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

 RYR2_HUMAN              Reviewed;        4967 AA.
Q92736; Q15411; Q546N8; Q5T3P2;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
30-AUG-2017, entry version 191.
RecName: Full=Ryanodine receptor 2;
Short=RYR-2;
Short=RyR2;
Short=hRYR-2;
AltName: Full=Cardiac muscle ryanodine receptor;
AltName: Full=Cardiac muscle ryanodine receptor-calcium release channel;
AltName: Full=Type 2 ryanodine receptor;
Name=RYR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Heart muscle;
PubMed=8809036; DOI=10.1042/bj3180477;
Tunwell R.E.A., Wickenden C., Bertrand B.M.A., Shevchenko V.I.,
Walsh M.B., Allen P.D., Lai F.A.;
"The human cardiac muscle ryanodine receptor-calcium release channel:
identification, primary structure and topological analysis.";
Biochem. J. 318:477-487(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARVD2 GLN-176;
PRO-433; ILE-2386 AND MET-2504.
PubMed=11159936; DOI=10.1093/hmg/10.3.189;
Tiso N., Stephan D.A., Nava A., Bagattin A., Devaney J.M., Stanchi F.,
Larderet G., Brahmbhatt B., Brown K., Bauce B., Muriago M., Basso C.,
Thiene G., Danieli G.A., Rampazzo A.;
"Identification of mutations in the cardiac ryanodine receptor gene in
families affected with arrhythmogenic right ventricular cardiomyopathy
type 2 (ARVD2).";
Hum. Mol. Genet. 10:189-194(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-87 AND 533-681, DEVELOPMENTAL STAGE,
AND INDUCTION BY TGFB1.
TISSUE=Heart muscle, and Myometrium;
PubMed=9148749; DOI=10.1042/bj3220777;
Awad S.S., Lamb H.K., Morgan J.M., Dunlop W., Gillespie J.I.;
"Differential expression of ryanodine receptor RyR2 mRNA in the non-
pregnant and pregnant human myometrium.";
Biochem. J. 322:777-783(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 4292-4479, AND TISSUE SPECIFICITY.
TISSUE=Cerebellum, and Hippocampus;
PubMed=9607712; DOI=10.1016/S0306-4522(97)00612-X;
Martin C., Chapman K.E., Seckl J.R., Ashley R.H.;
"Partial cloning and differential expression of ryanodine
receptor/calcium-release channel genes in human tissues including the
hippocampus and cerebellum.";
Neuroscience 85:205-216(1998).
[6]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH FKBP1B; PP1; PP2A AKAP6 AND
PKA, INTERACTION WITH FKBP1B; PKA; PP1 AND PP2A, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, MUTAGENESIS OF SER-2808, AND PHOSPHORYLATION AT
SER-2808.
PubMed=10830164; DOI=10.1016/S0092-8674(00)80847-8;
Marx S.O., Reiken S., Hisamatsu Y., Jayaraman T., Burkhoff D.,
Rosemblit N., Marks A.R.;
"PKA phosphorylation dissociates FKBP12.6 from the calcium release
channel (ryanodine receptor): defective regulation in failing
hearts.";
Cell 101:365-376(2000).
[7]
INTERACTION WITH CALM AND S100A1.
PubMed=18650434; DOI=10.1074/jbc.M804432200;
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
Weber D.J.;
"S100A1 and calmodulin compete for the same binding site on ryanodine
receptor.";
J. Biol. Chem. 283:26676-26683(2008).
[8]
FUNCTION, AND PHOSPHORYLATION AT SER-2808 AND SER-2814.
PubMed=20056922; DOI=10.1161/CIRCRESAHA.109.203836;
Neef S., Dybkova N., Sossalla S., Ort K.R., Fluschnik N., Neumann K.,
Seipelt R., Schondube F.A., Hasenfuss G., Maier L.S.;
"CaMKII-dependent diastolic SR Ca2+ leak and elevated diastolic Ca2+
levels in right atrial myocardium of patients with atrial
fibrillation.";
Circ. Res. 106:1134-1144(2010).
[9]
REVIEW.
PubMed=11805843; DOI=10.1038/415198a;
Bers D.M.;
"Cardiac excitation-contraction coupling.";
Nature 415:198-205(2002).
[10]
REVIEW.
PubMed=19482609; DOI=10.2741/3591;
Currie S.;
"Cardiac ryanodine receptor phosphorylation by CaM Kinase II: keeping
the balance right.";
Front. Biosci. 14:5134-5156(2009).
[11]
REVIEW.
PubMed=21472222; DOI=10.3892/mmr_00000240;
Ozawa T.;
"Modulation of ryanodine receptor Ca2+ channels.";
Mol. Med. Report. 3:199-204(2010).
[12]
REVIEW.
PubMed=20961976; DOI=10.1101/cshperspect.a003996;
Lanner J.T., Georgiou D.K., Joshi A.D., Hamilton S.L.;
"Ryanodine receptors: structure, expression, molecular details, and
function in calcium release.";
Cold Spring Harb. Perspect. Biol. 2:E3996-E3996(2010).
[13] {ECO:0000244|PDB:4JKQ}
X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 1-606, AND CHARACTERIZATION
OF VARIANT CPVT1 PHE-419.
PubMed=25372681; DOI=10.1107/S1399004714020343;
Borko L., Bauerova-Hlinkova V., Hostinova E., Gasperik J., Beck K.,
Lai F.A., Zahradnikova A., Sevcik J.;
"Structural insights into the human RyR2 N-terminal region involved in
cardiac arrhythmias.";
Acta Crystallogr. D 70:2897-2912(2014).
[14]
VARIANTS VTSIP LEU-2246; SER-2474; LYS-4104 AND CYS-4497.
PubMed=11208676; DOI=10.1161/01.CIR.103.2.196;
Priori S.G., Napolitano C., Tiso N., Memmi M., Vignati G., Bloise R.,
Sorrentino V.V., Danieli G.A.;
"Mutations in the cardiac ryanodine receptor gene (hRyR2) underlie
catecholaminergic polymorphic ventricular tachycardia.";
Circulation 103:196-200(2001).
[15]
VARIANTS CPVT1 SER-2328; ARG-4201 AND PHE-4653, AND VARIANT ARG-2958.
PubMed=11157710; DOI=10.1161/01.CIR.103.4.485;
Laitinen P.J., Brown K.M., Piippo K., Swan H., Devaney J.M.,
Brahmbhatt B., Donarum E.A., Marino M., Tiso N., Viitasalo M.,
Toivonen L., Stephan D.A., Kontula K.;
"Mutations of the cardiac ryanodine receptor (RyR2) gene in familial
polymorphic ventricular tachycardia.";
Circulation 103:485-490(2001).
[16]
VARIANTS CPVT1 LEU-2246; ASP-2311; SER-2474; PHE-3778; SER-3946;
SER-3946; LYS-4104; CYS-4497; ILE-4771; GLY-4860; MET-4867; ASP-4895
AND LYS-4950.
PubMed=12093772; DOI=10.1161/01.CIR.0000020013.73106.D8;
Priori S.G., Napolitano C., Memmi M., Colombi B., Drago F.,
Gasparini M., DeSimone L., Coltorti F., Bloise R., Keegan R.,
Cruz Filho F.E.S., Vignati G., Benatar A., DeLogu A.;
"Clinical and molecular characterization of patients with
catecholaminergic polymorphic ventricular tachycardia.";
Circulation 106:69-74(2002).
[17]
VARIANTS CPVT1 GLN-176; TRP-420; PRO-433; ILE-2386; CYS-2392 AND
MET-2504.
PubMed=12106942; DOI=10.1016/S0735-1097(02)01946-0;
Bauce B., Rampazzo A., Basso C., Bagattin A., Daliento L., Tiso N.,
Turrini P., Thiene G., Danieli G.A., Nava A.;
"Screening for ryanodine receptor type 2 mutations in families with
effort-induced polymorphic ventricular arrhythmias and sudden death:
early diagnosis of asymptomatic carriers.";
J. Am. Coll. Cardiol. 40:341-349(2002).
[18]
VARIANTS VTSIP ILE-2306; LEU-4902 AND GLN-4959.
PubMed=14571276; DOI=10.1038/sj.ejhg.5201061;
Laitinen P.J., Swan H., Kontula K.;
"Molecular genetics of exercise-induced polymorphic ventricular
tachycardia: identification of three novel cardiac ryanodine receptor
mutations and two common calsequestrin 2 amino-acid polymorphisms.";
Eur. J. Hum. Genet. 11:888-891(2003).
[19]
VARIANTS CPVT1 SER-164; LEU-414; PHE-419; THR-2403; CYS-4499;
THR-4510; ARG-4671 AND VAL-4848.
PubMed=15466642; DOI=10.1161/01.CIR.0000144471.98080.CA;
Choi G., Kopplin L.J., Tester D.J., Will M.L., Haglund C.M.,
Ackerman M.J.;
"Spectrum and frequency of cardiac channel defects in swimming-
triggered arrhythmia syndromes.";
Circulation 110:2119-2124(2004).
[20]
VARIANTS CPVT1 ILE-4504 AND ALA-4880.
PubMed=15046072;
Bagattin A., Veronese C., Rampazzo A., Danieli G.A.;
"Gene symbol: RYR2. Disease: effort-induced polymorphic ventricular
arrhythmias.";
Hum. Genet. 114:404-404(2004).
[21]
VARIANTS CPVT1 PRO-2387 AND PRO-4607.
PubMed=15046073;
Bagattin A., Veronese C., Rampazzo A., Danieli G.A.;
"Gene symbol: RYR2. Disease: effort-induced polymorphic ventricular
arrhythmias.";
Hum. Genet. 114:405-405(2004).
[22]
VARIANTS CPVT1 TRP-420; LEU-2246; SER-4097; LYS-4146; PRO-4158 AND
CYS-4497.
PubMed=15544015; DOI=10.4065/79.11.1380;
Tester D.J., Spoon D.B., Valdivia H.H., Makielski J.C., Ackerman M.J.;
"Targeted mutational analysis of the RyR2-encoded cardiac ryanodine
receptor in sudden unexplained death: a molecular autopsy of 49
medical examiner/coroner's cases.";
Mayo Clin. Proc. 79:1380-1384(2004).
[23]
VARIANT GLU-4955.
PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C.,
Patry L., Massicotte C., Ambalavanan A., Spiegelman D., Diallo O.,
Henrion E., Dionne-Laporte A., Fougerat A., Pshezhetsky A.V.,
Venkateswaran S., Rouleau G.A., Michaud J.L.;
"De novo mutations in moderate or severe intellectual disability.";
PLoS Genet. 10:E1004772-E1004772(2014).
[24]
CHARACTERIZATION OF VARIANT CPVT1 GLY-4860.
PubMed=17984046; DOI=10.1073/pnas.0706573104;
Jiang D., Chen W., Wang R., Zhang L., Chen S.R.W.;
"Loss of luminal Ca(2+) activation in the cardiac ryanodine receptor
is associated with ventricular fibrillation and sudden death.";
Proc. Natl. Acad. Sci. U.S.A. 104:18309-18314(2007).
[25]
VARIANT ASP-29.
PubMed=25463374; DOI=10.1016/j.ijcard.2014.11.119;
Cheung J.W., Meli A.C., Xie W., Mittal S., Reiken S., Wronska A.,
Xu L., Steinberg J.S., Markowitz S.M., Iwai S., Lacampagne A.,
Lerman B.B., Marks A.R.;
"Short-coupled polymorphic ventricular tachycardia at rest linked to a
novel ryanodine receptor (RyR2) mutation: leaky RyR2 channels under
non-stress conditions.";
Int. J. Cardiol. 180:228-236(2015).
[26]
CHARACTERIZATION OF VARIANT ASP-29.
PubMed=26405799; DOI=10.1371/journal.pone.0139058;
Xiao Z., Guo W., Yuen S.M., Wang R., Zhang L., Van Petegem F.,
Chen S.R.;
"The H29D nutation does not enhance cytosolic Ca2+ activation of the
cardiac ryanodine receptor.";
PLoS ONE 10:E0139058-E0139058(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:10830164, ECO:0000269|PubMed:20056922}.
-!- SUBUNIT: Homotetramer. Can also form heterotetramers with RYR1 and
RYR3 (By similarity). Interacts with FKBP1A and FKBP1B; these
interactions may stabilize the channel in its closed state and
prevent Ca(2+) leaks. 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. Interacts with SELENON (By similarity).
{ECO:0000250|UniProtKB:P30957, ECO:0000269|PubMed:10830164,
ECO:0000269|PubMed:18650434}.
-!- INTERACTION:
P62942:FKBP1A; NbExp=2; IntAct=EBI-1170425, EBI-1027571;
P68106:FKBP1B; NbExp=5; IntAct=EBI-1170425, EBI-6693977;
Q00987:MDM2; NbExp=2; IntAct=EBI-1170425, EBI-389668;
-!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
{ECO:0000269|PubMed:10830164}; Multi-pass membrane protein
{ECO:0000269|PubMed:10830164}. Membrane
{ECO:0000305|PubMed:10830164}; Multi-pass membrane protein
{ECO:0000305|PubMed:10830164}. 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q92736-1; Sequence=Displayed;
Name=2;
IsoId=Q92736-2; Sequence=VSP_005953;
-!- TISSUE SPECIFICITY: Detected in heart muscle (at protein level).
Heart muscle, brain (cerebellum and hippocampus) and placenta.
{ECO:0000269|PubMed:10830164, ECO:0000269|PubMed:9607712}.
-!- DEVELOPMENTAL STAGE: Expressed in myometrium during pregnancy.
{ECO:0000269|PubMed:9148749}.
-!- INDUCTION: By TGFB1. {ECO:0000269|PubMed:9148749}.
-!- 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-2808 and Ser-2814 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:10830164,
ECO:0000269|PubMed:20056922}.
-!- PTM: Phosphorylation at Ser-2031 by PKA enhances the response to
lumenal calcium. {ECO:0000250}.
-!- DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 2
(ARVD2) [MIM:600996]: A congenital heart disease characterized by
infiltration of adipose and fibrous tissue into the right
ventricle and loss of myocardial cells, resulting in ventricular
and supraventricular arrhythmias. {ECO:0000269|PubMed:11159936}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Ventricular tachycardia, catecholaminergic polymorphic,
1, with or without atrial dysfunction and/or dilated
cardiomyopathy (CPVT1) [MIM:604772]: An arrhythmogenic disorder
characterized by stress-induced, bidirectional ventricular
tachycardia that may degenerate into cardiac arrest and cause
sudden death. Patients present with recurrent syncope, seizures,
or sudden death after physical activity or emotional stress. CPVT1
inheritance is autosomal dominant. {ECO:0000269|PubMed:11157710,
ECO:0000269|PubMed:12093772, ECO:0000269|PubMed:12106942,
ECO:0000269|PubMed:15046072, ECO:0000269|PubMed:15046073,
ECO:0000269|PubMed:15466642, ECO:0000269|PubMed:15544015,
ECO:0000269|PubMed:17984046, ECO:0000269|PubMed:25372681}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- 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). {ECO:0000250}.
-!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family.
RYR2 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAH71369.1; Type=Miscellaneous discrepancy; Note=Erroneous gene model prediction.; Evidence={ECO:0000305};
Sequence=CAH71393.1; Type=Miscellaneous discrepancy; Note=Erroneous gene model prediction.; Evidence={ECO:0000305};
Sequence=CAH73918.1; Type=Miscellaneous discrepancy; Note=Erroneous gene model prediction.; Evidence={ECO:0000305};
Sequence=CAI14440.1; Type=Miscellaneous discrepancy; Note=Erroneous gene model prediction.; Evidence={ECO:0000305};
Sequence=CAI15350.1; Type=Miscellaneous discrepancy; Note=Erroneous gene model prediction.; Evidence={ECO:0000305};
Sequence=CAI15936.1; Type=Miscellaneous discrepancy; Note=Erroneous gene model prediction.; Evidence={ECO:0000305};
Sequence=CAI22065.1; Type=Miscellaneous discrepancy; Note=Erroneous gene model prediction.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Ryanodine receptor entry;
URL="https://en.wikipedia.org/wiki/Ryanodine_receptor";
-!- WEB RESOURCE: Name=Wikipedia; Note=RYR2 entry;
URL="https://en.wikipedia.org/wiki/RYR2";
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EMBL; X98330; CAA66975.1; -; mRNA.
EMBL; AJ300340; CAC18855.1; -; Genomic_DNA.
EMBL; AJ300341; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300342; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300343; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300347; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300349; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300351; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300353; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300355; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300364; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300363; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300362; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300361; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300360; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300359; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300358; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300357; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300356; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300373; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300372; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300371; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300370; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300369; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300368; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300367; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300366; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300365; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300382; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300381; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300380; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300379; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300378; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300377; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300376; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300375; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300374; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300399; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300398; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300397; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300396; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300395; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300394; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300393; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300392; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300391; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300416; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300415; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300414; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300413; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300412; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300411; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300410; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300409; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300408; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300433; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300432; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300431; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300430; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300429; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300428; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300427; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300426; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300425; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300444; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300443; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300442; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300441; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300440; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300439; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300438; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300437; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300436; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300435; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300434; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300424; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300423; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300422; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300421; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300420; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300419; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300418; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300417; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300407; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300406; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300405; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300404; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300403; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300402; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300401; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300400; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300390; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300389; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300388; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300387; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300386; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300385; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300384; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300383; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300354; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300352; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300350; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300348; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300346; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300345; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AJ300344; CAC18855.1; JOINED; Genomic_DNA.
EMBL; AL365332; CAH71369.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356773; CAH71369.1; JOINED; Genomic_DNA.
EMBL; AL359924; CAH71369.1; JOINED; Genomic_DNA.
EMBL; AL391809; CAH71369.1; JOINED; Genomic_DNA.
EMBL; AL442065; CAH71369.1; JOINED; Genomic_DNA.
EMBL; AL445473; CAH71369.1; JOINED; Genomic_DNA.
EMBL; AL513130; CAH71369.1; JOINED; Genomic_DNA.
EMBL; AL445473; CAH71393.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356773; CAH71393.1; JOINED; Genomic_DNA.
EMBL; AL359924; CAH71393.1; JOINED; Genomic_DNA.
EMBL; AL365332; CAH71393.1; JOINED; Genomic_DNA.
EMBL; AL391809; CAH71393.1; JOINED; Genomic_DNA.
EMBL; AL442065; CAH71393.1; JOINED; Genomic_DNA.
EMBL; AL513130; CAH71393.1; JOINED; Genomic_DNA.
EMBL; AL356773; CAH73918.1; ALT_SEQ; Genomic_DNA.
EMBL; AL359924; CAH73918.1; JOINED; Genomic_DNA.
EMBL; AL365332; CAH73918.1; JOINED; Genomic_DNA.
EMBL; AL391809; CAH73918.1; JOINED; Genomic_DNA.
EMBL; AL442065; CAH73918.1; JOINED; Genomic_DNA.
EMBL; AL445473; CAH73918.1; JOINED; Genomic_DNA.
EMBL; AL513130; CAH73918.1; JOINED; Genomic_DNA.
EMBL; AL391809; CAI14440.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356773; CAI14440.1; JOINED; Genomic_DNA.
EMBL; AL359924; CAI14440.1; JOINED; Genomic_DNA.
EMBL; AL365332; CAI14440.1; JOINED; Genomic_DNA.
EMBL; AL442065; CAI14440.1; JOINED; Genomic_DNA.
EMBL; AL445473; CAI14440.1; JOINED; Genomic_DNA.
EMBL; AL513130; CAI14440.1; JOINED; Genomic_DNA.
EMBL; AL442065; CAI15350.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356773; CAI15350.1; JOINED; Genomic_DNA.
EMBL; AL359924; CAI15350.1; JOINED; Genomic_DNA.
EMBL; AL365332; CAI15350.1; JOINED; Genomic_DNA.
EMBL; AL391809; CAI15350.1; JOINED; Genomic_DNA.
EMBL; AL445473; CAI15350.1; JOINED; Genomic_DNA.
EMBL; AL513130; CAI15350.1; JOINED; Genomic_DNA.
EMBL; AL513130; CAI15936.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356773; CAI15936.1; JOINED; Genomic_DNA.
EMBL; AL359924; CAI15936.1; JOINED; Genomic_DNA.
EMBL; AL365332; CAI15936.1; JOINED; Genomic_DNA.
EMBL; AL391809; CAI15936.1; JOINED; Genomic_DNA.
EMBL; AL442065; CAI15936.1; JOINED; Genomic_DNA.
EMBL; AL445473; CAI15936.1; JOINED; Genomic_DNA.
EMBL; AL359924; CAI22065.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356773; CAI22065.1; JOINED; Genomic_DNA.
EMBL; AL365332; CAI22065.1; JOINED; Genomic_DNA.
EMBL; AL391809; CAI22065.1; JOINED; Genomic_DNA.
EMBL; AL442065; CAI22065.1; JOINED; Genomic_DNA.
EMBL; AL445473; CAI22065.1; JOINED; Genomic_DNA.
EMBL; AL513130; CAI22065.1; JOINED; Genomic_DNA.
EMBL; Y08218; CAA69395.1; -; mRNA.
EMBL; X91869; CAA62975.1; -; mRNA.
EMBL; AJ002511; CAA05502.1; -; mRNA.
CCDS; CCDS55691.1; -. [Q92736-1]
PIR; S72269; S72269.
RefSeq; NP_001026.2; NM_001035.2. [Q92736-1]
RefSeq; XP_006711868.1; XM_006711805.3. [Q92736-2]
UniGene; Hs.109514; -.
UniGene; Hs.738571; -.
PDB; 4JKQ; X-ray; 2.39 A; A=1-606.
PDBsum; 4JKQ; -.
ProteinModelPortal; Q92736; -.
SMR; Q92736; -.
BioGrid; 112174; 25.
DIP; DIP-38325N; -.
IntAct; Q92736; 10.
MINT; MINT-1201008; -.
STRING; 9606.ENSP00000355533; -.
ChEMBL; CHEMBL4403; -.
DrugBank; DB09085; Tetracaine.
GuidetoPHARMACOLOGY; 748; -.
TCDB; 1.A.3.1.1; the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.
iPTMnet; Q92736; -.
PhosphoSitePlus; Q92736; -.
BioMuta; RYR2; -.
DMDM; 308153558; -.
EPD; Q92736; -.
MaxQB; Q92736; -.
PaxDb; Q92736; -.
PeptideAtlas; Q92736; -.
PRIDE; Q92736; -.
Ensembl; ENST00000366574; ENSP00000355533; ENSG00000198626. [Q92736-1]
GeneID; 6262; -.
KEGG; hsa:6262; -.
UCSC; uc001hyl.2; human. [Q92736-1]
CTD; 6262; -.
DisGeNET; 6262; -.
GeneCards; RYR2; -.
GeneReviews; RYR2; -.
HGNC; HGNC:10484; RYR2.
HPA; HPA020028; -.
MalaCards; RYR2; -.
MIM; 180902; gene.
MIM; 600996; phenotype.
MIM; 604772; phenotype.
neXtProt; NX_Q92736; -.
OpenTargets; ENSG00000198626; -.
Orphanet; 3286; Catecholaminergic polymorphic ventricular tachycardia.
Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
eggNOG; KOG2243; Eukaryota.
eggNOG; ENOG410YCNW; LUCA.
GeneTree; ENSGT00760000119152; -.
HOGENOM; HOG000231428; -.
HOVERGEN; HBG006699; -.
InParanoid; Q92736; -.
KO; K04962; -.
OMA; EHMPNDT; -.
OrthoDB; EOG091G00T0; -.
PhylomeDB; Q92736; -.
TreeFam; TF315244; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-5578775; Ion homeostasis.
SIGNOR; Q92736; -.
ChiTaRS; RYR2; human.
GeneWiki; Ryanodine_receptor_2; -.
GenomeRNAi; 6262; -.
PRO; PR:Q92736; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000198626; -.
CleanEx; HS_RYR2; -.
ExpressionAtlas; Q92736; baseline and differential.
Genevisible; Q92736; HS.
GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; TAS:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:BHF-UCL.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
GO; GO:0048763; F:calcium-induced calcium release activity; IDA:BHF-UCL.
GO; GO:0015278; F:calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IMP:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; IDA:BHF-UCL.
GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:BHF-UCL.
GO; GO:0043621; F:protein self-association; IEA:Ensembl.
GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0043924; F:suramin binding; IMP:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
GO; GO:0006816; P:calcium ion transport; IDA:BHF-UCL.
GO; GO:0060402; P:calcium ion transport into cytosol; IDA:BHF-UCL.
GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IDA:BHF-UCL.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0003300; P:cardiac muscle hypertrophy; ISS:BHF-UCL.
GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; IC:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0071313; P:cellular response to caffeine; IDA:BHF-UCL.
GO; GO:0071872; P:cellular response to epinephrine stimulus; ISS:BHF-UCL.
GO; GO:0005513; P:detection of calcium ion; IDA:BHF-UCL.
GO; GO:0003143; P:embryonic heart tube morphogenesis; ISS:UniProtKB.
GO; GO:0072599; P:establishment of protein localization to endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0003220; P:left ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
GO; GO:1901896; P:positive regulation of calcium-transporting ATPase activity; IDA:BHF-UCL.
GO; GO:0010460; P:positive regulation of heart rate; ISS:BHF-UCL.
GO; GO:0051284; P:positive regulation of sequestering of calcium ion; IDA:BHF-UCL.
GO; GO:0098735; P:positive regulation of the force of heart contraction; IMP:BHF-UCL.
GO; GO:0086029; P:Purkinje myocyte to ventricular cardiac muscle cell signaling; ISS:BHF-UCL.
GO; GO:0098910; P:regulation of atrial cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0098904; P:regulation of AV node cell action potential; IMP:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:BHF-UCL.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISS:BHF-UCL.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
GO; GO:0098907; P:regulation of SA node cell action potential; IMP:BHF-UCL.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:BHF-UCL.
GO; GO:0031000; P:response to caffeine; IDA:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; ISS:BHF-UCL.
GO; GO:0014850; P:response to muscle activity; IMP:BHF-UCL.
GO; GO:0035994; P:response to muscle stretch; IMP:BHF-UCL.
GO; GO:0051775; P:response to redox state; IDA:BHF-UCL.
GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; TAS:BHF-UCL.
GO; GO:0097050; P:type B pancreatic cell apoptotic process; IMP:BHF-UCL.
GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISS:BHF-UCL.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR014821; Ins145_P3_rcpt.
InterPro; IPR005821; Ion_trans_dom.
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; 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; Alternative splicing; Calcium; Calcium channel;
Calcium transport; Calmodulin-binding; Cardiomyopathy; Coiled coil;
Complete proteome; Developmental protein; Disease mutation;
Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 4967 Ryanodine receptor 2.
/FTId=PRO_0000219361.
TOPO_DOM 1 4281 Cytoplasmic. {ECO:0000255}.
TRANSMEM 4282 4302 Helical. {ECO:0000255}.
TRANSMEM 4504 4524 Helical. {ECO:0000255}.
TRANSMEM 4580 4600 Helical. {ECO:0000255}.
TRANSMEM 4730 4750 Helical. {ECO:0000255}.
TRANSMEM 4769 4789 Helical. {ECO:0000255}.
INTRAMEM 4820 4829 Pore-forming. {ECO:0000250}.
TRANSMEM 4850 4870 Helical. {ECO:0000255}.
TOPO_DOM 4871 4967 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 1337 1562 B30.2/SPRY 3. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
REPEAT 2692 2810 3.
REPEAT 2812 2925 4.
REGION 853 2925 4 X approximate repeats.
REGION 3581 3610 Interaction with CALM.
{ECO:0000269|PubMed:18650434}.
COILED 4412 4445 {ECO:0000255}.
COMPBIAS 4414 4455 Glu-rich (acidic).
MOD_RES 1341 1341 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q401}.
MOD_RES 1869 1869 Phosphoserine.
{ECO:0000250|UniProtKB:B0LPN4}.
MOD_RES 2031 2031 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:E9Q401}.
MOD_RES 2369 2369 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q401}.
MOD_RES 2697 2697 Phosphoserine.
{ECO:0000250|UniProtKB:B0LPN4}.
MOD_RES 2797 2797 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q401}.
MOD_RES 2808 2808 Phosphoserine; by CaMK2D and PKA.
{ECO:0000269|PubMed:10830164,
ECO:0000269|PubMed:20056922}.
MOD_RES 2811 2811 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q401}.
MOD_RES 2814 2814 Phosphoserine; by CaMK2D.
{ECO:0000269|PubMed:20056922}.
MOD_RES 2947 2947 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q401}.
VAR_SEQ 3715 3715 E -> EVTGSQRSK (in isoform 2).
{ECO:0000305}.
/FTId=VSP_005953.
VARIANT 29 29 H -> D (found in a patient with short-
coupled polymorphic ventricular
tachycardia at rest; unknown pathological
significance; no effect on cytosolic
Ca(2+) activation).
{ECO:0000269|PubMed:25463374,
ECO:0000269|PubMed:26405799}.
/FTId=VAR_075283.
VARIANT 164 164 P -> S (in CPVT1).
{ECO:0000269|PubMed:15466642}.
/FTId=VAR_044086.
VARIANT 176 176 R -> Q (in ARVD2 and CPVT1;
dbSNP:rs794728708).
{ECO:0000269|PubMed:11159936,
ECO:0000269|PubMed:12106942}.
/FTId=VAR_044087.
VARIANT 414 414 R -> L (in CPVT1).
{ECO:0000269|PubMed:15466642}.
/FTId=VAR_044088.
VARIANT 419 419 I -> F (in CPVT1; decreases protein
stability). {ECO:0000269|PubMed:15466642,
ECO:0000269|PubMed:25372681}.
/FTId=VAR_044089.
VARIANT 420 420 R -> W (in CPVT1; dbSNP:rs190140598).
{ECO:0000269|PubMed:12106942,
ECO:0000269|PubMed:15544015}.
/FTId=VAR_044090.
VARIANT 433 433 L -> P (in ARVD2 and CPVT1;
dbSNP:rs121918602).
{ECO:0000269|PubMed:11159936,
ECO:0000269|PubMed:12106942}.
/FTId=VAR_011395.
VARIANT 507 507 V -> I (in dbSNP:rs16835270).
/FTId=VAR_044091.
VARIANT 1886 1886 G -> S (in dbSNP:rs3766871).
/FTId=VAR_022078.
VARIANT 2246 2246 S -> L (in CPVT1; dbSNP:rs121918597).
{ECO:0000269|PubMed:11208676,
ECO:0000269|PubMed:12093772,
ECO:0000269|PubMed:15544015}.
/FTId=VAR_011396.
VARIANT 2306 2306 V -> I (in CPVT1; dbSNP:rs794728746).
{ECO:0000269|PubMed:14571276}.
/FTId=VAR_023694.
VARIANT 2311 2311 E -> D (in CPVT1; dbSNP:rs794728747).
{ECO:0000269|PubMed:12093772}.
/FTId=VAR_044092.
VARIANT 2328 2328 P -> S (in CPVT1; dbSNP:rs121918603).
{ECO:0000269|PubMed:11157710}.
/FTId=VAR_011397.
VARIANT 2386 2386 N -> I (in ARVD2 and CPVT1;
dbSNP:rs121918601).
{ECO:0000269|PubMed:11159936,
ECO:0000269|PubMed:12106942}.
/FTId=VAR_011398.
VARIANT 2387 2387 A -> P (in CPVT1).
{ECO:0000269|PubMed:15046073}.
/FTId=VAR_044093.
VARIANT 2392 2392 Y -> C (in CPVT1; dbSNP:rs772220753).
{ECO:0000269|PubMed:12106942}.
/FTId=VAR_044094.
VARIANT 2403 2403 A -> T (in CPVT1).
{ECO:0000269|PubMed:15466642}.
/FTId=VAR_044095.
VARIANT 2474 2474 R -> S (in CPVT1; dbSNP:rs121918598).
{ECO:0000269|PubMed:11208676,
ECO:0000269|PubMed:12093772}.
/FTId=VAR_011399.
VARIANT 2504 2504 T -> M (in ARVD2 and CPVT1;
dbSNP:rs769219555).
{ECO:0000269|PubMed:11159936,
ECO:0000269|PubMed:12106942}.
/FTId=VAR_044096.
VARIANT 2958 2958 Q -> R (in dbSNP:rs34967813).
{ECO:0000269|PubMed:11157710}.
/FTId=VAR_011590.
VARIANT 3778 3778 L -> F (in CPVT1).
{ECO:0000269|PubMed:12093772}.
/FTId=VAR_044097.
VARIANT 3946 3946 G -> S (in CPVT1; dbSNP:rs794728777).
{ECO:0000269|PubMed:12093772}.
/FTId=VAR_044098.
VARIANT 4097 4097 N -> S (in CPVT1; dbSNP:rs794728784).
{ECO:0000269|PubMed:15544015}.
/FTId=VAR_044099.
VARIANT 4104 4104 N -> K (in CPVT1; dbSNP:rs121918599).
{ECO:0000269|PubMed:11208676,
ECO:0000269|PubMed:12093772}.
/FTId=VAR_011400.
VARIANT 4146 4146 E -> K (in CPVT1).
{ECO:0000269|PubMed:15544015}.
/FTId=VAR_044100.
VARIANT 4158 4158 T -> P (in CPVT1).
{ECO:0000269|PubMed:15544015}.
/FTId=VAR_044101.
VARIANT 4201 4201 Q -> R (in CPVT1; dbSNP:rs121918605).
{ECO:0000269|PubMed:11157710}.
/FTId=VAR_011401.
VARIANT 4497 4497 R -> C (in CPVT1; dbSNP:rs121918600).
{ECO:0000269|PubMed:11208676,
ECO:0000269|PubMed:12093772,
ECO:0000269|PubMed:15544015}.
/FTId=VAR_011402.
VARIANT 4499 4499 F -> C (in CPVT1).
{ECO:0000269|PubMed:15466642}.
/FTId=VAR_044102.
VARIANT 4504 4504 M -> I (in CPVT1).
{ECO:0000269|PubMed:15046072}.
/FTId=VAR_044103.
VARIANT 4510 4510 A -> T (in CPVT1; dbSNP:rs397516510).
{ECO:0000269|PubMed:15466642}.
/FTId=VAR_044104.
VARIANT 4607 4607 A -> P (in CPVT1).
{ECO:0000269|PubMed:15046073}.
/FTId=VAR_044105.
VARIANT 4653 4653 V -> F (in CPVT1; dbSNP:rs121918604).
{ECO:0000269|PubMed:11157710}.
/FTId=VAR_011403.
VARIANT 4671 4671 G -> R (in CPVT1).
{ECO:0000269|PubMed:15466642}.
/FTId=VAR_044106.
VARIANT 4771 4771 V -> I (in CPVT1; dbSNP:rs794728804).
{ECO:0000269|PubMed:12093772}.
/FTId=VAR_044107.
VARIANT 4848 4848 I -> V (in CPVT1).
{ECO:0000269|PubMed:15466642}.
/FTId=VAR_044108.
VARIANT 4860 4860 A -> G (in CPVT1; diminishes the response
to activation by luminal Ca(2+) but has
little effect on the sensitivity of the
channel to activation by cytosolic
Ca(2+); shows caffeine-induced Ca(2+)
release but exhibits no store-overload-
induced Ca(2+) release (SOICR); HL1
cardiac cells transfected with the G-4860
mutant displayed attenuated SOICR
activity compared to cells transfected
with wild-type RYR2; dbSNP:rs121918606).
{ECO:0000269|PubMed:12093772,
ECO:0000269|PubMed:17984046}.
/FTId=VAR_044109.
VARIANT 4867 4867 I -> M (in CPVT1).
{ECO:0000269|PubMed:12093772}.
/FTId=VAR_044110.
VARIANT 4880 4880 V -> A (in CPVT1).
{ECO:0000269|PubMed:15046072}.
/FTId=VAR_044111.
VARIANT 4895 4895 N -> D (in CPVT1).
{ECO:0000269|PubMed:12093772}.
/FTId=VAR_044112.
VARIANT 4902 4902 P -> L (in CPVT1).
{ECO:0000269|PubMed:14571276}.
/FTId=VAR_023695.
VARIANT 4950 4950 E -> K (in CPVT1).
{ECO:0000269|PubMed:12093772}.
/FTId=VAR_044113.
VARIANT 4955 4955 G -> E (probable disease-associated
mutation found in a patient with
intellectual disability, seizures, short
stature and severe atrial arrhythmias).
{ECO:0000269|PubMed:25356899}.
/FTId=VAR_078648.
VARIANT 4959 4959 R -> Q (in CPVT1; dbSNP:rs794728811).
{ECO:0000269|PubMed:14571276}.
/FTId=VAR_023696.
MUTAGEN 2808 2808 S->A: Abolishes phosphorylation by PKA.
{ECO:0000269|PubMed:10830164}.
CONFLICT 1037 1037 L -> P (in Ref. 1; CAA66975 and 2;
CAC18855). {ECO:0000305}.
CONFLICT 2785 2789 WGWRI -> RTMRT (in Ref. 1; CAA66975 and
2; CAC18855). {ECO:0000305}.
STRAND 19 28 {ECO:0000244|PDB:4JKQ}.
STRAND 31 38 {ECO:0000244|PDB:4JKQ}.
STRAND 48 51 {ECO:0000244|PDB:4JKQ}.
TURN 53 57 {ECO:0000244|PDB:4JKQ}.
HELIX 63 65 {ECO:0000244|PDB:4JKQ}.
STRAND 67 73 {ECO:0000244|PDB:4JKQ}.
TURN 108 110 {ECO:0000244|PDB:4JKQ}.
STRAND 118 127 {ECO:0000244|PDB:4JKQ}.
STRAND 129 132 {ECO:0000244|PDB:4JKQ}.
TURN 139 141 {ECO:0000244|PDB:4JKQ}.
STRAND 145 151 {ECO:0000244|PDB:4JKQ}.
STRAND 159 166 {ECO:0000244|PDB:4JKQ}.
STRAND 180 185 {ECO:0000244|PDB:4JKQ}.
TURN 186 188 {ECO:0000244|PDB:4JKQ}.
STRAND 191 196 {ECO:0000244|PDB:4JKQ}.
STRAND 198 208 {ECO:0000244|PDB:4JKQ}.
STRAND 212 218 {ECO:0000244|PDB:4JKQ}.
STRAND 233 238 {ECO:0000244|PDB:4JKQ}.
TURN 239 242 {ECO:0000244|PDB:4JKQ}.
STRAND 243 246 {ECO:0000244|PDB:4JKQ}.
STRAND 250 252 {ECO:0000244|PDB:4JKQ}.
HELIX 256 258 {ECO:0000244|PDB:4JKQ}.
STRAND 261 263 {ECO:0000244|PDB:4JKQ}.
HELIX 265 269 {ECO:0000244|PDB:4JKQ}.
HELIX 271 273 {ECO:0000244|PDB:4JKQ}.
STRAND 275 280 {ECO:0000244|PDB:4JKQ}.
TURN 283 286 {ECO:0000244|PDB:4JKQ}.
STRAND 295 299 {ECO:0000244|PDB:4JKQ}.
TURN 300 302 {ECO:0000244|PDB:4JKQ}.
STRAND 305 308 {ECO:0000244|PDB:4JKQ}.
STRAND 310 312 {ECO:0000244|PDB:4JKQ}.
STRAND 314 317 {ECO:0000244|PDB:4JKQ}.
HELIX 319 321 {ECO:0000244|PDB:4JKQ}.
HELIX 324 327 {ECO:0000244|PDB:4JKQ}.
STRAND 329 336 {ECO:0000244|PDB:4JKQ}.
STRAND 340 342 {ECO:0000244|PDB:4JKQ}.
TURN 356 358 {ECO:0000244|PDB:4JKQ}.
STRAND 360 365 {ECO:0000244|PDB:4JKQ}.
TURN 366 368 {ECO:0000244|PDB:4JKQ}.
STRAND 371 375 {ECO:0000244|PDB:4JKQ}.
STRAND 388 396 {ECO:0000244|PDB:4JKQ}.
STRAND 403 407 {ECO:0000244|PDB:4JKQ}.
HELIX 410 437 {ECO:0000244|PDB:4JKQ}.
HELIX 442 444 {ECO:0000244|PDB:4JKQ}.
HELIX 449 462 {ECO:0000244|PDB:4JKQ}.
HELIX 472 491 {ECO:0000244|PDB:4JKQ}.
HELIX 494 506 {ECO:0000244|PDB:4JKQ}.
STRAND 508 510 {ECO:0000244|PDB:4JKQ}.
HELIX 511 518 {ECO:0000244|PDB:4JKQ}.
HELIX 520 541 {ECO:0000244|PDB:4JKQ}.
SEQUENCE 4967 AA; 564567 MW; 44984485F8677B42 CRC64;
MADGGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP
DLSICTFVLE QSLSVRALQE MLANTVEKSE GQVDVEKWKF MMKTAQGGGH RTLLYGHAIL
LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ EDTTGEACWW TIHPASKQRS EGEKVRVGDD
LILVSVSSER YLHLSYGNGS LHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH
MDECLTVPSG EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV
TTGKYLSLME DKNLLLMDKE KADVKSTAFT FRSSKEKLDV GVRKEVDGMG TSEIKYGDSV
CYIQHVDTGL WLTYQSVDVK SVRMGSIQRK AIMHHEGHMD DGISLSRSQH EESRTARVIR
STVFLFNRFI RGLDALSKKA KASTVDLPIE 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 PCYEAVLPKE KLKVEHSREY
KQERTYTRDL LGPTVSLTQA AFTPIPVDTS QIVLPPHLER IREKLAENIH ELWVMNKIEL
GWQYGPVRDD NKRQHPCLVE FSKLPEQERN YNLQMSLETL KTLLALGCHV GISDEHAEDK
VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA ENAHNVWARD RIRQGWTYGI
QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL REAVRTLLGY GYNLEAPDQD HAARAEVCSG
TGERFRIFRA EKTYAVKAGR WYFEFETVTA GDMRVGWSRP GCQPDQELGS DERAFAFDGF
KAQRWHQGNE HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG
FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW LSKRLPQFLQ
VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNSNTDIM FYRLSMPIEC AEVFSKTVAG
GLPGAGLFGP KNDLEDYDAD SDFEVLMKTA HGHLVPDRVD KDKEATKPEF NNHKDYAQEK
PSRLKQRFLL RRTKPDYSTS HSARLTEDVL ADDRDDYDFL MQTSTYYYSV RIFPGQEPAN
VWVGWITSDF HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR
NNNGLEIGCV VDAASGLLTF IANGKELSTY YQVEPSTKLF PAVFAQATSP NVFQFELGRI
KNVMPLSAGL FKSEHKNPVP QCPPRLHVQF LSHVLWSRMP NQFLKVDVSR ISERQGWLVQ
CLDPLQFMSL HIPEENRSVD ILELTEQEEL LKFHYHTLRL YSAVCALGNH RVAHALCSHV
DEPQLLYAIE NKYMPGLLRA GYYDLLIDIH LSSYATARLM MNNEYIVPMT EETKSITLFP
DENKKHGLPG IGLSTSLRPR MQFSSPSFVS ISNECYQYSP EFPLDILKSK TIQMLTEAVK
EGSLHARDPV GGTTEFLFVP LIKLFYTLLI MGIFHNEDLK HILQLIEPSV FKEAATPEEE
SDTLEKELSV DDAKLQGAGE EEAKGGKRPK EGLLQMKLPE PVKLQMCLLL QYLCDCQVRH
RIEAIVAFSD DFVAKLQDNQ RFRYNEVMQA LNMSAALTAR KTKEFRSPPQ EQINMLLNFK
DDKSECPCPE EIRDQLLDFH EDLMTHCGIE LDEDGSLDGN SDLTIRGRLL SLVEKVTYLK
KKQAEKPVES DSKKSSTLQQ LISETMVRWA QESVIEDPEL VRAMFVLLHR QYDGIGGLVR
ALPKTYTING VSVEDTINLL ASLGQIRSLL SVRMGKEEEK LMIRGLGDIM NNKVFYQHPN
LMRALGMHET VMEVMVNVLG GGESKEITFP KMVANCCRFL CYFCRISRQN QKAMFDHLSY
LLENSSVGLA SPAMRGSTPL DVAAASVMDN NELALALREP DLEKVVRYLA GCGLQSCQML
VSKGYPDIGW NPVEGERYLD FLRFAVFCNG ESVEENANVV VRLLIRRPEC FGPALRGEGG
NGLLAAMEEA IKIAEDPSRD GPSPNSGSSK TLDTEEEEDD TIHMGNAIMT FYSALIDLLG
RCAPEMHLIH AGKGEAIRIR SILRSLIPLG DLVGVISIAF QMPTIAKDGN VVEPDMSAGF
CPDHKAAMVL FLDRVYGIEV QDFLLHLLEV GFLPDLRAAA SLDTAALSAT DMALALNRYL
CTAVLPLLTR CAPLFAGTEH HASLIDSLLH TVYRLSKGCS LTKAQRDSIE VCLLSICGQL
RPSMMQHLLR RLVFDVPLLN EHAKMPLKLL TNHYERCWKY YCLPGGWGNF GAASEEELHL
SRKLFWGIFD ALSQKKYEQE LFKLALPCLS AVAGALPPDY MESNYVSMME KQSSMDSEGN
FNPQPVDTSN ITIPEKLEYF INKYAEHSHD KWSMDKLANG WIYGEIYSDS SKVQPLMKPY
KLLSEKEKEI YRWPIKESLK TMLAWGWRIE RTREGDSMAL YNRTRRISQT SQVSVDAAHG
YSPRAIDMSN VTLSRDLHAM AEMMAENYHN IWAKKKKMEL ESKGGGNHPL LVPYDTLTAK
EKAKDREKAQ DILKFLQING YAVSRGFKDL ELDTPSIEKR FAYSFLQQLI RYVDEAHQYI
LEFDGGSRGK GEHFPYEQEI KFFAKVVLPL IDQYFKNHRL YFLSAASRPL CSGGHASNKE
KEMVTSLFCK LGVLVRHRIS LFGNDATSIV NCLHILGQTL DARTVMKTGL ESVKSALRAF
LDNAAEDLEK TMENLKQGQF THTRNQPKGV TQIINYTTVA LLPMLSSLFE HIGQHQFGED
LILEDVQVSC YRILTSLYAL GTSKSIYVER QRSALGECLA AFAGAFPVAF LETHLDKHNI
YSIYNTKSSR ERAALSLPTN VEDVCPNIPS LEKLMEEIVE LAESGIRYTQ MPHVMEVILP
MLCSYMSRWW EHGPENNPER AEMCCTALNS EHMNTLLGNI LKIIYNNLGI DEGAWMKRLA
VFSQPIINKV KPQLLKTHFL PLMEKLKKKA ATVVSEEDHL KAEARGDMSE AELLILDEFT
TLARDLYAFY PLLIRFVDYN RAKWLKEPNP EAEELFRMVA EVFIYWSKSH NFKREEQNFV
VQNEINNMSF LITDTKSKMS KAAVSDQERK KMKRKGDRYS MQTSLIVAAL KRLLPIGLNI
CAPGDQELIA LAKNRFSLKD TEDEVRDIIR SNIHLQGKLE DPAIRWQMAL YKDLPNRTDD
TSDPEKTVER VLDIANVLFH LEQKSKRVGR RHYCLVEHPQ RSKKAVWHKL LSKQRKRAVV
ACFRMAPLYN LPRHRAVNLF LQGYEKSWIE TEEHYFEDKL IEDLAKPGAE PPEEDEGTKR
VDPLHQLILL FSRTALTEKC KLEEDFLYMA YADIMAKSCH DEEDDDGEEE VKSFEEKEME
KQKLLYQQAR LHDRGAAEMV LQTISASKGE TGPMVAATLK LGIAILNGGN STVQQKMLDY
LKEKKDVGFF QSLAGLMQSC SVLDLNAFER QNKAEGLGMV TEEGSGEKVL QDDEFTCDLF
RFLQLLCEGH NSDFQNYLRT QTGNNTTVNI IISTVDYLLR VQESISDFYW YYSGKDVIDE
QGQRNFSKAI QVAKQVFNTL TEYIQGPCTG NQQSLAHSRL WDAVVGFLHV FAHMQMKLSQ
DSSQIELLKE LMDLQKDMVV MLLSMLEGNV VNGTIGKQMV DMLVESSNNV EMILKFFDMF
LKLKDLTSSD TFKEYDPDGK GVISKRDFHK AMESHKHYTQ SETEFLLSCA ETDENETLDY
EEFVKRFHEP AKDIGFNVAV LLTNLSEHMP NDTRLQTFLE LAESVLNYFQ PFLGRIEIMG
SAKRIERVYF EISESSRTQW EKPQVKESKR QFIFDVVNEG GEKEKMELFV NFCEDTIFEM
QLAAQISESD LNERSANKEE SEKERPEEQG PRMAFFSILT VRSALFALRY NILTLMRMLS
LKSLKKQMKK VKKMTVKDMV TAFFSSYWSI FMTLLHFVAS VFRGFFRIIC SLLLGGSLVE
GAKKIKVAEL LANMPDPTQD EVRGDGEEGE RKPLEAALPS EDLTDLKELT EESDLLSDIF
GLDLKREGGQ YKLIPHNPNA GLSDLMSNPV PMPEVQEKFQ EQKAKEEEKE EKEETKSEPE
KAEGEDGEKE EKAKEDKGKQ KLRQLHTHRY GEPEVPESAF WKKIIAYQQK LLNYFARNFY
NMRMLALFVA FAINFILLFY KVSTSSVVEG KELPTRSSSE NAKVTSLDSS SHRIIAVHYV
LEESSGYMEP TLRILAILHT VISFFCIIGY YCLKVPLVIF KREKEVARKL EFDGLYITEQ
PSEDDIKGQW DRLVINTQSF PNNYWDKFVK RKVMDKYGEF YGRDRISELL GMDKAALDFS
DAREKKKPKK DSSLSAVLNS IDVKYQMWKL GVVFTDNSFL YLAWYMTMSV LGHYNNFFFA
AHLLDIAMGF KTLRTILSSV THNGKQLVLT VGLLAVVVYL YTVVAFNFFR KFYNKSEDGD
TPDMKCDDML TCYMFHMYVG VRAGGGIGDE IEDPAGDEYE IYRIIFDITF FFFVIVILLA
IIQGLIIDAF GELRDQQEQV KEDMETKCFI CGIGNDYFDT VPHGFETHTL QEHNLANYLF
FLMYLINKDE TEHTGQESYV WKMYQERCWE FFPAGDCFRK QYEDQLN


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