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E9Q401 (RYR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ryr2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length4966 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.3 Ref.7 Ref.8

Subunit structure

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. Ref.1 Ref.7 Ref.8

Subcellular location

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

Tissue specificity

Highly expressed in heart, lung, cerebellum and brain. Detected at lower levels in adrenal gland, stomach, thymus, esophagus and ovary. Ref.4 Ref.5

Domain

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

Post-translational modification

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.

Disruption phenotype

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+. Ref.3

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.

Sequence similarities

Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR2 subfamily. [View classification]

Contains 3 B30.2/SPRY domains.

Contains 5 MIR domains.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
Sarcoplasmic reticulum
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Calmodulin-binding
   Molecular functionCalcium channel
Developmental protein
Ion channel
Ligand-gated ion channel
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from direct assay PubMed 17360443. Source: MGI

Purkinje myocyte to ventricular cardiac muscle cell signaling

Inferred from mutant phenotype PubMed 17872467. Source: BHF-UCL

calcium ion transmembrane transport

Inferred from mutant phenotype PubMed 21673970. Source: MGI

calcium ion transport

Inferred from direct assay Ref.1. Source: UniProtKB

calcium-mediated signaling

Inferred from mutant phenotype Ref.3. Source: UniProtKB

calcium-mediated signaling using intracellular calcium source

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway

Inferred from direct assay PubMed 17360443. Source: MGI

cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

cardiac muscle hypertrophy

Inferred from mutant phenotype PubMed 17431507. Source: MGI

cellular calcium ion homeostasis

Inferred from mutant phenotype Ref.3. Source: UniProtKB

cellular response to caffeine

Inferred from direct assay Ref.3. Source: UniProtKB

cytosolic calcium ion transport

Inferred from mutant phenotype PubMed 17431507. Source: MGI

detection of calcium ion

Inferred from electronic annotation. Source: Ensembl

embryonic heart tube morphogenesis

Inferred from mutant phenotype Ref.3. Source: UniProtKB

establishment of protein localization to endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

left ventricular cardiac muscle tissue morphogenesis

Inferred from mutant phenotype PubMed 17431507. Source: MGI

positive regulation of calcium-transporting ATPase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of heart rate

Inferred from mutant phenotype PubMed 12089338PubMed 17431507. Source: MGI

positive regulation of ryanodine-sensitive calcium-release channel activity by adrenergic receptor signaling pathway involved in positive regulation of cardiac muscle contraction

Inferred from mutant phenotype PubMed 17872467. Source: BHF-UCL

positive regulation of sequestering of calcium ion

Inferred from electronic annotation. Source: Ensembl

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred from genetic interaction PubMed 12837242. Source: BHF-UCL

regulation of heart rate

Inferred from mutant phenotype PubMed 17872467. Source: BHF-UCL

release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from direct assay PubMed 20226167. Source: BHF-UCL

response to caffeine

Inferred from direct assay Ref.1. Source: UniProtKB

response to hypoxia

Inferred from direct assay PubMed 19120137. Source: BHF-UCL

response to redox state

Inferred from electronic annotation. Source: Ensembl

type B pancreatic cell apoptotic process

Inferred from mutant phenotype PubMed 15044459. Source: BHF-UCL

ventricular cardiac muscle cell action potential

Inferred from mutant phenotype PubMed 17872467. Source: BHF-UCL

   Cellular_componentZ disc

Inferred from direct assay PubMed 16204356PubMed 19383796. Source: MGI

calcium channel complex

Inferred from direct assay PubMed 16213210. Source: BHF-UCL

integral component of membrane

Inferred by curator PubMed 14593104. Source: MGI

membrane

Inferred from direct assay PubMed 17431507. Source: MGI

protein complex

Inferred from sequence orthology PubMed 18468998. Source: MGI

sarcomere

Inferred from direct assay PubMed 20226167. Source: BHF-UCL

sarcoplasmic reticulum

Inferred from direct assay PubMed 12919952PubMed 22406107. Source: BHF-UCL

sarcoplasmic reticulum membrane

Inferred from direct assay PubMed 14592808PubMed 16481613. Source: MGI

   Molecular_functionbinding

Inferred from physical interaction PubMed 17431507. Source: MGI

calcium channel activity

Inferred from direct assay Ref.3. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-induced calcium release activity

Inferred from electronic annotation. Source: Ensembl

calmodulin binding

Inferred from direct assay PubMed 17431507. Source: MGI

enzyme binding

Inferred from physical interaction PubMed 16213210PubMed 20080623PubMed 22406107. Source: BHF-UCL

intracellular ligand-gated calcium channel activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 12676814. Source: BHF-UCL

protein self-association

Inferred from mutant phenotype Ref.1. Source: UniProtKB

ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 14593104PubMed 17431507. Source: MGI

suramin binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Fkbp1bQ9Z2I22EBI-643628,EBI-6379859

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 49664966Ryanodine receptor 2
PRO_0000415582

Regions

Topological domain1 – 42314231Cytoplasmic Potential
Transmembrane4232 – 425221Helical; Potential
Transmembrane4278 – 429821Helical; Potential
Transmembrane4502 – 452221Helical; Potential
Transmembrane4579 – 459921Helical; Potential
Transmembrane4729 – 474921Helical; Potential
Transmembrane4768 – 478821Helical; Potential
Intramembrane4819 – 482810Pore-forming; Probable
Transmembrane4849 – 486921Helical; Potential
Topological domain4870 – 496697Cytoplasmic Potential
Domain110 – 16556MIR 1
Domain172 – 21746MIR 2
Domain225 – 28056MIR 3
Domain286 – 34358MIR 4
Domain351 – 40858MIR 5
Domain599 – 809211B30.2/SPRY 1
Repeat853 – 9661141
Repeat967 – 10801142
Domain1025 – 1222198B30.2/SPRY 2
Domain1357 – 1563207B30.2/SPRY 3
Repeat2691 – 28091193
Repeat2811 – 29241144
Region853 – 292420724 X approximate repeats
Region3580 – 360930Interaction with CALM By similarity

Amino acid modifications

Modified residue20301Phosphoserine; by PKA Ref.6
Modified residue28071Phosphoserine; by CaMK2D and PKA Ref.7 Ref.8
Modified residue28131Phosphoserine; by CaMK2D Ref.7

Experimental info

Mutagenesis771A → V: No change to global protein fold or protein stability. Alters local protein folding. Ref.10
Mutagenesis1861V → M: No change to global protein fold or protein stability. Alters local protein folding. Ref.10
Mutagenesis28131S → A: Protects against tachycardia and subsequent death due to heart failure. Ref.7
Mutagenesis28131S → D: Abolishes phosphorylation by CaMK2D. Tendency to tachycardia and subsequent death due to heart failure. Ref.7
Mutagenesis48191G → A: Strongly reduced calcium channel activity. Abolishes ryanodine binding. Ref.1
Mutagenesis48211R → A: No effect on calcium channel activity. Abolishes ryanodine binding. Ref.1
Mutagenesis48231G → A: Reduced calcium channel activity. Reduces single channel conductance by 97%. No effect on ryaodine binding. Ref.1
Mutagenesis48241G → A: No effect on calcium channel activity. Abolishes ryanodine binding. Ref.1
Mutagenesis48251G → A: Strongly reduced calcium channel activity. Abolishes ryanodine binding. Ref.1
Mutagenesis48271G → A: No effect on calcium channel activity. Abolishes ryanodine binding. Ref.1
Mutagenesis48281D → A: No effect on calcium channel activity. Abolishes ryanodine binding. Ref.1
Sequence conflict13321N → S in AAG34081. Ref.1
Sequence conflict14121D → G in AAG34081. Ref.1
Sequence conflict19621R → K in AAG34081. Ref.1
Sequence conflict22651V → VA in AAG34081. Ref.1
Sequence conflict25321P → R in AAG34081. Ref.1
Sequence conflict31921A → T in AAG34081. Ref.1
Sequence conflict35331L → F in AAG34081. Ref.1
Sequence conflict43241I → T in CAA58785. Ref.4
Sequence conflict48531V → E in CAA58785. Ref.4

Secondary structure

........................................................................................................................ 4966
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
E9Q401 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: F43425091AF7114F

FASTA4,966564,819
        10         20         30         40         50         60 
MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP 

        70         80         90        100        110        120 
DLSICTFVLE QSLSVRALQE MLANTVEKSE GQVDVEKWKF MMKTAQGGGH RTLLYGHAIL 

       130        140        150        160        170        180 
LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ EDTTGEACWW TIHPASKQRS EGEKVRVGDD 

       190        200        210        220        230        240 
LILVSVSSER YLHLSYGNSS WHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH 

       250        260        270        280        290        300 
MDECLTVPSG EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV 

       310        320        330        340        350        360 
TTGKYLSLME DKNLLLMDKE KADVKSTAFA FRSSKEKLDV GVRKEVDGMG TSEIKYGDSI 

       370        380        390        400        410        420 
CYIQHVDTGL WLTYQAVDVK SARMGSIQRK AIMHHEGHMD DGLNLSRSQH EESRTARVIR 

       430        440        450        460        470        480 
STVFLFNRFI RGLDALSKKV KLPTIDLPIE SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR 

       490        500        510        520        530        540 
ALKNRQNLFQ EEGMINLVLE CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL 

       550        560        570        580        590        600 
IRGNRKNCAQ FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL 

       610        620        630        640        650        660 
LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN HVSSMRPNIF 

       670        680        690        700        710        720 
LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST EGYSPYPGGG EEWGGNGVGD 

       730        740        750        760        770        780 
DLFSYGFDGL HLWSGCIART VSSPNQHLLR TDDVISCCLD LSAPSISFRI NGQPVQGMFE 

       790        800        810        820        830        840 
NFNIDGLFFP VVSFSAGIKV RFLLGGRHGE FKFLPPPGYA ACYEAVLPKE KLKVEHSREY 

       850        860        870        880        890        900 
KQERTYTRDL LGPTVSLTQA AFTPVPVDTS QIVLPPHLER IRERLAENIH ELWVMNKIEL 

       910        920        930        940        950        960 
GWQYGPVRDD NKRQHPCLVE FCKLPEQERN YNLQMSLETL KTLLALGCHV GIADEHAEEK 

       970        980        990       1000       1010       1020 
VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA ENAHNVWARD RIRQGWTYGI 

      1030       1040       1050       1060       1070       1080 
QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL REAVRTLLGY GYHLEAPDQD HASRAEVCSG 

      1090       1100       1110       1120       1130       1140 
TGERFRIFRA EKTYAVKAGR WYFEFEAVTA GDMRVGWSRP GCQPDLELGS DDRAFAFDGF 

      1150       1160       1170       1180       1190       1200 
KAQRWHQGNE HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG 

      1210       1220       1230       1240       1250       1260 
FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW LSKRLPQFLQ 

      1270       1280       1290       1300       1310       1320 
VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNNNTDIM FYRLSMPIEC AEVFSKSVAG 

      1330       1340       1350       1360       1370       1380 
GLPGAGFYGP KNDLEDFDVD SDFEVLMKTA HGHLVPDRID KDKETPKPEF NNHKDYAQEK 

      1390       1400       1410       1420       1430       1440 
PSRLKQRFLL RRTKPDYSTG HSARLTEDVL ADDRDDYEYL MQTSTYYYSV RIFPGQEPAN 

      1450       1460       1470       1480       1490       1500 
VWVGWITSDF HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR 

      1510       1520       1530       1540       1550       1560 
NNSNGLEIGC VVDAASGLLT FIANGKELST YYQVEPSTKL FPAVFAQATS PNVFQFELGR 

      1570       1580       1590       1600       1610       1620 
IKNVMPLSAG LFKSEHKNPV PQCPPRLHVQ FLSHVLWSRM PNQFLKVDVS RISERQGWLV 

      1630       1640       1650       1660       1670       1680 
QCLDPLQFMS LHIPEENRSV DILELTEQEE LLQFHYHTLR LYSAVCALGN HRVAHALCSH 

      1690       1700       1710       1720       1730       1740 
VDEPQLLYAI ENKYMPGLLR AGYYDLLIDI HLSSYATARL MMNNEFIVPM TEETKSITLF 

      1750       1760       1770       1780       1790       1800 
PDENKKHGLP GIGLSTSLRP RMRFSSPSFV SISNDCYQYS PEFPLDILKA KTIQMLTEAV 

      1810       1820       1830       1840       1850       1860 
KEGSLHARDP VGGTTEFLFV PLIKLFYTLL IMGIFHNEDL KHILQLIEPS VFKEAAVPEE 

      1870       1880       1890       1900       1910       1920 
EGGTPEKEIS IEDAKLEGEE EAKGGKRPKE GLLQMKLPEP VKLQMCLLLQ YLCDCQVRHR 

      1930       1940       1950       1960       1970       1980 
IEAIVAFSDD FVAKLQDNQR FRYNEVMQAL NMSAALTARK TREFRSPPQE QINMLLNFKD 

      1990       2000       2010       2020       2030       2040 
DKSECPCPEE IRDQLLDFHE DLMTHCGIEL DEDGSLDGSN DLTIRGRLLS LVEKVTYLKK 

      2050       2060       2070       2080       2090       2100 
KQAEKPVASD SRKCSSLQQL ISETMVRWAQ ESVIEDPELV RAMFVLLHRQ YDGIGGLVRA 

      2110       2120       2130       2140       2150       2160 
LPKTYTINGV SVEDTINLLA SLGQIRSLLS VRMGKEEEKL MIRGLGDIMN NKVFYQHPNL 

      2170       2180       2190       2200       2210       2220 
MRALGMHETV MEVMVNVLGG GESKEITFPK MVANCCRFLC YFCRISRQNQ KAMFDHLSYL 

      2230       2240       2250       2260       2270       2280 
LENSSVGLAS PAMRGSTPLD VAAASVMDNN ELALALREPD LEKVVRYLAG CGLQSCQMLV 

      2290       2300       2310       2320       2330       2340 
SKGYPDIGWN PVEGERYLDF LRFAVFCNGE SVEENANVVV RLLIRRPECF GPALRGEGGN 

      2350       2360       2370       2380       2390       2400 
GLLAAMEEAI KIAEDPSRDG PSPTSGSSKT LDIEEEEDDT IHMGNAIMTF YAALIDLLGR 

      2410       2420       2430       2440       2450       2460 
CAPEMHLIHA GKGEAIRIRS ILRSLIPLGD LVGVISIAFQ MPTIAKDGKV VEPDMSAGFC 

      2470       2480       2490       2500       2510       2520 
PDHKAAMVLF LDRVYGIEVQ DFLLHLLEVG FLPDLRAAAS LDTAALSATD MALALNRYLC 

      2530       2540       2550       2560       2570       2580 
TAVLPLLTRC APLFAGTEHH ASLIDSLLHT VYRLSKGCSL TKAQRDSIEV CLLSICGQLR 

      2590       2600       2610       2620       2630       2640 
PSMMQHLLRR LVFDVPLLNE HAKMPLKLLT NHYERCWKYY CLPGGWGNFG AASEEELHLS 

      2650       2660       2670       2680       2690       2700 
RKLFWGIFDA LSQKKYEQEL FKLALPCLSA VAGALPPDYM ESNYVSMMEK QSSMDSEGNF 

      2710       2720       2730       2740       2750       2760 
NPQPVDTSNI TIPEKLEYFI NKYAEHSHDK WSMDKLANGW IYGEIYSDSS KIQPLMKPYK 

      2770       2780       2790       2800       2810       2820 
LLSEKEKEIY RWPIKESLKT MLAWGWRIER TREGDSMALY NRTRRISQTS QVSIDAAHGY 

      2830       2840       2850       2860       2870       2880 
SPRAIDMSNV TLSRDLHAMA EMMAENYHNI WAKKKKLELE SKGGGNHPLL VPYDTLTAKE 

      2890       2900       2910       2920       2930       2940 
KAKDREKAQD IFKFLQISGY VVSRGFKDLD LDTPSIEKRF AYSFLQQLIR YVDEAHQYIL 

      2950       2960       2970       2980       2990       3000 
EFDGGSRSKG EHFPYEQEIK FFAKVVLPLI DQYFKNHRLY FLSAASRPLC TGGHASNKEK 

      3010       3020       3030       3040       3050       3060 
EMVTSLFCKL GVLVRHRISL FGNDATSIVN CLHILGQTLD ARTVMKTGLD SVKSALRAFL 

      3070       3080       3090       3100       3110       3120 
DNAAEDLEKT MENLKQGQFT HTRSQPKGVT QIINYTTVAL LPMLSSLFEH IGQHQFGEDL 

      3130       3140       3150       3160       3170       3180 
ILEDVQVSCY RILTSLYALG TSKSIYVERQ RSALGECLAA FAGAFPIAFL ETHLDKHNVY 

      3190       3200       3210       3220       3230       3240 
SIYNTRSSRE RAALSLPANV EDVCPNIPSL EKLMTEIIEL AESGIRYTQM PYMMEVVLPM 

      3250       3260       3270       3280       3290       3300 
LCSYMSRWWE HGPENHPERA EMCCTALNSE HMNTLLGNIL KIIYNNLGID EGAWMKRLAV 

      3310       3320       3330       3340       3350       3360 
FSQPIINKVK PQLLKTHFLP LMEKLKKKAA MVVSEEDHLK AEARGDMSEA ELLILDEFTT 

      3370       3380       3390       3400       3410       3420 
LARDLYAFYP LLIRFVDYNR AKWLKEPNPE AEELFRMVAE VFIYWSKSHN FKREEQNFVV 

      3430       3440       3450       3460       3470       3480 
QNEINNMSFL ITDTKSKMSK AAISDQERKK MKRKGDRYSM QTSLIVAALK RLLPIGLNIC 

      3490       3500       3510       3520       3530       3540 
APGDQELIAL AKNRFSLKDT EEEVRDIIRS NIHLQGKLED PAIRWQMALY KDLPNRTEDP 

      3550       3560       3570       3580       3590       3600 
SDPERTVERV LGIANVLFHL EQKSKYTGRG YFSLVEHPQR SKKAVWHKLL SKQRKRAVVA 

      3610       3620       3630       3640       3650       3660 
CFRMAPLYNL PRHRAVNLFL QGYEKSWIET EEHYFEDKLI EDLAKPGAEL PEEDEAMKRV 

      3670       3680       3690       3700       3710       3720 
DPLHQLILLF SRTALTEKCK LEEDFLYMAY ADIMAKSCHD EEDDDGEEEV KSFEEKEMEK 

      3730       3740       3750       3760       3770       3780 
QKLLYQQARL HDRGAAEMVL QTISASKGET GPMVAATLKL GIAILNGGNS TVQQKMLDYL 

      3790       3800       3810       3820       3830       3840 
KEKKDVGFFQ SLAGLMQSCS VLDLNAFERQ NKAEGLGMVT EEGSGEKVLQ DDEFTCDLFR 

      3850       3860       3870       3880       3890       3900 
FLQLLCEGHN SDFQNYLRTQ TGNNTTVNII ISTVDYLLRV QESISDFYWY YSGKDIIDEQ 

      3910       3920       3930       3940       3950       3960 
GQRNFSKAIQ VAKQVFNTLT EYIQGPCTGN QQSLAHSRLW DAVVGFLHVF AHMQMKLSQD 

      3970       3980       3990       4000       4010       4020 
SSQIELLKEL MDLQKDMVVM LLSMLEGNVV NGTIGKQMVD MLVESSNNVE MILKFFDMFL 

      4030       4040       4050       4060       4070       4080 
KLKDLTSSDT FKEYDPDGKG VISKRDFHKA MESHKHYTQS ETEFLLSCAE TDENETLDYE 

      4090       4100       4110       4120       4130       4140 
EFVKRFHEPA KDIGFNVAVL LTNLSEHMPN DTRLQTFLEL AESVLNYFQP FLGRIEIMGS 

      4150       4160       4170       4180       4190       4200 
AKRIERVYFE ISESSRTQWE KPQVKESKRQ FIFDVVNEGG EKEKMELFVN FCEDTIFEMQ 

      4210       4220       4230       4240       4250       4260 
LAAQISESDL NERLANKEES EKERPEEQAP RMGFFSLLTI QSALFALRYN VLTLVRMLSL 

      4270       4280       4290       4300       4310       4320 
KSLKKQMKRM KKMTVKDMVL AFFSSYWSVF VTLLHFVASV CRGFFRIVSS LLLGGSLVEG 

      4330       4340       4350       4360       4370       4380 
AKKIKVAELL ANMPDPTQDE VRGDEEEGER KPLESALPSE DLTDLKELTE ESDLLSDIFG 

      4390       4400       4410       4420       4430       4440 
LDLKREGGQY KLIPHNPNAG LSDLMTNPVP VPEVQEKFQE QKAKEEKEEK EETKSEPEKA 

      4450       4460       4470       4480       4490       4500 
EGEDGEKEEK AKDEKSKQKL RQLHTHRYGE PEVPESAFWK KIIAYQQKLL NYFARNFYNM 

      4510       4520       4530       4540       4550       4560 
RMLALFVAFA INFILLFYKV STSSVVEGKE LPTRTSSDTA KVTNSLDSSP HRIIAVHYVL 

      4570       4580       4590       4600       4610       4620 
EESSGYMEPT LRILAILHTI ISFFCIIGYY CLKVPLVIFK REKEVARKLE FDGLYITEQP 

      4630       4640       4650       4660       4670       4680 
SEDDIKGQWD RLVINTQSFP NNYWDKFVKR KVMDKYGEFY GRDRISELLG MDKAALDFSD 

      4690       4700       4710       4720       4730       4740 
AREKKKPKKD SSLSAVLNSI DVKYQMWKLG VVFTDNSFLY LAWYMTMSVL GHYNNFFFAA 

      4750       4760       4770       4780       4790       4800 
HLLDIAMGFK TLRTILSSVT HNGKQLVLTV GLLAVVVYLY TVVAFNFFRK FYNKSEDGDT 

      4810       4820       4830       4840       4850       4860 
PDMKCDDMLT CYMFHMYVGV RAGGGIGDEI EDPAGDEYEI YRIIFDITFF FFVIVILLAI 

      4870       4880       4890       4900       4910       4920 
IQGLIIDAFG ELRDQQEQVK EDMETKCFIC GIGNDYFDTV PHGFETHTLQ EHNLANYLFF 

      4930       4940       4950       4960 
LMYLINKDET EHTGQESYVW KMYQERCWEF FPAGDCFRKQ YEDQLN 

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References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI48742.
RefSeqNP_076357.2. NM_023868.2.
UniGeneMm.239871.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalE9Q401.
SMRE9Q401. Positions 11-543, 2700-2904, 3580-3606.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActE9Q401. 6 interactions.
MINTMINT-4129173.

PTM databases

PhosphoSiteE9Q401.

Proteomic databases

PRIDEE9Q401.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021750; ENSMUSP00000021750; ENSMUSG00000021313.
GeneID20191.
KEGGmmu:20191.
UCSCuc007pld.1. mouse.

Organism-specific databases

CTD6262.
MGIMGI:99685. Ryr2.

Phylogenomic databases

eggNOGNOG247670.
GeneTreeENSGT00690000101961.
HOGENOMHOG000231428.
HOVERGENHBG006699.
KOK04962.
OMASKVQPLM.
OrthoDBEOG71K622.
TreeFamTF315244.

Gene expression databases

ArrayExpressE9Q401.
BgeeE9Q401.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProIPR001870. 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]
PANTHERPTHR13715. PTHR13715. 1 hit.
PfamPF08709. 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]
PRINTSPR00795. RYANODINER.
SMARTSM00054. EFh. 2 hits.
SM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMSSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9ERN6.
NextBio297739.
PROE9Q401.
SOURCESearch...

Entry information

Entry nameRYR2_MOUSE
AccessionPrimary (citable) accession number: E9Q401
Secondary accession number(s): O70181 expand/collapse secondary AC list , Q62174, Q62197, Q9ERN6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot