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Protein

Ryanodine receptor 2

Gene

Ryr2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

  • calcium channel activity Source: UniProtKB
  • calcium-induced calcium release activity Source: MGI
  • calcium ion binding Source: GO_Central
  • calcium-release channel activity Source: UniProtKB
  • calmodulin binding Source: MGI
  • enzyme binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • organic cyclic compound binding Source: MGI
  • protein kinase A catalytic subunit binding Source: MGI
  • protein kinase A regulatory subunit binding Source: MGI
  • protein kinase binding Source: BHF-UCL
  • protein self-association Source: UniProtKB
  • ryanodine-sensitive calcium-release channel activity Source: MGI
  • suramin binding Source: MGI

GO - Biological processi

  • BMP signaling pathway Source: MGI
  • calcium ion transmembrane transport Source: MGI
  • calcium ion transport Source: UniProtKB
  • calcium ion transport into cytosol Source: MGI
  • calcium-mediated signaling Source: UniProtKB
  • calcium-mediated signaling using intracellular calcium source Source: MGI
  • canonical Wnt signaling pathway Source: MGI
  • cardiac muscle contraction Source: MGI
  • cardiac muscle hypertrophy Source: MGI
  • cellular calcium ion homeostasis Source: UniProtKB
  • cellular response to caffeine Source: UniProtKB
  • cellular response to epinephrine stimulus Source: BHF-UCL
  • cytosolic calcium ion transport Source: MGI
  • detection of calcium ion Source: MGI
  • embryonic heart tube morphogenesis Source: UniProtKB
  • establishment of protein localization to endoplasmic reticulum Source: MGI
  • left ventricular cardiac muscle tissue morphogenesis Source: MGI
  • positive regulation of calcium-transporting ATPase activity Source: MGI
  • positive regulation of heart rate Source: MGI
  • positive regulation of sequestering of calcium ion Source: MGI
  • positive regulation of the force of heart contraction Source: MGI
  • Purkinje myocyte to ventricular cardiac muscle cell signaling Source: BHF-UCL
  • regulation of atrial cardiac muscle cell action potential Source: MGI
  • regulation of AV node cell action potential Source: MGI
  • regulation of cardiac muscle contraction Source: MGI
  • regulation of cardiac muscle contraction by calcium ion signaling Source: MGI
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  • regulation of heart rate Source: BHF-UCL
  • regulation of SA node cell action potential Source: MGI
  • regulation of ventricular cardiac muscle cell action potential Source: MGI
  • release of sequestered calcium ion into cytosol Source: MGI
  • release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  • response to caffeine Source: UniProtKB
  • response to hypoxia Source: BHF-UCL
  • response to muscle activity Source: MGI
  • response to muscle stretch Source: MGI
  • response to redox state Source: MGI
  • type B pancreatic cell apoptotic process Source: BHF-UCL
  • 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

ReactomeiR-MMU-2672351. Stimuli-sensing channels.
R-MMU-5578775. Ion homeostasis.

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
Proteomesi
  • UP000000589 Componenti: 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
  • Sarcoplasmic reticulum By similarity

  • 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)DescriptionActionsGraphical viewLength
Topological domaini1 – 4231CytoplasmicSequence analysisAdd BLAST4231
Transmembranei4232 – 4252HelicalSequence analysisAdd BLAST21
Transmembranei4278 – 4298HelicalSequence analysisAdd BLAST21
Transmembranei4502 – 4522HelicalSequence analysisAdd BLAST21
Transmembranei4579 – 4599HelicalSequence analysisAdd BLAST21
Transmembranei4729 – 4749HelicalSequence analysisAdd BLAST21
Transmembranei4768 – 4788HelicalSequence analysisAdd BLAST21
Intramembranei4819 – 4828Pore-formingCurated10
Transmembranei4849 – 4869HelicalSequence analysisAdd BLAST21
Topological domaini4870 – 4966CytoplasmicSequence analysisAdd BLAST97

GO - Cellular componenti

  • calcium channel complex Source: BHF-UCL
  • extracellular exosome Source: MGI
  • integral component of membrane Source: MGI
  • membrane Source: MGI
  • protein complex Source: MGI
  • sarcolemma Source: GO_Central
  • sarcomere Source: BHF-UCL
  • sarcoplasmic reticulum Source: BHF-UCL
  • sarcoplasmic reticulum membrane Source: MGI
  • smooth endoplasmic reticulum Source: MGI
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi77A → V: No change to global protein fold or protein stability. Alters local protein folding. 1 Publication1
Mutagenesisi186V → M: No change to global protein fold or protein stability. Alters local protein folding. 1 Publication1
Mutagenesisi2813S → A: Protects against tachycardia and subsequent death due to heart failure. 1 Publication1
Mutagenesisi2813S → D: Abolishes phosphorylation by CaMK2D. Tendency to tachycardia and subsequent death due to heart failure. 1 Publication1
Mutagenesisi4819G → A: Strongly reduced calcium channel activity. Abolishes ryanodine binding. 1 Publication1
Mutagenesisi4821R → A: No effect on calcium channel activity. Abolishes ryanodine binding. 1 Publication1
Mutagenesisi4823G → A: Reduced calcium channel activity. Reduces single channel conductance by 97%. No effect on ryaodine binding. 1 Publication1
Mutagenesisi4824G → A: No effect on calcium channel activity. Abolishes ryanodine binding. 1 Publication1
Mutagenesisi4825G → A: Strongly reduced calcium channel activity. Abolishes ryanodine binding. 1 Publication1
Mutagenesisi4827G → A: No effect on calcium channel activity. Abolishes ryanodine binding. 1 Publication1
Mutagenesisi4828D → A: No effect on calcium channel activity. Abolishes ryanodine binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004155821 – 4966Ryanodine receptor 2Add BLAST4966

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1341PhosphoserineCombined sources1
Modified residuei1870PhosphoserineBy similarity1
Modified residuei2030Phosphoserine; by PKA1 Publication1
Modified residuei2368PhosphoserineCombined sources1
Modified residuei2696PhosphoserineBy similarity1
Modified residuei2796PhosphoserineCombined sources1
Modified residuei2807Phosphoserine; by CaMK2D and PKACombined sources2 Publications1
Modified residuei2810PhosphoserineCombined sources1
Modified residuei2813Phosphoserine; by CaMK2DCombined sources1 Publication1
Modified residuei2946PhosphoserineCombined sources1

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.
PaxDbiE9Q401.
PeptideAtlasiE9Q401.
PRIDEiE9Q401.

PTM databases

iPTMnetiE9Q401.
PhosphoSitePlusiE9Q401.

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

BgeeiENSMUSG00000021313.
ExpressionAtlasiE9Q401. baseline and differential.
GenevisibleiE9Q401. MM.

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. Interacts with SEPN1 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-643628,EBI-643628
Fkbp1bQ9Z2I22EBI-643628,EBI-6379859
HRCP233273EBI-643628,EBI-9639760From a different organism.
Plce1Q8K4S12EBI-643628,EBI-6902760

GO - Molecular functioni

  • calmodulin binding Source: MGI
  • enzyme binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • protein kinase A catalytic subunit binding Source: MGI
  • protein kinase A regulatory subunit binding Source: MGI
  • protein kinase binding Source: BHF-UCL
  • protein self-association Source: UniProtKB

Protein-protein interaction databases

BioGridi203046. 5 interactors.
IntActiE9Q401. 11 interactors.
MINTiMINT-4129173.
STRINGi10090.ENSMUSP00000021750.

Structurei

Secondary structure

14966
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 17Combined sources3
Beta strandi19 – 28Combined sources10
Beta strandi31 – 38Combined sources8
Beta strandi41 – 43Combined sources3
Beta strandi48 – 51Combined sources4
Turni53 – 57Combined sources5
Helixi62 – 64Combined sources3
Beta strandi67 – 73Combined sources7
Helixi75 – 84Combined sources10
Beta strandi97 – 102Combined sources6
Beta strandi118 – 123Combined sources6
Turni124 – 126Combined sources3
Beta strandi129 – 132Combined sources4
Beta strandi145 – 151Combined sources7
Beta strandi154 – 156Combined sources3
Beta strandi159 – 167Combined sources9
Beta strandi180 – 185Combined sources6
Turni186 – 188Combined sources3
Beta strandi191 – 196Combined sources6
Beta strandi198 – 208Combined sources11
Beta strandi212 – 216Combined sources5
Helixi220 – 222Combined sources3
Beta strandi233 – 238Combined sources6
Turni239 – 242Combined sources4
Beta strandi243 – 246Combined sources4
Helixi256 – 258Combined sources3
Beta strandi261 – 264Combined sources4
Helixi265 – 269Combined sources5
Helixi271 – 273Combined sources3
Beta strandi275 – 280Combined sources6
Turni283 – 286Combined sources4
Beta strandi294 – 299Combined sources6
Turni300 – 302Combined sources3
Beta strandi305 – 308Combined sources4
Beta strandi314 – 317Combined sources4
Helixi319 – 321Combined sources3
Helixi324 – 327Combined sources4
Beta strandi329 – 333Combined sources5
Turni356 – 358Combined sources3
Beta strandi360 – 365Combined sources6
Turni366 – 368Combined sources3
Beta strandi371 – 374Combined sources4
Beta strandi389 – 396Combined sources8
Beta strandi403 – 407Combined sources5
Helixi410 – 436Combined sources27
Helixi449 – 462Combined sources14
Helixi472 – 491Combined sources20
Helixi494 – 505Combined sources12
Beta strandi508 – 510Combined sources3
Helixi511 – 518Combined sources8
Helixi520 – 541Combined sources22
Beta strandi653 – 658Combined sources6
Beta strandi672 – 681Combined sources10
Beta strandi693 – 699Combined sources7
Helixi700 – 702Combined sources3
Beta strandi704 – 706Combined sources3
Helixi707 – 709Combined sources3
Beta strandi710 – 712Combined sources3
Beta strandi724 – 727Combined sources4
Beta strandi729 – 734Combined sources6
Beta strandi737 – 740Combined sources4
Beta strandi754 – 760Combined sources7
Turni761 – 764Combined sources4
Beta strandi765 – 770Combined sources6
Beta strandi788 – 794Combined sources7
Beta strandi799 – 803Combined sources5
Helixi822 – 825Combined sources4
Beta strandi833 – 839Combined sources7
Beta strandi1086 – 1089Combined sources4
Helixi1092 – 1094Combined sources3
Beta strandi1096 – 1109Combined sources14
Beta strandi1111 – 1118Combined sources8
Beta strandi1130 – 1138Combined sources9
Turni1139 – 1142Combined sources4
Beta strandi1143 – 1153Combined sources11
Beta strandi1161 – 1167Combined sources7
Turni1168 – 1171Combined sources4
Beta strandi1172 – 1177Combined sources6
Beta strandi1191 – 1194Combined sources4
Beta strandi1201 – 1207Combined sources7
Beta strandi1213 – 1216Combined sources4
Helixi1221 – 1223Combined sources3
Turni1227 – 1235Combined sources9
Helixi1239 – 1242Combined sources4
Helixi2714 – 2716Combined sources3
Helixi2717 – 2737Combined sources21
Turni2748 – 2751Combined sources4
Helixi2759 – 2761Combined sources3
Helixi2764 – 2783Combined sources20
Beta strandi2787 – 2790Combined sources4
Helixi2796 – 2799Combined sources4
Helixi2817 – 2819Combined sources3
Helixi2827 – 2829Combined sources3
Helixi2834 – 2861Combined sources28
Helixi2873 – 2875Combined sources3
Helixi2878 – 2897Combined sources20
Beta strandi2900 – 2903Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4P9IX-ray1.34A1080-1253[»]
4P9LX-ray1.44A1080-1253[»]
5C33X-ray1.21A/B650-844[»]
ProteinModelPortaliE9Q401.
SMRiE9Q401.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini110 – 165MIR 1PROSITE-ProRule annotationAdd BLAST56
Domaini172 – 217MIR 2PROSITE-ProRule annotationAdd BLAST46
Domaini225 – 280MIR 3PROSITE-ProRule annotationAdd BLAST56
Domaini286 – 343MIR 4PROSITE-ProRule annotationAdd BLAST58
Domaini351 – 408MIR 5PROSITE-ProRule annotationAdd BLAST58
Domaini599 – 809B30.2/SPRY 1PROSITE-ProRule annotationAdd BLAST211
Repeati853 – 9661Add BLAST114
Repeati967 – 10802Add BLAST114
Domaini1025 – 1222B30.2/SPRY 2PROSITE-ProRule annotationAdd BLAST198
Domaini1357 – 1563B30.2/SPRY 3PROSITE-ProRule annotationAdd BLAST207
Repeati2691 – 28093Add BLAST119
Repeati2811 – 29244Add BLAST114

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni853 – 29244 X approximate repeatsAdd BLAST2072
Regioni3580 – 3609Interaction with CALMBy similarityAdd BLAST30

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

eggNOGiKOG2243. Eukaryota.
ENOG410YCNW. LUCA.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiE9Q401.
KOiK04962.
OMAiRWWEHGP.
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. 5 hits.
PfamiPF13833. EF-hand_8. 1 hit.
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]
PRINTSiPR00795. RYANODINER.
SMARTiSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF47473. SSF47473. 1 hit.
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

« Hide

        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)DescriptionActionsGraphical viewLength
Sequence conflicti1332N → S in AAG34081 (PubMed:10473538).Curated1
Sequence conflicti1412D → G in AAG34081 (PubMed:10473538).Curated1
Sequence conflicti1962R → K in AAG34081 (PubMed:10473538).Curated1
Sequence conflicti2265V → VA in AAG34081 (PubMed:10473538).Curated1
Sequence conflicti2532P → R in AAG34081 (PubMed:10473538).Curated1
Sequence conflicti3192A → T in AAG34081 (PubMed:10473538).Curated1
Sequence conflicti3533L → F in AAG34081 (PubMed:10473538).Curated1
Sequence conflicti4324I → T in CAA58785 (PubMed:7876312).Curated1
Sequence conflicti4853V → E in CAA58785 (PubMed:7876312).Curated1

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.
CCDSiCCDS49206.1.
PIRiI48742.
RefSeqiNP_076357.2. NM_023868.2.
UniGeneiMm.239871.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4P9IX-ray1.34A1080-1253[»]
4P9LX-ray1.44A1080-1253[»]
5C33X-ray1.21A/B650-844[»]
ProteinModelPortaliE9Q401.
SMRiE9Q401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203046. 5 interactors.
IntActiE9Q401. 11 interactors.
MINTiMINT-4129173.
STRINGi10090.ENSMUSP00000021750.

PTM databases

iPTMnetiE9Q401.
PhosphoSitePlusiE9Q401.

Proteomic databases

MaxQBiE9Q401.
PaxDbiE9Q401.
PeptideAtlasiE9Q401.
PRIDEiE9Q401.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6262.
MGIiMGI:99685. Ryr2.

Phylogenomic databases

eggNOGiKOG2243. Eukaryota.
ENOG410YCNW. LUCA.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiE9Q401.
KOiK04962.
OMAiRWWEHGP.
TreeFamiTF315244.

Enzyme and pathway databases

ReactomeiR-MMU-2672351. Stimuli-sensing channels.
R-MMU-5578775. Ion homeostasis.

Miscellaneous databases

PROiE9Q401.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021313.
ExpressionAtlasiE9Q401. baseline and differential.
GenevisibleiE9Q401. MM.

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. 5 hits.
PfamiPF13833. EF-hand_8. 1 hit.
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]
PRINTSiPR00795. RYANODINER.
SMARTiSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF47473. SSF47473. 1 hit.
SSF49899. SSF49899. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 59 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.