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E9Q401

- RYR2_MOUSE

UniProt

E9Q401 - RYR2_MOUSE

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Protein

Ryanodine receptor 2

Gene
Ryr2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 42314231Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei4232 – 425221Helical; Reviewed predictionAdd
BLAST
Transmembranei4278 – 429821Helical; Reviewed predictionAdd
BLAST
Transmembranei4502 – 452221Helical; Reviewed predictionAdd
BLAST
Transmembranei4579 – 459921Helical; Reviewed predictionAdd
BLAST
Transmembranei4729 – 474921Helical; Reviewed predictionAdd
BLAST
Transmembranei4768 – 478821Helical; Reviewed predictionAdd
BLAST
Intramembranei4819 – 482810Pore-forming; Inferred
Transmembranei4849 – 486921Helical; Reviewed predictionAdd
BLAST
Topological domaini4870 – 496697Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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.
Phosphorylation at Ser-2030 by PKA enhances the response to lumenal calcium.

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.3 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.

Miscellaneous databases

EvolutionaryTraceiQ9ERN6.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni853 – 292420724 X approximate repeatsAdd
BLAST
Regioni3580 – 360930Interaction with CALM By 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 Inferred.

Sequence similaritiesi

Contains 3 B30.2/SPRY domains.
Contains 5 MIR domains.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1332 – 13321N → S in AAG34081. 1 Publication
Sequence conflicti1412 – 14121D → G in AAG34081. 1 Publication
Sequence conflicti1962 – 19621R → K in AAG34081. 1 Publication
Sequence conflicti2265 – 22651V → VA in AAG34081. 1 Publication
Sequence conflicti2532 – 25321P → R in AAG34081. 1 Publication
Sequence conflicti3192 – 31921A → T in AAG34081. 1 Publication
Sequence conflicti3533 – 35331L → F in AAG34081. 1 Publication
Sequence conflicti4324 – 43241I → T in CAA58785. 1 Publication
Sequence conflicti4853 – 48531V → E in CAA58785. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 35 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.

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

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