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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 kinase binding Source: BHF-UCL
  9. protein self-association Source: UniProtKB
  10. ryanodine-sensitive calcium-release channel activity Source: MGI
  11. 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 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 42314231CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei4232 – 425221HelicalSequence AnalysisAdd
BLAST
Transmembranei4278 – 429821HelicalSequence AnalysisAdd
BLAST
Transmembranei4502 – 452221HelicalSequence AnalysisAdd
BLAST
Transmembranei4579 – 459921HelicalSequence AnalysisAdd
BLAST
Transmembranei4729 – 474921HelicalSequence AnalysisAdd
BLAST
Transmembranei4768 – 478821HelicalSequence AnalysisAdd
BLAST
Intramembranei4819 – 482810Pore-formingCurated
Transmembranei4849 – 486921HelicalSequence AnalysisAdd
BLAST
Topological domaini4870 – 496697CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. calcium channel complex Source: BHF-UCL
  2. extracellular vesicular exosome Source: Ensembl
  3. integral component of membrane Source: MGI
  4. membrane Source: MGI
  5. protein complex Source: MGI
  6. sarcomere Source: BHF-UCL
  7. sarcoplasmic reticulum Source: BHF-UCL
  8. sarcoplasmic reticulum membrane Source: MGI
  9. smooth endoplasmic reticulum Source: MGI
  10. 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.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

BgeeiE9Q401.
ExpressionAtlasiE9Q401. baseline and differential.

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiE9Q401.
KOiK04962.
OMAiSKVQPLM.
OrthoDBiEOG71K622.
TreeFamiTF315244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
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.
IPR003877. SPRY_dom.
[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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        10         20         30         40         50
MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE
60 70 80 90 100
STSNSKNVPP DLSICTFVLE QSLSVRALQE MLANTVEKSE GQVDVEKWKF
110 120 130 140 150
MMKTAQGGGH RTLLYGHAIL LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ
160 170 180 190 200
EDTTGEACWW TIHPASKQRS EGEKVRVGDD LILVSVSSER YLHLSYGNSS
210 220 230 240 250
WHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH MDECLTVPSG
260 270 280 290 300
EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV
310 320 330 340 350
TTGKYLSLME DKNLLLMDKE KADVKSTAFA FRSSKEKLDV GVRKEVDGMG
360 370 380 390 400
TSEIKYGDSI CYIQHVDTGL WLTYQAVDVK SARMGSIQRK AIMHHEGHMD
410 420 430 440 450
DGLNLSRSQH EESRTARVIR STVFLFNRFI RGLDALSKKV KLPTIDLPIE
460 470 480 490 500
SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR ALKNRQNLFQ EEGMINLVLE
510 520 530 540 550
CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL IRGNRKNCAQ
560 570 580 590 600
FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL
610 620 630 640 650
LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN
660 670 680 690 700
HVSSMRPNIF LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST
710 720 730 740 750
EGYSPYPGGG EEWGGNGVGD DLFSYGFDGL HLWSGCIART VSSPNQHLLR
760 770 780 790 800
TDDVISCCLD LSAPSISFRI NGQPVQGMFE NFNIDGLFFP VVSFSAGIKV
810 820 830 840 850
RFLLGGRHGE FKFLPPPGYA ACYEAVLPKE KLKVEHSREY KQERTYTRDL
860 870 880 890 900
LGPTVSLTQA AFTPVPVDTS QIVLPPHLER IRERLAENIH ELWVMNKIEL
910 920 930 940 950
GWQYGPVRDD NKRQHPCLVE FCKLPEQERN YNLQMSLETL KTLLALGCHV
960 970 980 990 1000
GIADEHAEEK VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA
1010 1020 1030 1040 1050
ENAHNVWARD RIRQGWTYGI QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL
1060 1070 1080 1090 1100
REAVRTLLGY GYHLEAPDQD HASRAEVCSG TGERFRIFRA EKTYAVKAGR
1110 1120 1130 1140 1150
WYFEFEAVTA GDMRVGWSRP GCQPDLELGS DDRAFAFDGF KAQRWHQGNE
1160 1170 1180 1190 1200
HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG
1210 1220 1230 1240 1250
FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW
1260 1270 1280 1290 1300
LSKRLPQFLQ VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNNNTDIM
1310 1320 1330 1340 1350
FYRLSMPIEC AEVFSKSVAG GLPGAGFYGP KNDLEDFDVD SDFEVLMKTA
1360 1370 1380 1390 1400
HGHLVPDRID KDKETPKPEF NNHKDYAQEK PSRLKQRFLL RRTKPDYSTG
1410 1420 1430 1440 1450
HSARLTEDVL ADDRDDYEYL MQTSTYYYSV RIFPGQEPAN VWVGWITSDF
1460 1470 1480 1490 1500
HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR
1510 1520 1530 1540 1550
NNSNGLEIGC VVDAASGLLT FIANGKELST YYQVEPSTKL FPAVFAQATS
1560 1570 1580 1590 1600
PNVFQFELGR IKNVMPLSAG LFKSEHKNPV PQCPPRLHVQ FLSHVLWSRM
1610 1620 1630 1640 1650
PNQFLKVDVS RISERQGWLV QCLDPLQFMS LHIPEENRSV DILELTEQEE
1660 1670 1680 1690 1700
LLQFHYHTLR LYSAVCALGN HRVAHALCSH VDEPQLLYAI ENKYMPGLLR
1710 1720 1730 1740 1750
AGYYDLLIDI HLSSYATARL MMNNEFIVPM TEETKSITLF PDENKKHGLP
1760 1770 1780 1790 1800
GIGLSTSLRP RMRFSSPSFV SISNDCYQYS PEFPLDILKA KTIQMLTEAV
1810 1820 1830 1840 1850
KEGSLHARDP VGGTTEFLFV PLIKLFYTLL IMGIFHNEDL KHILQLIEPS
1860 1870 1880 1890 1900
VFKEAAVPEE EGGTPEKEIS IEDAKLEGEE EAKGGKRPKE GLLQMKLPEP
1910 1920 1930 1940 1950
VKLQMCLLLQ YLCDCQVRHR IEAIVAFSDD FVAKLQDNQR FRYNEVMQAL
1960 1970 1980 1990 2000
NMSAALTARK TREFRSPPQE QINMLLNFKD DKSECPCPEE IRDQLLDFHE
2010 2020 2030 2040 2050
DLMTHCGIEL DEDGSLDGSN DLTIRGRLLS LVEKVTYLKK KQAEKPVASD
2060 2070 2080 2090 2100
SRKCSSLQQL ISETMVRWAQ ESVIEDPELV RAMFVLLHRQ YDGIGGLVRA
2110 2120 2130 2140 2150
LPKTYTINGV SVEDTINLLA SLGQIRSLLS VRMGKEEEKL MIRGLGDIMN
2160 2170 2180 2190 2200
NKVFYQHPNL MRALGMHETV MEVMVNVLGG GESKEITFPK MVANCCRFLC
2210 2220 2230 2240 2250
YFCRISRQNQ KAMFDHLSYL LENSSVGLAS PAMRGSTPLD VAAASVMDNN
2260 2270 2280 2290 2300
ELALALREPD LEKVVRYLAG CGLQSCQMLV SKGYPDIGWN PVEGERYLDF
2310 2320 2330 2340 2350
LRFAVFCNGE SVEENANVVV RLLIRRPECF GPALRGEGGN GLLAAMEEAI
2360 2370 2380 2390 2400
KIAEDPSRDG PSPTSGSSKT LDIEEEEDDT IHMGNAIMTF YAALIDLLGR
2410 2420 2430 2440 2450
CAPEMHLIHA GKGEAIRIRS ILRSLIPLGD LVGVISIAFQ MPTIAKDGKV
2460 2470 2480 2490 2500
VEPDMSAGFC PDHKAAMVLF LDRVYGIEVQ DFLLHLLEVG FLPDLRAAAS
2510 2520 2530 2540 2550
LDTAALSATD MALALNRYLC TAVLPLLTRC APLFAGTEHH ASLIDSLLHT
2560 2570 2580 2590 2600
VYRLSKGCSL TKAQRDSIEV CLLSICGQLR PSMMQHLLRR LVFDVPLLNE
2610 2620 2630 2640 2650
HAKMPLKLLT NHYERCWKYY CLPGGWGNFG AASEEELHLS RKLFWGIFDA
2660 2670 2680 2690 2700
LSQKKYEQEL FKLALPCLSA VAGALPPDYM ESNYVSMMEK QSSMDSEGNF
2710 2720 2730 2740 2750
NPQPVDTSNI TIPEKLEYFI NKYAEHSHDK WSMDKLANGW IYGEIYSDSS
2760 2770 2780 2790 2800
KIQPLMKPYK LLSEKEKEIY RWPIKESLKT MLAWGWRIER TREGDSMALY
2810 2820 2830 2840 2850
NRTRRISQTS QVSIDAAHGY SPRAIDMSNV TLSRDLHAMA EMMAENYHNI
2860 2870 2880 2890 2900
WAKKKKLELE SKGGGNHPLL VPYDTLTAKE KAKDREKAQD IFKFLQISGY
2910 2920 2930 2940 2950
VVSRGFKDLD LDTPSIEKRF AYSFLQQLIR YVDEAHQYIL EFDGGSRSKG
2960 2970 2980 2990 3000
EHFPYEQEIK FFAKVVLPLI DQYFKNHRLY FLSAASRPLC TGGHASNKEK
3010 3020 3030 3040 3050
EMVTSLFCKL GVLVRHRISL FGNDATSIVN CLHILGQTLD ARTVMKTGLD
3060 3070 3080 3090 3100
SVKSALRAFL DNAAEDLEKT MENLKQGQFT HTRSQPKGVT QIINYTTVAL
3110 3120 3130 3140 3150
LPMLSSLFEH IGQHQFGEDL ILEDVQVSCY RILTSLYALG TSKSIYVERQ
3160 3170 3180 3190 3200
RSALGECLAA FAGAFPIAFL ETHLDKHNVY SIYNTRSSRE RAALSLPANV
3210 3220 3230 3240 3250
EDVCPNIPSL EKLMTEIIEL AESGIRYTQM PYMMEVVLPM LCSYMSRWWE
3260 3270 3280 3290 3300
HGPENHPERA EMCCTALNSE HMNTLLGNIL KIIYNNLGID EGAWMKRLAV
3310 3320 3330 3340 3350
FSQPIINKVK PQLLKTHFLP LMEKLKKKAA MVVSEEDHLK AEARGDMSEA
3360 3370 3380 3390 3400
ELLILDEFTT LARDLYAFYP LLIRFVDYNR AKWLKEPNPE AEELFRMVAE
3410 3420 3430 3440 3450
VFIYWSKSHN FKREEQNFVV QNEINNMSFL ITDTKSKMSK AAISDQERKK
3460 3470 3480 3490 3500
MKRKGDRYSM QTSLIVAALK RLLPIGLNIC APGDQELIAL AKNRFSLKDT
3510 3520 3530 3540 3550
EEEVRDIIRS NIHLQGKLED PAIRWQMALY KDLPNRTEDP SDPERTVERV
3560 3570 3580 3590 3600
LGIANVLFHL EQKSKYTGRG YFSLVEHPQR SKKAVWHKLL SKQRKRAVVA
3610 3620 3630 3640 3650
CFRMAPLYNL PRHRAVNLFL QGYEKSWIET EEHYFEDKLI EDLAKPGAEL
3660 3670 3680 3690 3700
PEEDEAMKRV DPLHQLILLF SRTALTEKCK LEEDFLYMAY ADIMAKSCHD
3710 3720 3730 3740 3750
EEDDDGEEEV KSFEEKEMEK QKLLYQQARL HDRGAAEMVL QTISASKGET
3760 3770 3780 3790 3800
GPMVAATLKL GIAILNGGNS TVQQKMLDYL KEKKDVGFFQ SLAGLMQSCS
3810 3820 3830 3840 3850
VLDLNAFERQ NKAEGLGMVT EEGSGEKVLQ DDEFTCDLFR FLQLLCEGHN
3860 3870 3880 3890 3900
SDFQNYLRTQ TGNNTTVNII ISTVDYLLRV QESISDFYWY YSGKDIIDEQ
3910 3920 3930 3940 3950
GQRNFSKAIQ VAKQVFNTLT EYIQGPCTGN QQSLAHSRLW DAVVGFLHVF
3960 3970 3980 3990 4000
AHMQMKLSQD SSQIELLKEL MDLQKDMVVM LLSMLEGNVV NGTIGKQMVD
4010 4020 4030 4040 4050
MLVESSNNVE MILKFFDMFL KLKDLTSSDT FKEYDPDGKG VISKRDFHKA
4060 4070 4080 4090 4100
MESHKHYTQS ETEFLLSCAE TDENETLDYE EFVKRFHEPA KDIGFNVAVL
4110 4120 4130 4140 4150
LTNLSEHMPN DTRLQTFLEL AESVLNYFQP FLGRIEIMGS AKRIERVYFE
4160 4170 4180 4190 4200
ISESSRTQWE KPQVKESKRQ FIFDVVNEGG EKEKMELFVN FCEDTIFEMQ
4210 4220 4230 4240 4250
LAAQISESDL NERLANKEES EKERPEEQAP RMGFFSLLTI QSALFALRYN
4260 4270 4280 4290 4300
VLTLVRMLSL KSLKKQMKRM KKMTVKDMVL AFFSSYWSVF VTLLHFVASV
4310 4320 4330 4340 4350
CRGFFRIVSS LLLGGSLVEG AKKIKVAELL ANMPDPTQDE VRGDEEEGER
4360 4370 4380 4390 4400
KPLESALPSE DLTDLKELTE ESDLLSDIFG LDLKREGGQY KLIPHNPNAG
4410 4420 4430 4440 4450
LSDLMTNPVP VPEVQEKFQE QKAKEEKEEK EETKSEPEKA EGEDGEKEEK
4460 4470 4480 4490 4500
AKDEKSKQKL RQLHTHRYGE PEVPESAFWK KIIAYQQKLL NYFARNFYNM
4510 4520 4530 4540 4550
RMLALFVAFA INFILLFYKV STSSVVEGKE LPTRTSSDTA KVTNSLDSSP
4560 4570 4580 4590 4600
HRIIAVHYVL EESSGYMEPT LRILAILHTI ISFFCIIGYY CLKVPLVIFK
4610 4620 4630 4640 4650
REKEVARKLE FDGLYITEQP SEDDIKGQWD RLVINTQSFP NNYWDKFVKR
4660 4670 4680 4690 4700
KVMDKYGEFY GRDRISELLG MDKAALDFSD AREKKKPKKD SSLSAVLNSI
4710 4720 4730 4740 4750
DVKYQMWKLG VVFTDNSFLY LAWYMTMSVL GHYNNFFFAA HLLDIAMGFK
4760 4770 4780 4790 4800
TLRTILSSVT HNGKQLVLTV GLLAVVVYLY TVVAFNFFRK FYNKSEDGDT
4810 4820 4830 4840 4850
PDMKCDDMLT CYMFHMYVGV RAGGGIGDEI EDPAGDEYEI YRIIFDITFF
4860 4870 4880 4890 4900
FFVIVILLAI IQGLIIDAFG ELRDQQEQVK EDMETKCFIC GIGNDYFDTV
4910 4920 4930 4940 4950
PHGFETHTLQ EHNLANYLFF LMYLINKDET EHTGQESYVW KMYQERCWEF
4960
FPAGDCFRKQ YEDQLN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ENSGT00760000119152.
HOGENOMi HOG000231428.
HOVERGENi HBG006699.
InParanoidi E9Q401.
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

Bgeei E9Q401.
ExpressionAtlasi E9Q401. baseline and differential.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProi IPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
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.
IPR003877. SPRY_dom.
[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: October 29, 2014
This is version 37 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