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Ryanodine receptor 2 (RYR-2) (RyR2) (Cardiac muscle ryanodine receptor) (Cardiac muscle ryanodine receptor-calcium release channel) (Type 2 ryanodine receptor)

 RYR2_MOUSE              Reviewed;        4966 AA.
E9Q401; O70181; Q62174; Q62197; Q9ERN6;
22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 1.
22-NOV-2017, entry version 66.
RecName: Full=Ryanodine receptor 2;
Short=RYR-2;
Short=RyR2;
AltName: Full=Cardiac muscle ryanodine receptor;
AltName: Full=Cardiac muscle ryanodine receptor-calcium release channel;
AltName: Full=Type 2 ryanodine receptor;
Name=Ryr2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
AND MUTAGENESIS OF GLY-4819; ARG-4821; GLY-4823; GLY-4824; GLY-4825;
GLY-4827 AND ASP-4828.
PubMed=10473538; DOI=10.1074/jbc.274.37.25971;
Zhao M., Li P., Li X., Zhang L., Winkfein R.J., Chen S.R.;
"Molecular identification of the ryanodine receptor pore-forming
segment.";
J. Biol. Chem. 274:25971-25974(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16, FUNCTION, AND DISRUPTION
PHENOTYPE.
PubMed=9628868; DOI=10.1093/emboj/17.12.3309;
Takeshima H., Komazaki S., Hirose K., Nishi M., Noda T., Iino M.;
"Embryonic lethality and abnormal cardiac myocytes in mice lacking
ryanodine receptor type 2.";
EMBO J. 17:3309-3316(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 4145-4966, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=7876312; DOI=10.1083/jcb.128.5.893;
Giannini G., Conti A., Mammarella S., Scrobogna M., Sorrentino V.;
"The ryanodine receptor/calcium channel genes are widely and
differentially expressed in murine brain and peripheral tissues.";
J. Cell Biol. 128:893-904(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 4863-4966, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Heart;
PubMed=7621815;
Takeshima H., Yamazawa T., Ikemoto T., Takekura H., Nishi M., Noda T.,
Iino M.;
"Ca(2+)-induced Ca2+ release in myocytes from dyspedic mice lacking
the type-1 ryanodine receptor.";
EMBO J. 14:2999-3006(1995).
[6]
PHOSPHORYLATION AT SER-2030.
PubMed=17693412; DOI=10.1074/jbc.M703510200;
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.;
"Functional consequence of protein kinase A-dependent phosphorylation
of the cardiac ryanodine receptor: sensitization of store overload-
induced Ca2+ release.";
J. Biol. Chem. 282:30256-30264(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1341; SER-2368;
SER-2796; SER-2807; SER-2810; SER-2813 AND SER-2946, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, PHOSPHORYLATION AT SER-2807 AND SER-2813, INTERACTION WITH
FKBP1B, AND MUTAGENESIS OF SER-2813.
PubMed=21098440; DOI=10.1161/CIRCULATIONAHA.110.982298;
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.;
"Ryanodine receptor phosphorylation by calcium/calmodulin-dependent
protein kinase II promotes life-threatening ventricular arrhythmias in
mice with heart failure.";
Circulation 122:2669-2679(2010).
[9]
FUNCTION, INTERACTION WITH FKBP1A AND FKBP1B, AND PHOSPHORYLATION AT
SER-2807.
PubMed=20431056; DOI=10.1161/CIRCRESAHA.110.219816;
Guo T., Cornea R.L., Huke S., Camors E., Yang Y., Picht E.,
Fruen B.R., Bers D.M.;
"Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized
cardiac myocytes and effects on Ca sparks.";
Circ. Res. 106:1743-1752(2010).
[10]
REVIEW.
PubMed=20214899; DOI=10.1016/j.febslet.2010.03.005;
Kushnir A., Betzenhauser M.J., Marks A.R.;
"Ryanodine receptor studies using genetically engineered mice.";
FEBS Lett. 584:1956-1965(2010).
[11]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-217, AND MUTAGENESIS OF
ALA-77 AND VAL-186.
PubMed=19913485; DOI=10.1016/j.str.2009.08.016;
Lobo P.A., Van Petegem F.;
"Crystal structures of the N-terminal domains of cardiac and skeletal
muscle ryanodine receptors: insights into disease mutations.";
Structure 17:1505-1514(2009).
[12]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-217.
PubMed=21645850; DOI=10.1016/j.str.2011.03.016;
Lobo P.A., Kimlicka L., Tung C.C., Van Petegem F.;
"The deletion of exon 3 in the cardiac ryanodine receptor is rescued
by beta strand switching.";
Structure 19:790-798(2011).
[13] {ECO:0000244|PDB:4ETV}
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2699-2904.
PubMed=22705209; DOI=10.1016/j.str.2012.04.015;
Yuchi Z., Lau K., Van Petegem F.;
"Disease mutations in the ryanodine receptor central region: crystal
structures of a phosphorylation hot spot domain.";
Structure 20:1201-1211(2012).
[14] {ECO:0000244|PDB:2MC2, ECO:0000244|PDB:4KEI, ECO:0000244|PDB:4KEJ, ECO:0000244|PDB:4KEK}
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-217, AND DISULFIDE BONDS.
PubMed=23978697; DOI=10.1016/j.jmb.2013.08.015;
Amador F.J., Kimlicka L., Stathopulos P.B., Gasmi-Seabrook G.M.,
Maclennan D.H., Van Petegem F., Ikura M.;
"Type 2 ryanodine receptor domain A contains a unique and dynamic
alpha-helix that transitions to a beta-strand in a mutant linked with
a heritable cardiomyopathy.";
J. Mol. Biol. 425:4034-4046(2013).
[15] {ECO:0000244|PDB:5C33}
X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) OF 650-844.
PubMed=26245150; DOI=10.1038/ncomms8947;
Yuchi Z., Yuen S.M., Lau K., Underhill A.Q., Cornea R.L.,
Fessenden J.D., Van Petegem F.;
"Crystal structures of ryanodine receptor SPRY1 and tandem-repeat
domains reveal a critical FKBP12 binding determinant.";
Nat. Commun. 6:7947-7947(2015).
-!- FUNCTION: Calcium channel that mediates the release of Ca(2+) 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 Ca(2+) 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.
{ECO:0000269|PubMed:10473538, ECO:0000269|PubMed:20431056,
ECO:0000269|PubMed:21098440, ECO:0000269|PubMed:9628868}.
-!- ENZYME REGULATION: 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).
{ECO:0000250|UniProtKB:P11716}.
-!- SUBUNIT: 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 Ca(2+) leaks. Interacts with SELENON (By similarity).
{ECO:0000250|UniProtKB:P30957, ECO:0000250|UniProtKB:Q92736,
ECO:0000269|PubMed:10473538, ECO:0000269|PubMed:20431056,
ECO:0000269|PubMed:21098440}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-643628, EBI-643628;
Q9Z2I2:Fkbp1b; NbExp=3; IntAct=EBI-643628, EBI-6379859;
P23327:HRC (xeno); NbExp=3; IntAct=EBI-643628, EBI-9639760;
Q8K4S1:Plce1; NbExp=2; IntAct=EBI-643628, EBI-6902760;
-!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
{ECO:0000305|PubMed:10473538}; Multi-pass membrane protein
{ECO:0000305|PubMed:10473538}. Membrane
{ECO:0000305|PubMed:10473538}; Multi-pass membrane protein
{ECO:0000305|PubMed:10473538}. Sarcoplasmic reticulum
{ECO:0000250|UniProtKB:P30957}. Note=The number of predicted
transmembrane domains varies between orthologs, but both N-
terminus and C-terminus seem to be cytoplasmic. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in heart, lung, cerebellum
and brain. Detected at lower levels in adrenal gland, stomach,
thymus, esophagus and ovary. {ECO:0000269|PubMed:7621815,
ECO:0000269|PubMed:7876312}.
-!- DOMAIN: The calcium release channel activity resides in the C-
terminal region while the remaining part of the protein resides in
the cytoplasm. {ECO:0000305}.
-!- PTM: 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 Ca(2+) levels. {ECO:0000269|PubMed:17693412,
ECO:0000269|PubMed:20431056, ECO:0000269|PubMed:21098440}.
-!- PTM: Phosphorylation at Ser-2030 by PKA enhances the response to
lumenal calcium. {ECO:0000269|PubMed:17693412}.
-!- 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 Ca(2+).
{ECO:0000269|PubMed:9628868}.
-!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family.
RYR2 subfamily. {ECO:0000305}.
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EMBL; AF295105; AAG34081.1; -; mRNA.
EMBL; AC131329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC159208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CT010468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CT572985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB012003; BAA25137.1; -; Genomic_DNA.
EMBL; X83933; CAA58785.1; -; mRNA.
EMBL; D38217; BAA07392.1; -; mRNA.
CCDS; CCDS49206.1; -.
PIR; I48742; I48742.
RefSeq; NP_076357.2; NM_023868.2.
UniGene; Mm.239871; -.
PDB; 2MC2; NMR; -; A=10-224.
PDB; 3IM5; X-ray; 2.55 A; A/B=1-217.
PDB; 3IM6; X-ray; 1.70 A; A=1-217.
PDB; 3IM7; X-ray; 2.21 A; A=1-217.
PDB; 3QR5; X-ray; 2.30 A; A/B=1-217.
PDB; 4ETV; X-ray; 1.65 A; A/B=2699-2904.
PDB; 4KEI; X-ray; 2.41 A; A=1-217.
PDB; 4KEJ; X-ray; 2.55 A; A=1-217.
PDB; 4KEK; X-ray; 2.15 A; A=1-217.
PDB; 4L4H; X-ray; 2.00 A; A=1-547.
PDB; 4L4I; X-ray; 2.15 A; A=1-547.
PDB; 4P9I; X-ray; 1.34 A; A=1080-1253.
PDB; 4P9L; X-ray; 1.44 A; A=1080-1253.
PDB; 5C33; X-ray; 1.21 A; A/B=650-844.
PDBsum; 2MC2; -.
PDBsum; 3IM5; -.
PDBsum; 3IM6; -.
PDBsum; 3IM7; -.
PDBsum; 3QR5; -.
PDBsum; 4ETV; -.
PDBsum; 4KEI; -.
PDBsum; 4KEJ; -.
PDBsum; 4KEK; -.
PDBsum; 4L4H; -.
PDBsum; 4L4I; -.
PDBsum; 4P9I; -.
PDBsum; 4P9L; -.
PDBsum; 5C33; -.
ProteinModelPortal; E9Q401; -.
SMR; E9Q401; -.
BioGrid; 203046; 6.
IntAct; E9Q401; 13.
MINT; MINT-4129173; -.
STRING; 10090.ENSMUSP00000021750; -.
iPTMnet; E9Q401; -.
PhosphoSitePlus; E9Q401; -.
MaxQB; E9Q401; -.
PaxDb; E9Q401; -.
PeptideAtlas; E9Q401; -.
PRIDE; E9Q401; -.
Ensembl; ENSMUST00000021750; ENSMUSP00000021750; ENSMUSG00000021313.
GeneID; 20191; -.
KEGG; mmu:20191; -.
UCSC; uc007pld.1; mouse.
CTD; 6262; -.
MGI; MGI:99685; Ryr2.
eggNOG; KOG2243; Eukaryota.
eggNOG; ENOG410YCNW; LUCA.
GeneTree; ENSGT00760000119152; -.
HOGENOM; HOG000231428; -.
HOVERGEN; HBG006699; -.
InParanoid; E9Q401; -.
KO; K04962; -.
OMA; EHMPNDT; -.
TreeFam; TF315244; -.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
Reactome; R-MMU-5578775; Ion homeostasis.
PRO; PR:E9Q401; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021313; -.
ExpressionAtlas; E9Q401; baseline and differential.
Genevisible; E9Q401; MM.
GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IC:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0030017; C:sarcomere; IDA:BHF-UCL.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:MGI.
GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI.
GO; GO:0030018; C:Z disc; IDA:MGI.
GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
GO; GO:0048763; F:calcium-induced calcium release activity; ISO:MGI.
GO; GO:0015278; F:calcium-release channel activity; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0097159; F:organic cyclic compound binding; IPI:MGI.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0043621; F:protein self-association; IMP:UniProtKB.
GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IDA:MGI.
GO; GO:0043924; F:suramin binding; ISO:MGI.
GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0060402; P:calcium ion transport into cytosol; ISO:MGI.
GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
GO; GO:0003300; P:cardiac muscle hypertrophy; IMP:MGI.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0071313; P:cellular response to caffeine; IDA:UniProtKB.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IMP:BHF-UCL.
GO; GO:0060401; P:cytosolic calcium ion transport; IMP:MGI.
GO; GO:0005513; P:detection of calcium ion; ISO:MGI.
GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:UniProtKB.
GO; GO:0072599; P:establishment of protein localization to endoplasmic reticulum; ISO:MGI.
GO; GO:0003220; P:left ventricular cardiac muscle tissue morphogenesis; IMP:MGI.
GO; GO:1901896; P:positive regulation of calcium-transporting ATPase activity; ISO:MGI.
GO; GO:0010460; P:positive regulation of heart rate; IMP:MGI.
GO; GO:0051284; P:positive regulation of sequestering of calcium ion; ISO:MGI.
GO; GO:0098735; P:positive regulation of the force of heart contraction; ISO:MGI.
GO; GO:0086029; P:Purkinje myocyte to ventricular cardiac muscle cell signaling; IMP:BHF-UCL.
GO; GO:0098910; P:regulation of atrial cardiac muscle cell action potential; ISO:MGI.
GO; GO:0098904; P:regulation of AV node cell action potential; ISO:MGI.
GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:MGI.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; ISO:MGI.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IGI:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
GO; GO:0098907; P:regulation of SA node cell action potential; ISO:MGI.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:MGI.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:MGI.
GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0031000; P:response to caffeine; IDA:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
GO; GO:0014850; P:response to muscle activity; ISO:MGI.
GO; GO:0035994; P:response to muscle stretch; ISO:MGI.
GO; GO:0051775; P:response to redox state; ISO:MGI.
GO; GO:0097050; P:type B pancreatic cell apoptotic process; IMP:BHF-UCL.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
CDD; cd12877; SPRY1_RyR; 1.
CDD; cd12878; SPRY2_RyR; 1.
CDD; cd12879; SPRY3_RyR; 1.
Gene3D; 1.25.10.30; -; 2.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR014821; Ins145_P3_rcpt.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR035910; IP3R_RIH_dom_sf.
InterPro; IPR036300; MIR_dom_sf.
InterPro; IPR016093; MIR_motif.
InterPro; IPR013662; RIH_assoc-dom.
InterPro; IPR000699; RIH_dom.
InterPro; IPR013333; Ryan_recept.
InterPro; IPR003032; Ryanodine_rcpt.
InterPro; IPR015925; Ryanodine_recept-rel.
InterPro; IPR009460; Ryanrecept_TM4-6.
InterPro; IPR035761; SPRY1_RyR.
InterPro; IPR035764; SPRY2_RyR.
InterPro; IPR035762; SPRY3_RyR.
InterPro; IPR003877; SPRY_dom.
PANTHER; PTHR13715; PTHR13715; 1.
Pfam; PF13833; EF-hand_8; 1.
Pfam; PF08709; Ins145_P3_rec; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF02815; MIR; 1.
Pfam; PF08454; RIH_assoc; 1.
Pfam; PF06459; RR_TM4-6; 1.
Pfam; PF01365; RYDR_ITPR; 2.
Pfam; PF02026; RyR; 4.
Pfam; PF00622; SPRY; 3.
PRINTS; PR00795; RYANODINER.
SMART; SM00472; MIR; 4.
SMART; SM00449; SPRY; 3.
SUPFAM; SSF100909; SSF100909; 2.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49899; SSF49899; 2.
SUPFAM; SSF82109; SSF82109; 2.
PROSITE; PS50188; B302_SPRY; 3.
PROSITE; PS50919; MIR; 5.
1: Evidence at protein level;
3D-structure; Calcium; Calcium channel; Calcium transport;
Calmodulin-binding; Complete proteome; Developmental protein;
Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
Phosphoprotein; Reference proteome; Repeat; Sarcoplasmic reticulum;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 4966 Ryanodine receptor 2.
/FTId=PRO_0000415582.
TOPO_DOM 1 4231 Cytoplasmic. {ECO:0000255}.
TRANSMEM 4232 4252 Helical. {ECO:0000255}.
TRANSMEM 4278 4298 Helical. {ECO:0000255}.
TRANSMEM 4502 4522 Helical. {ECO:0000255}.
TRANSMEM 4579 4599 Helical. {ECO:0000255}.
TRANSMEM 4729 4749 Helical. {ECO:0000255}.
TRANSMEM 4768 4788 Helical. {ECO:0000255}.
INTRAMEM 4819 4828 Pore-forming. {ECO:0000305}.
TRANSMEM 4849 4869 Helical. {ECO:0000255}.
TOPO_DOM 4870 4966 Cytoplasmic. {ECO:0000255}.
DOMAIN 110 165 MIR 1. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 172 217 MIR 2. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 225 280 MIR 3. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 286 343 MIR 4. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 351 408 MIR 5. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 599 809 B30.2/SPRY 1. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
REPEAT 853 966 1.
REPEAT 967 1080 2.
DOMAIN 1025 1222 B30.2/SPRY 2. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
DOMAIN 1357 1563 B30.2/SPRY 3. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
REPEAT 2691 2809 3.
REPEAT 2811 2924 4.
REGION 853 2924 4 X approximate repeats.
REGION 3580 3609 Interaction with CALM. {ECO:0000250}.
MOD_RES 1341 1341 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1870 1870 Phosphoserine.
{ECO:0000250|UniProtKB:B0LPN4}.
MOD_RES 2030 2030 Phosphoserine; by PKA.
{ECO:0000269|PubMed:17693412}.
MOD_RES 2368 2368 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2696 2696 Phosphoserine.
{ECO:0000250|UniProtKB:B0LPN4}.
MOD_RES 2796 2796 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2807 2807 Phosphoserine; by CaMK2D and PKA.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:20431056,
ECO:0000269|PubMed:21098440}.
MOD_RES 2810 2810 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2813 2813 Phosphoserine; by CaMK2D.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:21098440}.
MOD_RES 2946 2946 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MUTAGEN 77 77 A->V: No change to global protein fold or
protein stability. Alters local protein
folding. {ECO:0000269|PubMed:19913485}.
MUTAGEN 186 186 V->M: No change to global protein fold or
protein stability. Alters local protein
folding. {ECO:0000269|PubMed:19913485}.
MUTAGEN 2813 2813 S->A: Protects against tachycardia and
subsequent death due to heart failure.
{ECO:0000269|PubMed:21098440}.
MUTAGEN 2813 2813 S->D: Abolishes phosphorylation by
CaMK2D. Tendency to tachycardia and
subsequent death due to heart failure.
{ECO:0000269|PubMed:21098440}.
MUTAGEN 4819 4819 G->A: Strongly reduced calcium channel
activity. Abolishes ryanodine binding.
{ECO:0000269|PubMed:10473538}.
MUTAGEN 4821 4821 R->A: No effect on calcium channel
activity. Abolishes ryanodine binding.
{ECO:0000269|PubMed:10473538}.
MUTAGEN 4823 4823 G->A: Reduced calcium channel activity.
Reduces single channel conductance by
97%. No effect on ryaodine binding.
{ECO:0000269|PubMed:10473538}.
MUTAGEN 4824 4824 G->A: No effect on calcium channel
activity. Abolishes ryanodine binding.
{ECO:0000269|PubMed:10473538}.
MUTAGEN 4825 4825 G->A: Strongly reduced calcium channel
activity. Abolishes ryanodine binding.
{ECO:0000269|PubMed:10473538}.
MUTAGEN 4827 4827 G->A: No effect on calcium channel
activity. Abolishes ryanodine binding.
{ECO:0000269|PubMed:10473538}.
MUTAGEN 4828 4828 D->A: No effect on calcium channel
activity. Abolishes ryanodine binding.
{ECO:0000269|PubMed:10473538}.
CONFLICT 1332 1332 N -> S (in Ref. 1; AAG34081).
{ECO:0000305}.
CONFLICT 1412 1412 D -> G (in Ref. 1; AAG34081).
{ECO:0000305}.
CONFLICT 1962 1962 R -> K (in Ref. 1; AAG34081).
{ECO:0000305}.
CONFLICT 2265 2265 V -> VA (in Ref. 1; AAG34081).
{ECO:0000305}.
CONFLICT 2532 2532 P -> R (in Ref. 1; AAG34081).
{ECO:0000305}.
CONFLICT 3192 3192 A -> T (in Ref. 1; AAG34081).
{ECO:0000305}.
CONFLICT 3533 3533 L -> F (in Ref. 1; AAG34081).
{ECO:0000305}.
CONFLICT 4324 4324 I -> T (in Ref. 4; CAA58785).
{ECO:0000305}.
CONFLICT 4853 4853 V -> E (in Ref. 4; CAA58785).
{ECO:0000305}.
STRAND 15 17 {ECO:0000244|PDB:4KEJ}.
STRAND 19 28 {ECO:0000244|PDB:3IM6}.
STRAND 31 38 {ECO:0000244|PDB:3IM6}.
STRAND 41 43 {ECO:0000244|PDB:3IM6}.
STRAND 48 51 {ECO:0000244|PDB:3IM6}.
TURN 53 57 {ECO:0000244|PDB:4L4H}.
HELIX 62 64 {ECO:0000244|PDB:3IM6}.
STRAND 67 73 {ECO:0000244|PDB:3IM6}.
HELIX 75 84 {ECO:0000244|PDB:3IM6}.
STRAND 95 97 {ECO:0000244|PDB:2MC2}.
HELIX 98 107 {ECO:0000244|PDB:2MC2}.
STRAND 118 123 {ECO:0000244|PDB:3IM6}.
TURN 124 126 {ECO:0000244|PDB:3IM6}.
STRAND 129 132 {ECO:0000244|PDB:3IM6}.
STRAND 145 151 {ECO:0000244|PDB:3IM6}.
STRAND 154 156 {ECO:0000244|PDB:3IM6}.
STRAND 159 167 {ECO:0000244|PDB:3IM6}.
STRAND 180 185 {ECO:0000244|PDB:3IM6}.
TURN 186 188 {ECO:0000244|PDB:3IM6}.
STRAND 191 196 {ECO:0000244|PDB:3IM6}.
STRAND 198 208 {ECO:0000244|PDB:3IM6}.
STRAND 212 216 {ECO:0000244|PDB:3IM6}.
HELIX 220 222 {ECO:0000244|PDB:4L4H}.
STRAND 233 238 {ECO:0000244|PDB:4L4H}.
TURN 239 242 {ECO:0000244|PDB:4L4H}.
STRAND 243 246 {ECO:0000244|PDB:4L4H}.
HELIX 256 258 {ECO:0000244|PDB:4L4H}.
STRAND 261 264 {ECO:0000244|PDB:4L4H}.
HELIX 265 269 {ECO:0000244|PDB:4L4H}.
HELIX 271 273 {ECO:0000244|PDB:4L4H}.
STRAND 275 280 {ECO:0000244|PDB:4L4H}.
TURN 283 286 {ECO:0000244|PDB:4L4H}.
STRAND 294 299 {ECO:0000244|PDB:4L4H}.
TURN 300 302 {ECO:0000244|PDB:4L4H}.
STRAND 305 308 {ECO:0000244|PDB:4L4H}.
STRAND 314 317 {ECO:0000244|PDB:4L4H}.
HELIX 319 321 {ECO:0000244|PDB:4L4H}.
HELIX 324 327 {ECO:0000244|PDB:4L4H}.
STRAND 329 333 {ECO:0000244|PDB:4L4H}.
TURN 356 358 {ECO:0000244|PDB:4L4H}.
STRAND 360 365 {ECO:0000244|PDB:4L4H}.
TURN 366 368 {ECO:0000244|PDB:4L4H}.
STRAND 371 374 {ECO:0000244|PDB:4L4H}.
STRAND 389 396 {ECO:0000244|PDB:4L4H}.
STRAND 403 407 {ECO:0000244|PDB:4L4H}.
HELIX 410 436 {ECO:0000244|PDB:4L4H}.
HELIX 449 462 {ECO:0000244|PDB:4L4H}.
HELIX 472 491 {ECO:0000244|PDB:4L4H}.
HELIX 494 505 {ECO:0000244|PDB:4L4H}.
STRAND 508 510 {ECO:0000244|PDB:4L4H}.
HELIX 511 518 {ECO:0000244|PDB:4L4H}.
HELIX 520 541 {ECO:0000244|PDB:4L4H}.
STRAND 653 658 {ECO:0000244|PDB:5C33}.
STRAND 672 681 {ECO:0000244|PDB:5C33}.
STRAND 693 699 {ECO:0000244|PDB:5C33}.
HELIX 700 702 {ECO:0000244|PDB:5C33}.
STRAND 704 706 {ECO:0000244|PDB:5C33}.
HELIX 707 709 {ECO:0000244|PDB:5C33}.
STRAND 710 712 {ECO:0000244|PDB:5C33}.
STRAND 724 727 {ECO:0000244|PDB:5C33}.
STRAND 729 734 {ECO:0000244|PDB:5C33}.
STRAND 737 740 {ECO:0000244|PDB:5C33}.
STRAND 754 760 {ECO:0000244|PDB:5C33}.
TURN 761 764 {ECO:0000244|PDB:5C33}.
STRAND 765 770 {ECO:0000244|PDB:5C33}.
STRAND 788 794 {ECO:0000244|PDB:5C33}.
STRAND 799 803 {ECO:0000244|PDB:5C33}.
HELIX 822 825 {ECO:0000244|PDB:5C33}.
STRAND 833 839 {ECO:0000244|PDB:5C33}.
STRAND 1086 1089 {ECO:0000244|PDB:4P9I}.
HELIX 1092 1094 {ECO:0000244|PDB:4P9I}.
STRAND 1096 1109 {ECO:0000244|PDB:4P9I}.
STRAND 1111 1118 {ECO:0000244|PDB:4P9I}.
STRAND 1130 1138 {ECO:0000244|PDB:4P9I}.
TURN 1139 1142 {ECO:0000244|PDB:4P9I}.
STRAND 1143 1153 {ECO:0000244|PDB:4P9I}.
STRAND 1161 1167 {ECO:0000244|PDB:4P9I}.
TURN 1168 1171 {ECO:0000244|PDB:4P9I}.
STRAND 1172 1177 {ECO:0000244|PDB:4P9I}.
STRAND 1191 1194 {ECO:0000244|PDB:4P9I}.
STRAND 1201 1207 {ECO:0000244|PDB:4P9I}.
STRAND 1213 1216 {ECO:0000244|PDB:4P9I}.
HELIX 1221 1223 {ECO:0000244|PDB:4P9I}.
TURN 1227 1235 {ECO:0000244|PDB:4P9I}.
HELIX 1239 1242 {ECO:0000244|PDB:4P9I}.
HELIX 2714 2716 {ECO:0000244|PDB:4ETV}.
HELIX 2717 2737 {ECO:0000244|PDB:4ETV}.
TURN 2748 2751 {ECO:0000244|PDB:4ETV}.
HELIX 2759 2761 {ECO:0000244|PDB:4ETV}.
HELIX 2764 2783 {ECO:0000244|PDB:4ETV}.
STRAND 2787 2790 {ECO:0000244|PDB:4ETV}.
HELIX 2796 2799 {ECO:0000244|PDB:4ETV}.
HELIX 2817 2819 {ECO:0000244|PDB:4ETV}.
HELIX 2827 2829 {ECO:0000244|PDB:4ETV}.
HELIX 2834 2861 {ECO:0000244|PDB:4ETV}.
HELIX 2873 2875 {ECO:0000244|PDB:4ETV}.
HELIX 2878 2897 {ECO:0000244|PDB:4ETV}.
STRAND 2900 2903 {ECO:0000244|PDB:4ETV}.
SEQUENCE 4966 AA; 564819 MW; F43425091AF7114F CRC64;
MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP
DLSICTFVLE QSLSVRALQE MLANTVEKSE GQVDVEKWKF MMKTAQGGGH RTLLYGHAIL
LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ EDTTGEACWW TIHPASKQRS EGEKVRVGDD
LILVSVSSER YLHLSYGNSS WHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH
MDECLTVPSG EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV
TTGKYLSLME DKNLLLMDKE KADVKSTAFA FRSSKEKLDV GVRKEVDGMG TSEIKYGDSI
CYIQHVDTGL WLTYQAVDVK SARMGSIQRK AIMHHEGHMD DGLNLSRSQH EESRTARVIR
STVFLFNRFI RGLDALSKKV KLPTIDLPIE SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR
ALKNRQNLFQ EEGMINLVLE CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL
IRGNRKNCAQ FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL
LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN HVSSMRPNIF
LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST EGYSPYPGGG EEWGGNGVGD
DLFSYGFDGL HLWSGCIART VSSPNQHLLR TDDVISCCLD LSAPSISFRI NGQPVQGMFE
NFNIDGLFFP VVSFSAGIKV RFLLGGRHGE FKFLPPPGYA ACYEAVLPKE KLKVEHSREY
KQERTYTRDL LGPTVSLTQA AFTPVPVDTS QIVLPPHLER IRERLAENIH ELWVMNKIEL
GWQYGPVRDD NKRQHPCLVE FCKLPEQERN YNLQMSLETL KTLLALGCHV GIADEHAEEK
VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA ENAHNVWARD RIRQGWTYGI
QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL REAVRTLLGY GYHLEAPDQD HASRAEVCSG
TGERFRIFRA EKTYAVKAGR WYFEFEAVTA GDMRVGWSRP GCQPDLELGS DDRAFAFDGF
KAQRWHQGNE HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG
FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW LSKRLPQFLQ
VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNNNTDIM FYRLSMPIEC AEVFSKSVAG
GLPGAGFYGP KNDLEDFDVD SDFEVLMKTA HGHLVPDRID KDKETPKPEF NNHKDYAQEK
PSRLKQRFLL RRTKPDYSTG HSARLTEDVL ADDRDDYEYL MQTSTYYYSV RIFPGQEPAN
VWVGWITSDF HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR
NNSNGLEIGC VVDAASGLLT FIANGKELST YYQVEPSTKL FPAVFAQATS PNVFQFELGR
IKNVMPLSAG LFKSEHKNPV PQCPPRLHVQ FLSHVLWSRM PNQFLKVDVS RISERQGWLV
QCLDPLQFMS LHIPEENRSV DILELTEQEE LLQFHYHTLR LYSAVCALGN HRVAHALCSH
VDEPQLLYAI ENKYMPGLLR AGYYDLLIDI HLSSYATARL MMNNEFIVPM TEETKSITLF
PDENKKHGLP GIGLSTSLRP RMRFSSPSFV SISNDCYQYS PEFPLDILKA KTIQMLTEAV
KEGSLHARDP VGGTTEFLFV PLIKLFYTLL IMGIFHNEDL KHILQLIEPS VFKEAAVPEE
EGGTPEKEIS IEDAKLEGEE EAKGGKRPKE GLLQMKLPEP VKLQMCLLLQ YLCDCQVRHR
IEAIVAFSDD FVAKLQDNQR FRYNEVMQAL NMSAALTARK TREFRSPPQE QINMLLNFKD
DKSECPCPEE IRDQLLDFHE DLMTHCGIEL DEDGSLDGSN DLTIRGRLLS LVEKVTYLKK
KQAEKPVASD SRKCSSLQQL ISETMVRWAQ ESVIEDPELV RAMFVLLHRQ YDGIGGLVRA
LPKTYTINGV SVEDTINLLA SLGQIRSLLS VRMGKEEEKL MIRGLGDIMN NKVFYQHPNL
MRALGMHETV MEVMVNVLGG GESKEITFPK MVANCCRFLC YFCRISRQNQ KAMFDHLSYL
LENSSVGLAS PAMRGSTPLD VAAASVMDNN ELALALREPD LEKVVRYLAG CGLQSCQMLV
SKGYPDIGWN PVEGERYLDF LRFAVFCNGE SVEENANVVV RLLIRRPECF GPALRGEGGN
GLLAAMEEAI KIAEDPSRDG PSPTSGSSKT LDIEEEEDDT IHMGNAIMTF YAALIDLLGR
CAPEMHLIHA GKGEAIRIRS ILRSLIPLGD LVGVISIAFQ MPTIAKDGKV VEPDMSAGFC
PDHKAAMVLF LDRVYGIEVQ DFLLHLLEVG FLPDLRAAAS LDTAALSATD MALALNRYLC
TAVLPLLTRC APLFAGTEHH ASLIDSLLHT VYRLSKGCSL TKAQRDSIEV CLLSICGQLR
PSMMQHLLRR LVFDVPLLNE HAKMPLKLLT NHYERCWKYY CLPGGWGNFG AASEEELHLS
RKLFWGIFDA LSQKKYEQEL FKLALPCLSA VAGALPPDYM ESNYVSMMEK QSSMDSEGNF
NPQPVDTSNI TIPEKLEYFI NKYAEHSHDK WSMDKLANGW IYGEIYSDSS KIQPLMKPYK
LLSEKEKEIY RWPIKESLKT MLAWGWRIER TREGDSMALY NRTRRISQTS QVSIDAAHGY
SPRAIDMSNV TLSRDLHAMA EMMAENYHNI WAKKKKLELE SKGGGNHPLL VPYDTLTAKE
KAKDREKAQD IFKFLQISGY VVSRGFKDLD LDTPSIEKRF AYSFLQQLIR YVDEAHQYIL
EFDGGSRSKG EHFPYEQEIK FFAKVVLPLI DQYFKNHRLY FLSAASRPLC TGGHASNKEK
EMVTSLFCKL GVLVRHRISL FGNDATSIVN CLHILGQTLD ARTVMKTGLD SVKSALRAFL
DNAAEDLEKT MENLKQGQFT HTRSQPKGVT QIINYTTVAL LPMLSSLFEH IGQHQFGEDL
ILEDVQVSCY RILTSLYALG TSKSIYVERQ RSALGECLAA FAGAFPIAFL ETHLDKHNVY
SIYNTRSSRE RAALSLPANV EDVCPNIPSL EKLMTEIIEL AESGIRYTQM PYMMEVVLPM
LCSYMSRWWE HGPENHPERA EMCCTALNSE HMNTLLGNIL KIIYNNLGID EGAWMKRLAV
FSQPIINKVK PQLLKTHFLP LMEKLKKKAA MVVSEEDHLK AEARGDMSEA ELLILDEFTT
LARDLYAFYP LLIRFVDYNR AKWLKEPNPE AEELFRMVAE VFIYWSKSHN FKREEQNFVV
QNEINNMSFL ITDTKSKMSK AAISDQERKK MKRKGDRYSM QTSLIVAALK RLLPIGLNIC
APGDQELIAL AKNRFSLKDT EEEVRDIIRS NIHLQGKLED PAIRWQMALY KDLPNRTEDP
SDPERTVERV LGIANVLFHL EQKSKYTGRG YFSLVEHPQR SKKAVWHKLL SKQRKRAVVA
CFRMAPLYNL PRHRAVNLFL QGYEKSWIET EEHYFEDKLI EDLAKPGAEL PEEDEAMKRV
DPLHQLILLF SRTALTEKCK LEEDFLYMAY ADIMAKSCHD EEDDDGEEEV KSFEEKEMEK
QKLLYQQARL HDRGAAEMVL QTISASKGET GPMVAATLKL GIAILNGGNS TVQQKMLDYL
KEKKDVGFFQ SLAGLMQSCS VLDLNAFERQ NKAEGLGMVT EEGSGEKVLQ DDEFTCDLFR
FLQLLCEGHN SDFQNYLRTQ TGNNTTVNII ISTVDYLLRV QESISDFYWY YSGKDIIDEQ
GQRNFSKAIQ VAKQVFNTLT EYIQGPCTGN QQSLAHSRLW DAVVGFLHVF AHMQMKLSQD
SSQIELLKEL MDLQKDMVVM LLSMLEGNVV NGTIGKQMVD MLVESSNNVE MILKFFDMFL
KLKDLTSSDT FKEYDPDGKG VISKRDFHKA MESHKHYTQS ETEFLLSCAE TDENETLDYE
EFVKRFHEPA KDIGFNVAVL LTNLSEHMPN DTRLQTFLEL AESVLNYFQP FLGRIEIMGS
AKRIERVYFE ISESSRTQWE KPQVKESKRQ FIFDVVNEGG EKEKMELFVN FCEDTIFEMQ
LAAQISESDL NERLANKEES EKERPEEQAP RMGFFSLLTI QSALFALRYN VLTLVRMLSL
KSLKKQMKRM KKMTVKDMVL AFFSSYWSVF VTLLHFVASV CRGFFRIVSS LLLGGSLVEG
AKKIKVAELL ANMPDPTQDE VRGDEEEGER KPLESALPSE DLTDLKELTE ESDLLSDIFG
LDLKREGGQY KLIPHNPNAG LSDLMTNPVP VPEVQEKFQE QKAKEEKEEK EETKSEPEKA
EGEDGEKEEK AKDEKSKQKL RQLHTHRYGE PEVPESAFWK KIIAYQQKLL NYFARNFYNM
RMLALFVAFA INFILLFYKV STSSVVEGKE LPTRTSSDTA KVTNSLDSSP HRIIAVHYVL
EESSGYMEPT LRILAILHTI ISFFCIIGYY CLKVPLVIFK REKEVARKLE FDGLYITEQP
SEDDIKGQWD RLVINTQSFP NNYWDKFVKR KVMDKYGEFY GRDRISELLG MDKAALDFSD
AREKKKPKKD SSLSAVLNSI DVKYQMWKLG VVFTDNSFLY LAWYMTMSVL GHYNNFFFAA
HLLDIAMGFK TLRTILSSVT HNGKQLVLTV GLLAVVVYLY TVVAFNFFRK FYNKSEDGDT
PDMKCDDMLT CYMFHMYVGV RAGGGIGDEI EDPAGDEYEI YRIIFDITFF FFVIVILLAI
IQGLIIDAFG ELRDQQEQVK EDMETKCFIC GIGNDYFDTV PHGFETHTLQ EHNLANYLFF
LMYLINKDET EHTGQESYVW KMYQERCWEF FPAGDCFRKQ YEDQLN


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