLTEAV 1800
    KEGSLHARDP VGGTTEFLFV PLIKLFYTLL IMGIFHNEDL KHILQLIEPS 1850
    VFKEAAVPEE EGGTPEKEIS IEDAKLEGEE EAKGGKRPKE GLLQMKLPEP 1900
    VKLQMCLLLQ YLCDCQVRHR IEAIVAFSDD FVAKLQDNQR FRYNEVMQAL 1950
    NMSAALTARK TREFRSPPQE QINMLLNFKD DKSECPCPEE IRDQLLDFHE 2000
    DLMTHCGIEL DEDGSLDGSN DLTIRGRLLS LVEKVTYLKK KQAEKPVASD 2050
    SRKCSSLQQL ISETMVRWAQ ESVIEDPELV RAMFVLLHRQ YDGIGGLVRA 2100
    LPKTYTINGV SVEDTINLLA SLGQIRSLLS VRMGKEEEKL MIRGLGDIMN 2150
    NKVFYQHPNL MRALGMHETV MEVMVNVLGG GESKEITFPK MVANCCRFLC 2200
    YFCRISRQNQ KAMFDHLSYL LENSSVGLAS PAMRGSTPLD VAAASVMDNN 2250
    ELALALREPD LEKVVRYLAG CGLQSCQMLV SKGYPDIGWN PVEGERYLDF 2300
    LRFAVFCNGE SVEENANVVV RLLIRRPECF GPALRGEGGN GLLAAMEEAI 2350
    KIAEDPSRDG PSPTSGSSKT LDIEEEEDDT IHMGNAIMTF YAALIDLLGR 2400
    CAPEMHLIHA GKGEAIRIRS ILRSLIPLGD LVGVISIAFQ MPTIAKDGKV 2450
    VEPDMSAGFC PDHKAAMVLF LDRVYGIEVQ DFLLHLLEVG FLPDLRAAAS 2500
    LDTAALSATD MALALNRYLC TAVLPLLTRC APLFAGTEHH ASLIDSLLHT 2550
    VYRLSKGCSL TKAQRDSIEV CLLSICGQLR PSMMQHLLRR LVFDVPLLNE 2600
    HAKMPLKLLT NHYERCWKYY CLPGGWGNFG AASEEELHLS RKLFWGIFDA 2650
    LSQKKYEQEL FKLALPCLSA VAGALPPDYM ESNYVSMMEK QSSMDSEGNF 2700
    NPQPVDTSNI TIPEKLEYFI NKYAEHSHDK WSMDKLANGW IYGEIYSDSS 2750
    KIQPLMKPYK LLSEKEKEIY RWPIKESLKT MLAWGWRIER TREGDSMALY 2800
    NRTRRISQTS QVSIDAAHGY SPRAIDMSNV TLSRDLHAMA EMMAENYHNI 2850
    WAKKKKLELE SKGGGNHPLL VPYDTLTAKE KAKDREKAQD IFKFLQISGY 2900
    VVSRGFKDLD LDTPSIEKRF AYSFLQQLIR YVDEAHQYIL EFDGGSRSKG 2950
    EHFPYEQEIK FFAKVVLPLI DQYFKNHRLY FLSAASRPLC TGGHASNKEK 3000
    EMVTSLFCKL GVLVRHRISL FGNDATSIVN CLHILGQTLD ARTVMKTGLD 3050
    SVKSALRAFL DNAAEDLEKT MENLKQGQFT HTRSQPKGVT QIINYTTVAL 3100
    LPMLSSLFEH IGQHQFGEDL ILEDVQVSCY RILTSLYALG TSKSIYVERQ 3150
    RSALGECLAA FAGAFPIAFL ETHLDKHNVY SIYNTRSSRE RAALSLPANV 3200
    EDVCPNIPSL EKLMTEIIEL AESGIRYTQM PYMMEVVLPM LCSYMSRWWE 3250
    HGPENHPERA EMCCTALNSE HMNTLLGNIL KIIYNNLGID EGAWMKRLAV 3300
    FSQPIINKVK PQLLKTHFLP LMEKLKKKAA MVVSEEDHLK AEARGDMSEA 3350
    ELLILDEFTT LARDLYAFYP LLIRFVDYNR AKWLKEPNPE AEELFRMVAE 3400
    VFIYWSKSHN FKREEQNFVV QNEINNMSFL ITDTKSKMSK AAISDQERKK 3450
    MKRKGDRYSM QTSLIVAALK RLLPIGLNIC APGDQELIAL AKNRFSLKDT 3500
    EEEVRDIIRS NIHLQGKLED PAIRWQMALY KDLPNRTEDP SDPERTVERV 3550
    LGIANVLFHL EQKSKYTGRG YFSLVEHPQR SKKAVWHKLL SKQRKRAVVA 3600
    CFRMAPLYNL PRHRAVNLFL QGYEKSWIET EEHYFEDKLI EDLAKPGAEL 3650
    PEEDEAMKRV DPLHQLILLF SRTALTEKCK LEEDFLYMAY ADIMAKSCHD 3700
    EEDDDGEEEV KSFEEKEMEK QKLLYQQARL HDRGAAEMVL QTISASKGET 3750
    GPMVAATLKL GIAILNGGNS TVQQKMLDYL KEKKDVGFFQ SLAGLMQSCS 3800
    VLDLNAFERQ NKAEGLGMVT EEGSGEKVLQ DDEFTCDLFR FLQLLCEGHN 3850
    SDFQNYLRTQ TGNNTTVNII ISTVDYLLRV QESISDFYWY YSGKDIIDEQ 3900
    GQRNFSKAIQ VAKQVFNTLT EYIQGPCTGN QQSLAHSRLW DAVVGFLHVF 3950
    AHMQMKLSQD SSQIELLKEL MDLQKDMVVM LLSMLEGNVV NGTIGKQMVD 4000
    MLVESSNNVE MILKFFDMFL KLKDLTSSDT FKEYDPDGKG VISKRDFHKA 4050
    MESHKHYTQS ETEFLLSCAE TDENETLDYE EFVKRFHEPA KDIGFNVAVL 4100
    LTNLSEHMPN DTRLQTFLEL AESVLNYFQP FLGRIEIMGS AKRIERVYFE 4150
    ISESSRTQWE KPQVKESKRQ FIFDVVNEGG EKEKMELFVN FCEDTIFEMQ 4200
    LAAQISESDL NERLANKEES EKERPEEQAP RMGFFSLLTI QSALFALRYN 4250
    VLTLVRMLSL KSLKKQMKRM KKMTVKDMVL AFFSSYWSVF VTLLHFVASV 4300
    CRGFFRIVSS LLLGGSLVEG AKKIKVAELL ANMPDPTQDE VRGDEEEGER 4350
    KPLESALPSE DLTDLKELTE ESDLLSDIFG LDLKREGGQY KLIPHNPNAG 4400
    LSDLMTNPVP VPEVQEKFQE QKAKEEKEEK EETKSEPEKA EGEDGEKEEK 4450
    AKDEKSKQKL RQLHTHRYGE PEVPESAFWK KIIAYQQKLL NYFARNFYNM 4500
    RMLALFVAFA INFILLFYKV STSSVVEGKE LPTRTSSDTA KVTNSLDSSP 4550
    HRIIAVHYVL EESSGYMEPT LRILAILHTI ISFFCIIGYY CLKVPLVIFK 4600
    REKEVARKLE FDGLYITEQP SEDDIKGQWD RLVINTQSFP NNYWDKFVKR 4650
    KVMDKYGEFY GRDRISELLG MDKAALDFSD AREKKKPKKD SSLSAVLNSI 4700
    DVKYQMWKLG VVFTDNSFLY LAWYMTMSVL GHYNNFFFAA HLLDIAMGFK 4750
    TLRTILSSVT HNGKQLVLTV GLLAVVVYLY TVVAFNFFRK FYNKSEDGDT 4800
    PDMKCDDMLT CYMFHMYVGV RAGGGIGDEI EDPAGDEYEI YRIIFDITFF 4850
    FFVIVILLAI IQGLIIDAFG ELRDQQEQVK EDMETKCFIC GIGNDYFDTV 4900
    PHGFETHTLQ EHNLANYLFF LMYLINKDET EHTGQESYVW KMYQERCWEF 4950
    FPAGDCFRKQ YEDQLN 4966
    Length:4,966
    Mass (Da):564,819
    Last modified:April 5, 2011 - v1
    Checksum:iF43425091AF7114F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1332 – 13321N → S in AAG34081. (PubMed:10473538)Curated
    Sequence conflicti1412 – 14121D → G in AAG34081. (PubMed:10473538)Curated
    Sequence conflicti1962 – 19621R → K in AAG34081. (PubMed:10473538)Curated
    Sequence conflicti2265 – 22651V → VA in AAG34081. (PubMed:10473538)Curated
    Sequence conflicti2532 – 25321P → R in AAG34081. (PubMed:10473538)Curated
    Sequence conflicti3192 – 31921A → T in AAG34081. (PubMed:10473538)Curated
    Sequence conflicti3533 – 35331L → F in AAG34081. (PubMed:10473538)Curated
    Sequence conflicti4324 – 43241I → T in CAA58785. (PubMed:7876312)Curated
    Sequence conflicti4853 – 48531V → E in CAA58785. (PubMed:7876312)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF295105 mRNA. Translation: AAG34081.1.
    AC131329 Genomic DNA. No translation available.
    AC159208 Genomic DNA. No translation available.
    CT010468 Genomic DNA. No translation available.
    CT572985 Genomic DNA. No translation available.
    AB012003 Genomic DNA. Translation: BAA25137.1.
    X83933 mRNA. Translation: CAA58785.1.
    D38217 mRNA. Translation: BAA07392.1.
    CCDSiCCDS49206.1.
    PIRiI48742.
    RefSeqiNP_076357.2. NM_023868.2.
    UniGeneiMm.239871.

    Genome annotation databases

    EnsembliENSMUST00000021750; ENSMUSP00000021750; ENSMUSG00000021313.
    GeneIDi20191.
    KEGGimmu:20191.
    UCSCiuc007pld.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF295105 mRNA. Translation: AAG34081.1 .
    AC131329 Genomic DNA. No translation available.
    AC159208 Genomic DNA. No translation available.
    CT010468 Genomic DNA. No translation available.
    CT572985 Genomic DNA. No translation available.
    AB012003 Genomic DNA. Translation: BAA25137.1 .
    X83933 mRNA. Translation: CAA58785.1 .
    D38217 mRNA. Translation: BAA07392.1 .
    CCDSi CCDS49206.1.
    PIRi I48742.
    RefSeqi NP_076357.2. NM_023868.2.
    UniGenei Mm.239871.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MC2 NMR - A 10-224 [» ]
    3IM5 X-ray 2.55 A/B 1-217 [» ]
    3IM6 X-ray 1.70 A 1-217 [» ]
    3IM7 X-ray 2.21 A 1-217 [» ]
    3QR5 X-ray 2.30 A/B 1-217 [» ]
    4ETV X-ray 1.65 A/B 2699-2904 [» ]
    4KEI X-ray 2.41 A 1-217 [» ]
    4KEJ X-ray 2.55 A 1-217 [» ]
    4KEK X-ray 2.15 A 1-217 [» ]
    4L4H X-ray 2.00 A 1-547 [» ]
    4L4I X-ray 2.15 A 1-547 [» ]
    ProteinModelPortali E9Q401.
    SMRi E9Q401. Positions 10-544, 2700-2904, 3580-3606.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi E9Q401. 6 interactions.
    MINTi MINT-4129173.

    PTM databases

    PhosphoSitei E9Q401.

    Proteomic databases

    MaxQBi E9Q401.
    PRIDEi E9Q401.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021750 ; ENSMUSP00000021750 ; ENSMUSG00000021313 .
    GeneIDi 20191.
    KEGGi mmu:20191.
    UCSCi uc007pld.1. mouse.

    Organism-specific databases

    CTDi 6262.
    MGIi MGI:99685. Ryr2.

    Phylogenomic databases

    eggNOGi NOG247670.
    GeneTreei ENSGT00690000101961.
    HOGENOMi HOG000231428.
    HOVERGENi HBG006699.
    KOi K04962.
    OMAi SKVQPLM.
    OrthoDBi EOG71K622.
    TreeFami TF315244.

    Enzyme and pathway databases

    Reactomei REACT_196640. Stimuli-sensing channels.

    Miscellaneous databases

    EvolutionaryTracei Q9ERN6.
    NextBioi 297739.
    PROi E9Q401.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi E9Q401.
    Bgeei E9Q401.

    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.
    IPR002048. EF_hand_dom.
    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 SM00054. EFh. 2 hits.
    SM00472. MIR. 4 hits.
    SM00449. SPRY. 3 hits.
    [Graphical view ]
    SUPFAMi SSF100909. SSF100909. 2 hits.
    SSF49899. SSF49899. 2 hits.
    SSF82109. SSF82109. 2 hits.
    PROSITEi PS50188. B302_SPRY. 3 hits.
    PS50919. MIR. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular identification of the ryanodine receptor pore-forming segment."
      Zhao M., Li P., Li X., Zhang L., Winkfein R.J., Chen S.R.
      J. Biol. Chem. 274:25971-25974(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF GLY-4819; ARG-4821; GLY-4823; GLY-4824; GLY-4825; GLY-4827 AND ASP-4828.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Embryonic lethality and abnormal cardiac myocytes in mice lacking ryanodine receptor type 2."
      Takeshima H., Komazaki S., Hirose K., Nishi M., Noda T., Iino M.
      EMBO J. 17:3309-3316(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16, FUNCTION, DISRUPTION PHENOTYPE.
    4. "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 4145-4966, TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Brain.
    5. "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 4863-4966, TISSUE SPECIFICITY.
      Strain: C57BL/6J.
      Tissue: Heart.
    6. "Functional consequence of protein kinase A-dependent phosphorylation of the cardiac ryanodine receptor: sensitization of store overload-induced Ca2+ release."
      Xiao B., Tian X., Xie W., Jones P.P., Cai S., Wang X., Jiang D., Kong H., Zhang L., Chen K., Walsh M.P., Cheng H., Chen S.R.W.
      J. Biol. Chem. 282:30256-30264(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-2030.
    7. "Ryanodine receptor phosphorylation by calcium/calmodulin-dependent protein kinase II promotes life-threatening ventricular arrhythmias in mice with heart failure."
      van Oort R.J., McCauley M.D., Dixit S.S., Pereira L., Yang Y., Respress J.L., Wang Q., De Almeida A.C., Skapura D.G., Anderson M.E., Bers D.M., Wehrens X.H.
      Circulation 122:2669-2679(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-2807 AND SER-2813, INTERACTION WITH FKBP1B, MUTAGENESIS OF SER-2813.
    8. "Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized cardiac myocytes and effects on Ca sparks."
      Guo T., Cornea R.L., Huke S., Camors E., Yang Y., Picht E., Fruen B.R., Bers D.M.
      Circ. Res. 106:1743-1752(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FKBP1A AND FKBP1B, PHOSPHORYLATION AT SER-2807.
    9. "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.
    10. "Crystal structures of the N-terminal domains of cardiac and skeletal muscle ryanodine receptors: insights into disease mutations."
      Lobo P.A., Van Petegem F.
      Structure 17:1505-1514(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-217, MUTAGENESIS OF ALA-77 AND VAL-186.
    11. "The deletion of exon 3 in the cardiac ryanodine receptor is rescued by beta strand switching."
      Lobo P.A., Kimlicka L., Tung C.C., Van Petegem F.
      Structure 19:790-798(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-217.

    Entry informationi

    Entry nameiRYR2_MOUSE
    AccessioniPrimary (citable) accession number: E9Q401
    Secondary accession number(s): O70181
    , Q62174, Q62197, Q9ERN6
    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 By similarity.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3