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Ryanodine receptor 1 (RYR-1) (RyR1) (Skeletal muscle calcium release channel) (Skeletal muscle ryanodine receptor) (Skeletal muscle-type ryanodine receptor) (Type 1 ryanodine receptor)

 RYR1_RABIT              Reviewed;        5037 AA.
P11716;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
25-OCT-2017, entry version 163.
RecName: Full=Ryanodine receptor 1;
Short=RYR-1;
Short=RyR1;
AltName: Full=Skeletal muscle calcium release channel;
AltName: Full=Skeletal muscle ryanodine receptor;
AltName: Full=Skeletal muscle-type ryanodine receptor;
AltName: Full=Type 1 ryanodine receptor;
Name=RYR1;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, DOMAIN, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Skeletal muscle;
PubMed=2725677; DOI=10.1038/339439a0;
Takeshima H., Nishimura S., Matsumoto T., Ishido H., Kangawa K.,
Minamino N., Matsuo H., Ueda M., Hanaoka M., Hirose T., Numa S.;
"Primary structure and expression from complementary DNA of skeletal
muscle ryanodine receptor.";
Nature 339:439-445(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=2298749;
Zorzato F., Fujii J., Otsu K., Phillips M.S., Green N.M., Lai F.A.,
Meissner G., Maclennan D.H.;
"Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+
release channel (ryanodine receptor) of skeletal muscle sarcoplasmic
reticulum.";
J. Biol. Chem. 265:2244-2256(1990).
[3]
PROTEIN SEQUENCE OF 3631-3650, S-NITROSYLATION AT CYS-3635, AND
INTERACTION WITH CALM.
PubMed=10601232; DOI=10.1074/jbc.274.52.36831;
Porter Moore C., Zhang J.Z., Hamilton S.L.;
"A role for cysteine 3635 of RYR1 in redox modulation and calmodulin
binding.";
J. Biol. Chem. 274:36831-36834(1999).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=3722165;
Pessah I.N., Francini A.O., Scales D.J., Waterhouse A.L., Casida J.E.;
"Calcium-ryanodine receptor complex. Solubilization and partial
characterization from skeletal muscle junctional sarcoplasmic
reticulum vesicles.";
J. Biol. Chem. 261:8643-8648(1986).
[5]
PHOSPHORYLATION AT SER-2843.
PubMed=8380342; DOI=10.1016/0167-4889(93)90023-I;
Suko J., Maurer-Fogy I., Plank B., Bertel O., Wyskovsky W.,
Hohenegger M., Hellmann G.;
"Phosphorylation of serine 2843 in ryanodine receptor-calcium release
channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein
kinase.";
Biochim. Biophys. Acta 1175:193-206(1993).
[6]
INTERACTION WITH FKBP1A, AND TISSUE SPECIFICITY.
PubMed=7669046; DOI=10.1006/bbrc.1995.2283;
Xin H.B., Timerman A.P., Onoue H., Wiederrecht G.J., Fleischer S.;
"Affinity purification of the ryanodine receptor/calcium release
channel from fast twitch skeletal muscle based on its tight
association with FKBP12.";
Biochem. Biophys. Res. Commun. 214:263-270(1995).
[7]
INTERACTION WITH FKBP1A.
PubMed=10603943; DOI=10.1111/j.1749-6632.1998.tb08263.x;
Ondrias K., Marx S.O., Gaburjakova M., Marks A.R.;
"FKBP12 modulates gating of the ryanodine receptor/calcium release
channel.";
Ann. N. Y. Acad. Sci. 853:149-156(1998).
[8]
INTERACTION WITH TRDN.
PubMed=9737879; DOI=10.1021/bi972803d;
Ohkura M., Furukawa K., Fujimori H., Kuruma A., Kawano S., Hiraoka M.,
Kuniyasu A., Nakayama H., Ohizumi Y.;
"Dual regulation of the skeletal muscle ryanodine receptor by triadin
and calsequestrin.";
Biochemistry 37:12987-12993(1998).
[9]
INTERACTION WITH CACNA1S, AND FUNCTION.
PubMed=10388749; DOI=10.1016/S0006-3495(99)76881-5;
Dulhunty A.F., Laver D.R., Gallant E.M., Casarotto M.G., Pace S.M.,
Curtis S.;
"Activation and inhibition of skeletal RyR channels by a part of the
skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12.";
Biophys. J. 77:189-203(1999).
[10]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF
ILE-4897, AND SUBUNIT.
PubMed=10097181; DOI=10.1073/pnas.96.7.4164;
Lynch P.J., Tong J., Lehane M., Mallet A., Giblin L., Heffron J.J.A.,
Vaughan P., Zafra G., MacLennan D.H., McCarthy T.V.;
"A mutation in the transmembrane/luminal domain of the ryanodine
receptor is associated with abnormal Ca(2+) release channel function
and severe central core disease.";
Proc. Natl. Acad. Sci. U.S.A. 96:4164-4169(1999).
[11]
S-NITROSYLATION AT CYS-3635, MUTAGENESIS OF CYS-3635, AND INTERACTION
WITH CALM.
PubMed=11562475; DOI=10.1073/pnas.201289098;
Sun J., Xin C., Eu J.P., Stamler J.S., Meissner G.;
"Cysteine-3635 is responsible for skeletal muscle ryanodine receptor
modulation by NO.";
Proc. Natl. Acad. Sci. U.S.A. 98:11158-11162(2001).
[12]
INTERACTION WITH RYR2.
PubMed=12213830; DOI=10.1074/jbc.M208210200;
Xiao B., Masumiya H., Jiang D., Wang R., Sei Y., Zhang L.,
Murayama T., Ogawa Y., Lai F.A., Wagenknecht T., Chen S.R.;
"Isoform-dependent formation of heteromeric Ca2+ release channels
(ryanodine receptors).";
J. Biol. Chem. 277:41778-41785(2002).
[13]
SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
PubMed=12486242; DOI=10.1073/pnas.012688999;
Du G.G., Sandhu B., Khanna V.K., Guo X.H., MacLennan D.H.;
"Topology of the Ca2+ release channel of skeletal muscle sarcoplasmic
reticulum (RyR1).";
Proc. Natl. Acad. Sci. U.S.A. 99:16725-16730(2002).
[14]
FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, AND MUTAGENESIS OF
ARG-164; GLY-342; ARG-615; ARG-2163; VAL-2168; ARG-2458 AND THR-4825.
PubMed=12732639; DOI=10.1074/jbc.M302165200;
Yang T., Ta T.A., Pessah I.N., Allen P.D.;
"Functional defects in six ryanodine receptor isoform-1 (RyR1)
mutations associated with malignant hyperthermia and their impact on
skeletal excitation-contraction coupling.";
J. Biol. Chem. 278:25722-25730(2003).
[15]
INTERACTION WITH SELENON.
PubMed=18713863; DOI=10.1073/pnas.0806015105;
Jurynec M.J., Xia R., Mackrill J.J., Gunther D., Crawford T.,
Flanigan K.M., Abramson J.J., Howard M.T., Grunwald D.J.;
"Selenoprotein N is required for ryanodine receptor calcium release
channel activity in human and zebrafish muscle.";
Proc. Natl. Acad. Sci. U.S.A. 105:12485-12490(2008).
[16]
INTERACTION WITH TRDN AND ASPH.
PubMed=19398037; DOI=10.1016/j.biocel.2009.04.017;
Wei L., Gallant E.M., Dulhunty A.F., Beard N.A.;
"Junctin and triadin each activate skeletal ryanodine receptors but
junctin alone mediates functional interactions with calsequestrin.";
Int. J. Biochem. Cell Biol. 41:2214-2224(2009).
[17]
INTERACTION WITH CACNB1.
PubMed=21320436; DOI=10.1016/j.bpj.2011.01.022;
Rebbeck R.T., Karunasekara Y., Gallant E.M., Board P.G., Beard N.A.,
Casarotto M.G., Dulhunty A.F.;
"The beta(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and
activates the channel via its 35-residue C-terminal tail.";
Biophys. J. 100:922-930(2011).
[18]
FUNCTION, ENZYME REGULATION, S-NITROSYLATION AT CYS-3635, AND
MUTAGENESIS OF CYS-3635.
PubMed=22036948; DOI=10.1038/emboj.2011.386;
Kakizawa S., Yamazawa T., Chen Y., Ito A., Murayama T., Oyamada H.,
Kurebayashi N., Sato O., Watanabe M., Mori N., Oguchi K., Sakurai T.,
Takeshima H., Saito N., Iino M.;
"Nitric oxide-induced calcium release via ryanodine receptors
regulates neuronal function.";
EMBO J. 31:417-428(2012).
[19]
STRUCTURE BY ELECTRON MICROSCOPY (10 ANGSTROMS), SUBUNIT, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15908964; DOI=10.1038/nsmb938;
Samso M., Wagenknecht T., Allen P.D.;
"Internal structure and visualization of transmembrane domains of the
RyR1 calcium release channel by cryo-EM.";
Nat. Struct. Mol. Biol. 12:539-544(2005).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3614-3643 IN COMPLEX WITH
CALM.
PubMed=17027503; DOI=10.1016/j.str.2006.08.011;
Maximciuc A.A., Putkey J.A., Shamoo Y., Mackenzie K.R.;
"Complex of calmodulin with a ryanodine receptor target reveals a
novel, flexible binding mode.";
Structure 14:1547-1556(2006).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS), AND SUBUNIT.
PubMed=18621707; DOI=10.1073/pnas.0803189105;
Serysheva I.I., Ludtke S.J., Baker M.L., Cong Y., Topf M., Eramian D.,
Sali A., Hamilton S.L., Chiu W.;
"Subnanometer-resolution electron cryomicroscopy-based domain models
for the cytoplasmic region of skeletal muscle RyR channel.";
Proc. Natl. Acad. Sci. U.S.A. 105:9610-9615(2008).
[22]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-210.
PubMed=19541610; DOI=10.1073/pnas.0905186106;
Amador F.J., Liu S., Ishiyama N., Plevin M.J., Wilson A.,
MacLennan D.H., Ikura M.;
"Crystal structure of type I ryanodine receptor amino-terminal beta-
trefoil domain reveals a disease-associated mutation 'hot spot'
loop.";
Proc. Natl. Acad. Sci. U.S.A. 106:11040-11044(2009).
[23]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 9-205.
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).
[24]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-559.
PubMed=21048710; DOI=10.1038/nature09471;
Tung C.C., Lobo P.A., Kimlicka L., Van Petegem F.;
"The amino-terminal disease hotspot of ryanodine receptors forms a
cytoplasmic vestibule.";
Nature 468:585-588(2010).
[25] {ECO:0000244|PDB:3RQR}
X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2733-2940.
PubMed=22913516; DOI=10.1111/j.1742-4658.2012.08755.x;
Sharma P., Ishiyama N., Nair U., Li W., Dong A., Miyake T., Wilson A.,
Ryan T., MacLennan D.H., Kislinger T., Ikura M., Dhe-Paganon S.,
Gramolini A.O.;
"Structural determination of the phosphorylation domain of the
ryanodine receptor.";
FEBS J. 279:3952-3964(2012).
[26] {ECO:0000244|PDB:4ERT, ECO:0000244|PDB:4ESU, ECO:0000244|PDB:4ETU}
X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 2734-2940, AND MUTAGENESIS
OF LEU-2867.
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).
[27] {ECO:0000244|PDB:4I0Y, ECO:0000244|PDB:4I1E, ECO:0000244|PDB:4I2S, ECO:0000244|PDB:4I37, ECO:0000244|PDB:4I3N, ECO:0000244|PDB:4I6I, ECO:0000244|PDB:4I7I, ECO:0000244|PDB:4I8M, ECO:0000244|PDB:4I96}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-536.
PubMed=23422674; DOI=10.1038/ncomms2501;
Kimlicka L., Lau K., Tung C.C., Van Petegem F.;
"Disease mutations in the ryanodine receptor N-terminal region couple
to a mobile intersubunit interface.";
Nat. Commun. 4:1506-1506(2013).
[28] {ECO:0000244|PDB:4P9J}
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 1070-1246, AND MUTAGENESIS
OF ARG-1076.
PubMed=25370123; DOI=10.1038/ncomms6397;
Lau K., Van Petegem F.;
"Crystal structures of wild type and disease mutant forms of the
ryanodine receptor SPRY2 domain.";
Nat. Commun. 5:5397-5397(2014).
[29] {ECO:0000244|PDB:5C30}
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 857-1054, INTERACTION WITH
FKBP1A, FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF
674-PHE-LEU-675; ASN-760; ARG-1044; GLY-1050 AND VAL-2461.
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).
[30] {ECO:0000244|PDB:4UWA, ECO:0000244|PDB:4UWE}
STRUCTURE BY ELECTRON MICROSCOPY (6.10 ANGSTROMS), SUBCELLULAR
LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
PubMed=25470059; DOI=10.1038/NATURE13916;
Efremov R.G., Leitner A., Aebersold R., Raunser S.;
"Architecture and conformational switch mechanism of the ryanodine
receptor.";
Nature 517:39-43(2015).
[31] {ECO:0000244|PDB:3J8H}
STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) IN COMPLEX WITH
FKBP1A, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY,
AND DOMAIN.
PubMed=25517095; DOI=10.1038/nature14063;
Yan Z., Bai X.C., Yan C., Wu J., Li Z., Xie T., Peng W., Yin C.C.,
Li X., Scheres S.H., Shi Y., Yan N.;
"Structure of the rabbit ryanodine receptor RyR1 at near-atomic
resolution.";
Nature 517:50-55(2015).
[32] {ECO:0000244|PDB:5T15, ECO:0000244|PDB:5T9M, ECO:0000244|PDB:5T9V, ECO:0000244|PDB:5TA3, ECO:0000244|PDB:5TAL, ECO:0000244|PDB:5TAM, ECO:0000244|PDB:5TAN}
STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 12-1275;
1573-2479; 2734-2939 AND 3639-5037 IN COMPLEXES WITH CALCIUM; ATP;
RYANODINE AND CAFFEINE, FUNCTION, ENZYME REGULATION, SUBUNIT,
SUBCELLULAR LOCATION, DOMAIN, AND TOPOLOGY.
PubMed=27662087; DOI=10.1016/j.cell.2016.08.075;
des Georges A., Clarke O.B., Zalk R., Yuan Q., Condon K.J.,
Grassucci R.A., Hendrickson W.A., Marks A.R., Frank J.;
"Structural basis for gating and activation of RyR1.";
Cell 167:145-157(2016).
[33] {ECO:0000244|PDB:5J8V}
STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), SUBUNIT,
SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
PubMed=27573175; DOI=10.1038/cr.2016.99;
Wei R., Wang X., Zhang Y., Mukherjee S., Zhang L., Chen Q., Huang X.,
Jing S., Liu C., Li S., Wang G., Xu Y., Zhu S., Williams A.J., Sun F.,
Yin C.C.;
"Structural insights into Ca(2+)-activated long-range allosteric
channel gating of RyR1.";
Cell Res. 26:977-994(2016).
[34] {ECO:0000244|PDB:5GKY, ECO:0000244|PDB:5GKZ, ECO:0000244|PDB:5GL0, ECO:0000244|PDB:5GL1}
STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) IN COMPLEX WITH
FKBP1A, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY,
AND DOMAIN.
PubMed=27468892; DOI=10.1038/cr.2016.89;
Bai X.C., Yan Z., Wu J., Li Z., Yan N.;
"The central domain of RyR1 is the transducer for long-range
allosteric gating of channel opening.";
Cell Res. 26:995-1006(2016).
-!- 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 muscle contraction following depolarization
of T-tubules (PubMed:3722165, PubMed:10388749, PubMed:10097181,
PubMed:12732639, PubMed:22036948, PubMed:26245150,
PubMed:27662087). Repeated very high-level exercise increases the
open probability of the channel and leads to Ca(2+) leaking into
the cytoplasm (By similarity). Can also mediate the release of
Ca(2+) from intracellular stores in neurons, and may thereby
promote prolonged Ca(2+) signaling in the brain. Required for
normal embryonic development of muscle fibers and skeletal muscle.
Required for normal heart morphogenesis, skin development and
ossification during embryogenesis (By similarity).
{ECO:0000250|UniProtKB:E9PZQ0, ECO:0000269|PubMed:10388749,
ECO:0000269|PubMed:12732639, ECO:0000269|PubMed:22036948,
ECO:0000269|PubMed:27662087, ECO:0000305|PubMed:10097181,
ECO:0000305|PubMed:26245150, ECO:0000305|PubMed:3722165}.
-!- ENZYME REGULATION: Channel activity is modulated by the alkaloid
ryanodine that binds to the open Ca-release channel with high
affinity (PubMed:27662087). At low concentrations, ryanodine
maintains the channel in an open conformation (PubMed:27662087).
High ryanodine concentrations inhibit channel activity
(PubMed:27662087). Channel activity is regulated by calmodulin
(CALM). The calcium release is activated by increased cytoplasmic
calcium levels, by nitric oxyde (NO), caffeine and ATP
(PubMed:12732639, PubMed:22036948, PubMed:26245150,
PubMed:27662087). Channel activity is inhibited by magnesium ions,
possibly by competition for calcium binding sites
(PubMed:12732639). {ECO:0000269|PubMed:12732639,
ECO:0000269|PubMed:22036948, ECO:0000269|PubMed:26245150,
ECO:0000269|PubMed:27662087}.
-!- SUBUNIT: Homotetramer (PubMed:10097181, PubMed:15908964,
PubMed:17027503, PubMed:18621707, PubMed:25470059,
PubMed:25517095, PubMed:27662087, PubMed:27573175,
PubMed:27468892). Can also form heterotetramers with RYR2
(PubMed:12213830). Identified in a complex composed of RYR1,
PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Repeated very
high-level exercise decreases interaction with PDE4D and protein
phosphatase 1 (PP1) (By similarity). Interacts with CALM; CALM
with bound calcium inhibits the RYR1 channel activity
(PubMed:10601232, PubMed:11562475, PubMed:17027503). Interacts
with S100A1 (By similarity). Interacts with FKBP1A; this
stabilizes the closed conformation of the channel (PubMed:7669046,
PubMed:10603943, PubMed:26245150, PubMed:25517095,
PubMed:27468892). Interacts with CACNA1S; interaction with CACNA1S
is important for activation of the RYR1 channel (PubMed:10388749).
Interacts with CACNB1 (PubMed:21320436). Interacts with TRDN and
ASPH; these interactions stimulate RYR1 channel activity
(PubMed:9737879, PubMed:19398037). Interacts with SELENON
(PubMed:18713863). {ECO:0000250|UniProtKB:E9PZQ0,
ECO:0000250|UniProtKB:P21817, ECO:0000269|PubMed:10097181,
ECO:0000269|PubMed:10388749, ECO:0000269|PubMed:10601232,
ECO:0000269|PubMed:10603943, ECO:0000269|PubMed:11562475,
ECO:0000269|PubMed:12213830, ECO:0000269|PubMed:15908964,
ECO:0000269|PubMed:17027503, ECO:0000269|PubMed:18621707,
ECO:0000269|PubMed:18713863, ECO:0000269|PubMed:19398037,
ECO:0000269|PubMed:21320436, ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095, ECO:0000269|PubMed:26245150,
ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
ECO:0000269|PubMed:27662087, ECO:0000269|PubMed:7669046,
ECO:0000269|PubMed:9737879}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-6477441, EBI-6477441;
P28652:Camk2b (xeno); NbExp=4; IntAct=EBI-6477441, EBI-397029;
P62943:FKBP1A; NbExp=2; IntAct=EBI-6477441, EBI-16134925;
P68106-1:FKBP1B (xeno); NbExp=2; IntAct=EBI-6477441, EBI-15766566;
P02639:S100A1 (xeno); NbExp=3; IntAct=EBI-6477441, EBI-6477285;
-!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
{ECO:0000269|PubMed:12486242, ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:2725677, ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175, ECO:0000269|PubMed:27662087,
ECO:0000269|PubMed:3722165}; Multi-pass membrane protein
{ECO:0000269|PubMed:25470059, ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
ECO:0000269|PubMed:27662087}. Sarcoplasmic reticulum
{ECO:0000269|PubMed:18713863}. Membrane
{ECO:0000269|PubMed:12732639}; Multi-pass membrane protein
{ECO:0000269|PubMed:25470059, ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
ECO:0000269|PubMed:27662087}. Note=The number of predicted
transmembrane domains varies between orthologs, but the 3D-
structures show the presence of six transmembrane regions. Both N-
terminus and C-terminus are cytoplasmic.
{ECO:0000269|PubMed:12486242, ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
ECO:0000269|PubMed:27662087}.
-!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level)
(PubMed:2725677, PubMed:3722165, PubMed:25470059, PubMed:25517095,
PubMed:27573175, PubMed:27468892). Fast- or slow-twitch skeletal
muscle. {ECO:0000269|PubMed:15908964, ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095, ECO:0000269|PubMed:2725677,
ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
ECO:0000269|PubMed:3722165, ECO:0000269|PubMed:7669046}.
-!- DOMAIN: The calcium release channel activity resides in the C-
terminal region while the remaining part of the protein
constitutes the 'foot' structure spanning the junctional gap
between the sarcoplasmic reticulum (SR) and the T-tubule
(PubMed:2725677, PubMed:25517095, PubMed:27662087,
PubMed:27573175, PubMed:27468892). Pore opening is mediated via
the cytoplasmic calcium-binding domains that mediate a small
rotation of the channel-forming transmembrane regions that then
leads to channel opening (PubMed:27468892).
{ECO:0000269|PubMed:25517095, ECO:0000269|PubMed:2725677,
ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
ECO:0000269|PubMed:27662087}.
-!- PTM: The N-terminus is blocked.
-!- PTM: Channel activity is modulated by phosphorylation.
Phosphorylation at Ser-2843 may increase channel activity.
Repeated very high-level exercise increases phosphorylation at
Ser-2843. {ECO:0000250|UniProtKB:P21817}.
-!- PTM: Activated by reversible S-nitrosylation (PubMed:22036948).
Repeated very high-level exercise increases S-nitrosylation (By
similarity). {ECO:0000250|UniProtKB:P21817,
ECO:0000269|PubMed:22036948}.
-!- MISCELLANEOUS: Coexpression of normal and mutant Thr-4897 RYR1 in
a 1:1 ratio produces RYR1 channels with normal halothane and
caffeine sensitivities, but maximal levels of Ca(2+) release are
reduced by 67%. Binding of [3H]ryanodine indicates that the
heterozygous channel is activated by Ca(2+) concentrations 4-fold
lower than normal. Single-cell analysis of cotransfected cells
shows a significantly increased resting cytoplasmic Ca(2+) level
and a significantly reduced luminal Ca(2+) level. These data
indicated a leaky channel, possibly caused by a reduction in the
Ca(2+) concentration required for channel activation.
{ECO:0000269|PubMed:10097181}.
-!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family.
RYR1 subfamily. {ECO:0000305}.
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EMBL; X15209; CAA33279.1; -; mRNA.
EMBL; X15750; CAA33762.1; -; mRNA.
PIR; S04654; B35041.
RefSeq; NP_001095188.1; NM_001101718.1.
UniGene; Ocu.2092; -.
PDB; 2BCX; X-ray; 2.00 A; B=3614-3643.
PDB; 2XOA; X-ray; 2.50 A; A=1-559.
PDB; 3HSM; X-ray; 2.50 A; A/B=1-210.
PDB; 3ILA; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I=9-205.
PDB; 3J8H; EM; 3.80 A; A/C/E/G=1-5037.
PDB; 3RQR; X-ray; 2.16 A; A=2733-2940.
PDB; 4ERT; X-ray; 1.95 A; A=2734-2940.
PDB; 4ESU; X-ray; 1.59 A; A=2734-2940.
PDB; 4ETT; X-ray; 2.20 A; A=2734-2940.
PDB; 4ETU; X-ray; 2.19 A; A=2734-2938.
PDB; 4I0Y; X-ray; 2.80 A; A=1-536.
PDB; 4I1E; X-ray; 2.40 A; A=1-536.
PDB; 4I2S; X-ray; 2.50 A; A=1-536.
PDB; 4I37; X-ray; 2.95 A; A=1-536.
PDB; 4I3N; X-ray; 2.95 A; A=1-536.
PDB; 4I6I; X-ray; 2.50 A; A=1-559.
PDB; 4I7I; X-ray; 2.90 A; A=1-536.
PDB; 4I8M; X-ray; 2.80 A; A=1-536.
PDB; 4I96; X-ray; 2.73 A; A=217-536.
PDB; 4P9J; X-ray; 1.84 A; A/B/C=1070-1246.
PDB; 4UWA; EM; 6.10 A; A/B/C/D=1-5037.
PDB; 4UWE; EM; 8.50 A; A/B/C/D=1-5037.
PDB; 5C30; X-ray; 1.55 A; A=857-1054.
PDB; 5GKY; EM; 3.80 A; A/C/E/G=1-5037.
PDB; 5GKZ; EM; 4.00 A; A/C/E/G=1-5037.
PDB; 5GL0; EM; 4.20 A; A/C/E/G=1-5037.
PDB; 5GL1; EM; 5.70 A; A/C/E/G=1-5037.
PDB; 5J8V; EM; 4.90 A; A/B/C/D=1-5037.
PDB; 5T15; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-5037.
PDB; 5T9M; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-5037.
PDB; 5T9N; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-5037.
PDB; 5T9R; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-5037.
PDB; 5T9S; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-5037.
PDB; 5T9V; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4540-5037.
PDB; 5TA3; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAL; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAM; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAN; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAP; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAQ; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAS; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAT; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAU; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAV; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAW; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAX; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAY; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TAZ; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TB0; EM; 3.80 A; B/E/G/I=1-5037.
PDB; 5TB1; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TB2; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TB3; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDB; 5TB4; EM; 3.80 A; B/E/G/I=12-1275, B/E/G/I=1573-2479, B/E/G/I=2734-2939, B/E/G/I=3639-4253, B/E/G/I=4541-5037.
PDBsum; 2BCX; -.
PDBsum; 2XOA; -.
PDBsum; 3HSM; -.
PDBsum; 3ILA; -.
PDBsum; 3J8H; -.
PDBsum; 3RQR; -.
PDBsum; 4ERT; -.
PDBsum; 4ESU; -.
PDBsum; 4ETT; -.
PDBsum; 4ETU; -.
PDBsum; 4I0Y; -.
PDBsum; 4I1E; -.
PDBsum; 4I2S; -.
PDBsum; 4I37; -.
PDBsum; 4I3N; -.
PDBsum; 4I6I; -.
PDBsum; 4I7I; -.
PDBsum; 4I8M; -.
PDBsum; 4I96; -.
PDBsum; 4P9J; -.
PDBsum; 4UWA; -.
PDBsum; 4UWE; -.
PDBsum; 5C30; -.
PDBsum; 5GKY; -.
PDBsum; 5GKZ; -.
PDBsum; 5GL0; -.
PDBsum; 5GL1; -.
PDBsum; 5J8V; -.
PDBsum; 5T15; -.
PDBsum; 5T9M; -.
PDBsum; 5T9N; -.
PDBsum; 5T9R; -.
PDBsum; 5T9S; -.
PDBsum; 5T9V; -.
PDBsum; 5TA3; -.
PDBsum; 5TAL; -.
PDBsum; 5TAM; -.
PDBsum; 5TAN; -.
PDBsum; 5TAP; -.
PDBsum; 5TAQ; -.
PDBsum; 5TAS; -.
PDBsum; 5TAT; -.
PDBsum; 5TAU; -.
PDBsum; 5TAV; -.
PDBsum; 5TAW; -.
PDBsum; 5TAX; -.
PDBsum; 5TAY; -.
PDBsum; 5TAZ; -.
PDBsum; 5TB0; -.
PDBsum; 5TB1; -.
PDBsum; 5TB2; -.
PDBsum; 5TB3; -.
PDBsum; 5TB4; -.
ProteinModelPortal; P11716; -.
SMR; P11716; -.
DIP; DIP-41872N; -.
IntAct; P11716; 8.
MINT; MINT-158193; -.
BindingDB; P11716; -.
ChEMBL; CHEMBL3288; -.
iPTMnet; P11716; -.
SwissPalm; P11716; -.
PRIDE; P11716; -.
GeneID; 100009540; -.
KEGG; ocu:100009540; -.
CTD; 6261; -.
HOVERGEN; HBG006699; -.
InParanoid; P11716; -.
KO; K04961; -.
EvolutionaryTrace; P11716; -.
PRO; PR:P11716; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0031301; C:integral component of organelle membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:1990425; C:ryanodine receptor complex; IDA:UniProtKB.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0014802; C:terminal cisterna; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0035381; F:ATP-gated ion channel activity; IDA:CAFA.
GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0015278; F:calcium-release channel activity; IMP:AgBase.
GO; GO:0005516; F:calmodulin binding; IDA:BHF-UCL.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0008144; F:drug binding; IDA:AgBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IDA:UniProtKB.
GO; GO:0015643; F:toxic substance binding; IDA:AgBase.
GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0071313; P:cellular response to caffeine; IDA:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
GO; GO:0043931; P:ossification involved in bone maturation; ISS:UniProtKB.
GO; GO:0003151; P:outflow tract morphogenesis; ISS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:CAFA.
GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:UniProtKB.
GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
GO; GO:0043588; P:skin development; ISS:UniProtKB.
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.
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.
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; IPR033215; RyR1.
InterPro; IPR035761; SPRY1_RyR.
InterPro; IPR035764; SPRY2_RyR.
InterPro; IPR035762; SPRY3_RyR.
InterPro; IPR003877; SPRY_dom.
PANTHER; PTHR13715; PTHR13715; 1.
PANTHER; PTHR13715:SF15; PTHR13715:SF15; 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; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49899; SSF49899; 3.
SUPFAM; SSF82109; SSF82109; 2.
PROSITE; PS50188; B302_SPRY; 3.
PROSITE; PS50919; MIR; 5.
1: Evidence at protein level;
3D-structure; ATP-binding; Calcium; Calcium channel;
Calcium transport; Calmodulin-binding; Complete proteome;
Developmental protein; Direct protein sequencing; Ion channel;
Ion transport; Ligand-gated ion channel; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; S-nitrosylation; Sarcoplasmic reticulum; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 5037 Ryanodine receptor 1.
/FTId=PRO_0000219360.
TOPO_DOM 1 4558 Cytoplasmic.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TRANSMEM 4559 4579 Helical; Name=1.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TOPO_DOM 4580 4640 Lumenal. {ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TRANSMEM 4641 4661 Helical; Name=2.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TOPO_DOM 4662 4779 Cytoplasmic.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TRANSMEM 4780 4802 Helical; Name=3.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TOPO_DOM 4803 4803 Lumenal. {ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TRANSMEM 4804 4820 Helical; Name=4.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TOPO_DOM 4821 4835 Cytoplasmic.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TRANSMEM 4836 4856 Helical; Name=5.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TOPO_DOM 4857 4879 Lumenal. {ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
INTRAMEM 4880 4899 Pore-forming.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TOPO_DOM 4900 4919 Lumenal. {ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TRANSMEM 4920 4940 Helical; Name=6.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
TOPO_DOM 4941 5037 Cytoplasmic.
{ECO:0000269|PubMed:25470059,
ECO:0000269|PubMed:25517095,
ECO:0000269|PubMed:27468892,
ECO:0000269|PubMed:27573175}.
DOMAIN 98 153 MIR 1. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 160 205 MIR 2. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 211 265 MIR 3. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 271 334 MIR 4. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 336 394 MIR 5. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 582 798 B30.2/SPRY 1. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
REPEAT 842 955 1.
REPEAT 956 1069 2.
DOMAIN 1014 1209 B30.2/SPRY 2. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
REPEAT 1345 1360 3; truncated.
DOMAIN 1358 1571 B30.2/SPRY 3. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
REPEAT 1373 1388 4; truncated.
REPEAT 2726 2845 5.
REPEAT 2846 2959 6.
DOMAIN 4075 4103 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448,
ECO:0000269|PubMed:27573175}.
NP_BIND 4211 4215 ATP. {ECO:0000244|PDB:5T9V,
ECO:0000244|PDB:5TA3,
ECO:0000244|PDB:5TAL,
ECO:0000244|PDB:5TAM,
ECO:0000244|PDB:5TAN,
ECO:0000244|PDB:5TAS,
ECO:0000244|PDB:5TAT,
ECO:0000244|PDB:5TAU,
ECO:0000305|PubMed:27662087}.
NP_BIND 4954 4959 ATP. {ECO:0000244|PDB:5T9V,
ECO:0000244|PDB:5TA3,
ECO:0000244|PDB:5TAL,
ECO:0000244|PDB:5TAM,
ECO:0000244|PDB:5TAN,
ECO:0000244|PDB:5TAS,
ECO:0000244|PDB:5TAT,
ECO:0000244|PDB:5TAU,
ECO:0000305|PubMed:27662087}.
NP_BIND 4979 4985 ATP. {ECO:0000244|PDB:5T9V,
ECO:0000244|PDB:5TA3,
ECO:0000244|PDB:5TAL,
ECO:0000244|PDB:5TAM,
ECO:0000244|PDB:5TAN,
ECO:0000244|PDB:5TAS,
ECO:0000244|PDB:5TAT,
ECO:0000244|PDB:5TAU,
ECO:0000305|PubMed:27662087}.
REGION 670 681 Interaction with FKBP1A.
{ECO:0000269|PubMed:26245150}.
REGION 842 2959 6 X approximate repeats.
REGION 3614 3643 Interaction with CALM.
MOTIF 4894 4900 Selectivity filter.
{ECO:0000305|PubMed:25517095,
ECO:0000305|PubMed:27573175,
ECO:0000305|PubMed:27662087}.
COMPBIAS 1873 1913 Glu-rich (acidic).
METAL 3893 3893 Calcium. {ECO:0000244|PDB:5TA3,
ECO:0000244|PDB:5TAL,
ECO:0000244|PDB:5TAM,
ECO:0000244|PDB:5TAN,
ECO:0000305|PubMed:27662087}.
METAL 3967 3967 Calcium. {ECO:0000244|PDB:5TA3,
ECO:0000244|PDB:5TAL,
ECO:0000244|PDB:5TAM,
ECO:0000244|PDB:5TAN,
ECO:0000305|PubMed:27662087}.
METAL 5001 5001 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:5TA3,
ECO:0000244|PDB:5TAL,
ECO:0000244|PDB:5TAM,
ECO:0000244|PDB:5TAN,
ECO:0000305|PubMed:27662087}.
BINDING 4716 4716 Caffeine. {ECO:0000244|PDB:5TAN,
ECO:0000305|PubMed:27662087}.
MOD_RES 1338 1338 Phosphoserine.
{ECO:0000250|UniProtKB:F1LMY4}.
MOD_RES 2345 2345 Phosphoserine.
{ECO:0000250|UniProtKB:F1LMY4}.
MOD_RES 2843 2843 Phosphoserine; by PKA and PKG.
{ECO:0000269|PubMed:8380342}.
MOD_RES 3635 3635 S-nitrosocysteine.
{ECO:0000269|PubMed:10601232,
ECO:0000269|PubMed:11562475,
ECO:0000269|PubMed:22036948}.
MOD_RES 4466 4466 Phosphothreonine.
{ECO:0000250|UniProtKB:F1LMY4}.
MOD_RES 4470 4470 Phosphoserine.
{ECO:0000250|UniProtKB:F1LMY4}.
MOD_RES 4863 4863 Phosphotyrosine.
{ECO:0000250|UniProtKB:P21817}.
MOD_RES 4866 4866 Phosphoserine.
{ECO:0000250|UniProtKB:P21817}.
MUTAGEN 164 164 R->C: Decreases threshold for channel
activation by K(+), caffeine and 4-
chloro-m-cresol. Decreases inhibition by
Mg(2+). {ECO:0000269|PubMed:12732639}.
MUTAGEN 342 342 G->R: Decreases threshold for channel
activation by K(+), caffeine and 4-
chloro-m-cresol. Decreases inhibition by
Mg(2+). {ECO:0000269|PubMed:12732639}.
MUTAGEN 615 615 R->C: Decreases threshold for channel
activation by K(+), caffeine and 4-
chloro-m-cresol. Decreases inhibition by
Mg(2+). {ECO:0000269|PubMed:12732639}.
MUTAGEN 674 675 FL->AA: Loss of interaction with FKBP1A.
{ECO:0000269|PubMed:26245150}.
MUTAGEN 760 760 N->D: Impairs interaction with FKBP1A.
{ECO:0000269|PubMed:26245150}.
MUTAGEN 1044 1044 R->C: Decreases protein stability.
{ECO:0000269|PubMed:26245150}.
MUTAGEN 1050 1050 G->S: Decreases protein stability.
{ECO:0000269|PubMed:26245150}.
MUTAGEN 1076 1076 R->W: Decreases protein stability.
{ECO:0000269|PubMed:25370123}.
MUTAGEN 2163 2163 R->C: Decreases threshold for channel
activation by K(+), caffeine and 4-
chloro-m-cresol. Decreases inhibition by
Mg(2+). {ECO:0000269|PubMed:12732639}.
MUTAGEN 2168 2168 V->M: Decreases threshold for channel
activation by K(+), caffeine and 4-
chloro-m-cresol. Decreases inhibition by
Mg(2+). {ECO:0000269|PubMed:12732639}.
MUTAGEN 2458 2458 R->H: Decreases threshold for channel
activation by K(+), caffeine and 4-
chloro-m-cresol. Decreases inhibition by
Mg(2+). {ECO:0000269|PubMed:12732639}.
MUTAGEN 2461 2461 V->G: Impairs interaction with FKBP1A.
{ECO:0000269|PubMed:26245150}.
MUTAGEN 2867 2867 L->G: Decreases protein stability.
{ECO:0000269|PubMed:22705209}.
MUTAGEN 3635 3635 C->A: Abolishes S-nitrosocysteine
formation. {ECO:0000269|PubMed:11562475,
ECO:0000269|PubMed:22036948}.
MUTAGEN 4825 4825 T->I: Decreases threshold for channel
activation by K(+), caffeine and 4-
chloro-m-cresol. Decreases inhibition by
Mg(2+). {ECO:0000269|PubMed:12732639}.
MUTAGEN 4897 4897 I->T: Loss of channel activation by
halothane and caffeine due to Ca(2+)
store depletion, probably due to constant
Ca(2+) leakage through the mutant
channel. {ECO:0000269|PubMed:10097181}.
CONFLICT 2015 2015 E -> D (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 3481 3485 Missing (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
STRAND 19 28 {ECO:0000244|PDB:4I1E}.
STRAND 31 38 {ECO:0000244|PDB:4I1E}.
STRAND 42 44 {ECO:0000244|PDB:3HSM}.
STRAND 48 51 {ECO:0000244|PDB:4I1E}.
TURN 53 57 {ECO:0000244|PDB:4I1E}.
TURN 63 65 {ECO:0000244|PDB:4I1E}.
STRAND 67 73 {ECO:0000244|PDB:4I1E}.
HELIX 75 83 {ECO:0000244|PDB:4I1E}.
STRAND 106 111 {ECO:0000244|PDB:4I1E}.
TURN 112 114 {ECO:0000244|PDB:4I1E}.
STRAND 117 120 {ECO:0000244|PDB:4I1E}.
STRAND 133 140 {ECO:0000244|PDB:4I1E}.
HELIX 144 146 {ECO:0000244|PDB:4I6I}.
STRAND 147 154 {ECO:0000244|PDB:4I1E}.
STRAND 164 166 {ECO:0000244|PDB:3ILA}.
STRAND 168 173 {ECO:0000244|PDB:4I1E}.
TURN 174 176 {ECO:0000244|PDB:4I1E}.
STRAND 179 183 {ECO:0000244|PDB:4I1E}.
STRAND 186 188 {ECO:0000244|PDB:4I8M}.
STRAND 190 196 {ECO:0000244|PDB:4I1E}.
STRAND 200 206 {ECO:0000244|PDB:4I1E}.
STRAND 219 223 {ECO:0000244|PDB:4I1E}.
STRAND 225 233 {ECO:0000244|PDB:4I1E}.
TURN 239 242 {ECO:0000244|PDB:4I1E}.
STRAND 245 250 {ECO:0000244|PDB:4I1E}.
HELIX 251 254 {ECO:0000244|PDB:4I1E}.
HELIX 256 258 {ECO:0000244|PDB:4I1E}.
STRAND 260 265 {ECO:0000244|PDB:4I1E}.
TURN 268 271 {ECO:0000244|PDB:4I1E}.
STRAND 280 284 {ECO:0000244|PDB:4I1E}.
TURN 285 287 {ECO:0000244|PDB:4I1E}.
STRAND 290 294 {ECO:0000244|PDB:4I1E}.
TURN 295 297 {ECO:0000244|PDB:4I1E}.
STRAND 298 302 {ECO:0000244|PDB:4I1E}.
HELIX 304 306 {ECO:0000244|PDB:4I1E}.
HELIX 309 312 {ECO:0000244|PDB:4I1E}.
STRAND 314 319 {ECO:0000244|PDB:4I1E}.
STRAND 332 334 {ECO:0000244|PDB:2XOA}.
TURN 341 343 {ECO:0000244|PDB:4I1E}.
STRAND 346 350 {ECO:0000244|PDB:4I1E}.
TURN 351 353 {ECO:0000244|PDB:4I1E}.
STRAND 356 359 {ECO:0000244|PDB:4I1E}.
STRAND 373 381 {ECO:0000244|PDB:4I1E}.
STRAND 388 392 {ECO:0000244|PDB:4I1E}.
HELIX 395 420 {ECO:0000244|PDB:4I1E}.
TURN 421 423 {ECO:0000244|PDB:4I1E}.
HELIX 438 451 {ECO:0000244|PDB:4I1E}.
STRAND 457 459 {ECO:0000244|PDB:4I3N}.
HELIX 461 480 {ECO:0000244|PDB:4I1E}.
HELIX 483 494 {ECO:0000244|PDB:4I1E}.
STRAND 497 499 {ECO:0000244|PDB:4I1E}.
HELIX 500 504 {ECO:0000244|PDB:4I1E}.
HELIX 509 512 {ECO:0000244|PDB:4I1E}.
HELIX 515 530 {ECO:0000244|PDB:4I1E}.
HELIX 865 867 {ECO:0000244|PDB:5C30}.
HELIX 868 888 {ECO:0000244|PDB:5C30}.
TURN 899 902 {ECO:0000244|PDB:5C30}.
HELIX 910 912 {ECO:0000244|PDB:5C30}.
HELIX 915 934 {ECO:0000244|PDB:5C30}.
STRAND 939 941 {ECO:0000244|PDB:5C30}.
HELIX 946 949 {ECO:0000244|PDB:5C30}.
HELIX 957 959 {ECO:0000244|PDB:5C30}.
HELIX 979 990 {ECO:0000244|PDB:5C30}.
STRAND 994 997 {ECO:0000244|PDB:5C30}.
TURN 998 1001 {ECO:0000244|PDB:5C30}.
STRAND 1002 1005 {ECO:0000244|PDB:5C30}.
STRAND 1021 1023 {ECO:0000244|PDB:5C30}.
HELIX 1024 1026 {ECO:0000244|PDB:5C30}.
HELIX 1029 1048 {ECO:0000244|PDB:5C30}.
STRAND 1051 1053 {ECO:0000244|PDB:5C30}.
STRAND 1073 1075 {ECO:0000244|PDB:4P9J}.
HELIX 1079 1081 {ECO:0000244|PDB:4P9J}.
STRAND 1083 1096 {ECO:0000244|PDB:4P9J}.
STRAND 1098 1105 {ECO:0000244|PDB:4P9J}.
STRAND 1121 1125 {ECO:0000244|PDB:4P9J}.
TURN 1126 1129 {ECO:0000244|PDB:4P9J}.
STRAND 1130 1140 {ECO:0000244|PDB:4P9J}.
STRAND 1148 1154 {ECO:0000244|PDB:4P9J}.
TURN 1155 1158 {ECO:0000244|PDB:4P9J}.
STRAND 1159 1164 {ECO:0000244|PDB:4P9J}.
STRAND 1178 1181 {ECO:0000244|PDB:4P9J}.
STRAND 1188 1194 {ECO:0000244|PDB:4P9J}.
STRAND 1200 1203 {ECO:0000244|PDB:4P9J}.
HELIX 1208 1210 {ECO:0000244|PDB:4P9J}.
TURN 1214 1222 {ECO:0000244|PDB:4P9J}.
HELIX 1226 1229 {ECO:0000244|PDB:4P9J}.
HELIX 1242 1244 {ECO:0000244|PDB:4P9J}.
HELIX 2749 2751 {ECO:0000244|PDB:4ESU}.
HELIX 2752 2772 {ECO:0000244|PDB:4ESU}.
TURN 2783 2786 {ECO:0000244|PDB:4ESU}.
HELIX 2794 2796 {ECO:0000244|PDB:4ESU}.
HELIX 2799 2818 {ECO:0000244|PDB:4ESU}.
STRAND 2822 2825 {ECO:0000244|PDB:4ESU}.
HELIX 2862 2864 {ECO:0000244|PDB:4ETT}.
HELIX 2869 2897 {ECO:0000244|PDB:4ESU}.
HELIX 2908 2910 {ECO:0000244|PDB:4ESU}.
HELIX 2913 2932 {ECO:0000244|PDB:4ESU}.
STRAND 2935 2938 {ECO:0000244|PDB:4ESU}.
HELIX 3617 3638 {ECO:0000244|PDB:2BCX}.
SEQUENCE 5037 AA; 565253 MW; 4ABD87AA26697070 CRC64;
MGDGGEGEDE VQFLRTDDEV VLQCSATVLK EQLKLCLAAE GFGNRLCFLE PTSNAQNVPP
DLAICCFTLE QSLSVRALQE MLANTVEAGV ESSQGGGHRT LLYGHAILLR HAHSRMYLSC
LTTSRSMTDK LAFDVGLQED ATGEACWWTM HPASKQRSEG EKVRVGDDLI LVSVSSERYL
HLSTASGELQ VDASFMQTLW NMNPICSCCE EGYVTGGHVL RLFHGHMDEC LTISAADSDD
QRRLVYYEGG AVCTHARSLW RLEPLRISWS GSHLRWGQPL RIRHVTTGRY LALTEDQGLV
VVDACKAHTK ATSFCFRVSK EKLDTAPKRD VEGMGPPEIK YGESLCFVQH VASGLWLTYA
APDPKALRLG VLKKKAILHQ EGHMDDALFL TRCQQEESQA ARMIHSTAGL YNQFIKGLDS
FSGKPRGSGP PAGPALPIEA VILSLQDLIG YFEPPSEELQ HEEKQSKLRS LRNRQSLFQE
EGMLSLVLNC IDRLNVYTTA AHFAEYAGEE AAESWKEIVN LLYELLASLI RGNRANCALF
STNLDWVVSK LDRLEASSGI LEVLYCVLIE SPEVLNIIQE NHIKSIISLL DKHGRNHKVL
DVLCSLCVCN GVAVRSNQDL ITENLLPGRE LLLQTNLINY VTSIRPNIFV GRAEGSTQYG
KWYFEVMVDE VVPFLTAQAT HLRVGWALTE GYSPYPGGGE GWGGNGVGDD LYSYGFDGLH
LWTGHVARPV TSPGQHLLAP EDVVSCCLDL SVPSISFRIN GCPVQGVFEA FNLDGLFFPV
VSFSAGVKVR FLLGGRHGEF KFLPPPGYAP CHEAVLPRER LRLEPIKEYR REGPRGPHLV
GPSRCLSHTD FVPCPVDTVQ IVLPPHLERI REKLAENIHE LWALTRIEQG WTYGPVRDDN
KRLHPCLVNF HSLPEPERNY NLQMSGETLK TLLALGCHVG MADEKAEDNL KKTKLPKTYM
MSNGYKPAPL DLSHVRLTPA QTTLVDRLAE NGHNVWARDR VAQGWSYSAV QDIPARRNPR
LVPYRLLDEA TKRSNRDSLC QAVRTLLGYG YNIEPPDQEP SQVENQSRWD RVRIFRAEKS
YTVQSGRWYF EFEAVTTGEM RVGWARPELR PDVELGADEL AYVFNGHRGQ RWHLGSEPFG
RPWQSGDVVG CMIDLTENTI IFTLNGEVLM SDSGSETAFR EIEIGDGFLP VCSLGPGQVG
HLNLGQDVSS LRFFAICGLQ EGFEPFAINM QRPVTTWFSK SLPQFEPVPP EHPHYEVARM
DGTVDTPPCL RLAHRTWGSQ NSLVEMLFLR LSLPVQFHQH FRCTAGATPL APPGLQPPAE
DEARAAEPDP DYENLRRSAG GWGEAEGGKE GTAKEGTPGG TPQPGVEAQP VRAENEKDAT
TEKNKKRGFL FKAKKAAMMT QPPATPALPR LPHDVVPADN RDDPEIILNT TTYYYSVRVF
AGQEPSCVWV GWVTPDYHQH DMNFDLSKVR AVTVTMGDEQ GNVHSSLKCS NCYMVWGGDF
VSPGQQGRIS HTDLVIGCLV DLATGLMTFT ANGKESNTFF QVEPNTKLFP AVFVLPTHQN
VIQFELGKQK NIMPLSAAMF LSERKNPAPQ CPPRLEVQML MPVSWSRMPN HFLQVETRRA
GERLGWAVQC QDPLTMMALH IPEENRCMDI LELSERLDLQ RFHSHTLRLY RAVCALGNNR
VAHALCSHVD QAQLLHALED AHLPGPLRAG YYDLLISIHL ESACRSRRSM LSEYIVPLTP
ETRAITLFPP GRKGGNARRH GLPGVGVTTS LRPPHHFSPP CFVAALPAAG VAEAPARLSP
AIPLEALRDK ALRMLGEAVR DGGQHARDPV GGSVEFQFVP VLKLVSTLLV MGIFGDEDVK
QILKMIEPEV FTEEEEEEEE EEEEEEEEEE DEEEKEEDEE EEEKEDAEKE EEEAPEGEKE
DLEEGLLQMK LPESVKLQMC NLLEYFCDQE LQHRVESLAA FAERYVDKLQ ANQRSRYALL
MRAFTMSAAE TARRTREFRS PPQEQINMLL HFKDEADEED CPLPEDIRQD LQDFHQDLLA
HCGIQLEGEE EEPEEETSLS SRLRSLLETV RLVKKKEEKP EEELPAEEKK PQSLQELVSH
MVVRWAQEDY VQSPELVRAM FSLLHRQYDG LGELLRALPR AYTISPSSVE DTMSLLECLG
QIRSLLIVQM GPQEENLMIQ SIGNIMNNKV FYQHPNLMRA LGMHETVMEV MVNVLGGGET
KEIRFPKMVT SCCRFLCYFC RISRQNQRSM FDHLSYLLEN SGIGLGMQGS TPLDVAAASV
IDNNELALAL QEQDLEKVVS YLAGCGLQSC PMLLAKGYPD IGWNPCGGER YLDFLRFAVF
VNGESVEENA NVVVRLLIRK PECFGPALRG EGGSGLLAAI EEAIRISEDP ARDGPGVRRD
RRREHFGEEP PEENRVHLGH AIMSFYAALI DLLGRCAPEM HLIQAGKGEA LRIRAILRSL
VPLDDLVGII SLPLQIPTLG KDGALVQPKM SASFVPDHKA SMVLFLDRVY GIENQDFLLH
VLDVGFLPDM RAAASLDTAT FSTTEMALAL NRYLCLAVLP LITKCAPLFA GTEHRAIMVD
SMLHTVYRLS RGRSLTKAQR DVIEDCLMAL CRYIRPSMLQ HLLRRLVFDV PILNEFAKMP
LKLLTNHYER CWKYYCLPTG WANFGVTSEE ELHLTRKLFW GIFDSLAHKK YDQELYRMAM
PCLCAIAGAL PPDYVDASYS SKAEKKATVD AEGNFDPRPV ETLNVIIPEK LDSFINKFAE
YTHEKWAFDK IQNNWSYGEN VDEELKTHPM LRPYKTFSEK DKEIYRWPIK ESLKAMIAWE
WTIEKAREGE EERTEKKKTR KISQTAQTYD PREGYNPQPP DLSGVTLSRE LQAMAEQLAE
NYHNTWGRKK KQELEAKGGG THPLLVPYDT LTAKEKARDR EKAQELLKFL QMNGYAVTRG
LKDMELDTSS IEKRFAFGFL QQLLRWMDIS QEFIAHLEAV VSSGRVEKSP HEQEIKFFAK
ILLPLINQYF TNHCLYFLST PAKVLGSGGH ASNKEKEMIT SLFCKLAALV RHRVSLFGTD
APAVVNCLHI LARSLDARTV MKSGPEIVKA GLRSFFESAS EDIEKMVENL RLGKVSQART
QVKGVGQNLT YTTVALLPVL TTLFQHIAQH QFGDDVILDD VQVSCYRTLC SIYSLGTTKN
TYVEKLRPAL GECLARLAAA MPVAFLEPQL NEYNACSVYT TKSPRERAIL GLPNSVEEMC
PDIPVLDRLM ADIGGLAESG ARYTEMPHVI EITLPMLCSY LPRWWERGPE APPPALPAGA
PPPCTAVTSD HLNSLLGNIL RIIVNNLGID EATWMKRLAV FAQPIVSRAR PELLHSHFIP
TIGRLRKRAG KVVAEEEQLR LEAKAEAEEG ELLVRDEFSV LCRDLYALYP LLIRYVDNNR
AHWLTEPNAN AEELFRMVGE IFIYWSKSHN FKREEQNFVV QNEINNMSFL TADSKSKMAK
AGDAQSGGSD QERTKKKRRG DRYSVQTSLI VATLKKMLPI GLNMCAPTDQ DLIMLAKTRY
ALKDTDEEVR EFLQNNLHLQ GKVEGSPSLR WQMALYRGLP GREEDADDPE KIVRRVQEVS
AVLYHLEQTE HPYKSKKAVW HKLLSKQRRR AVVACFRMTP LYNLPTHRAC NMFLESYKAA
WILTEDHSFE DRMIDDLSKA GEQEEEEEEV EEKKPDPLHQ LVLHFSRTAL TEKSKLDEDY
LYMAYADIMA KSCHLEEGGE NGEAEEEEVE VSFEEKEMEK QRLLYQQSRL HTRGAAEMVL
QMISACKGET GAMVSSTLKL GISILNGGNA EVQQKMLDYL KDKKEVGFFQ SIQALMQTCS
VLDLNAFERQ NKAEGLGMVN EDGTVINRQN GEKVMADDEF TQDLFRFLQL LCEGHNNDFQ
NYLRTQTGNT TTINIIICTV DYLLRLQESI SDFYWYYSGK DVIEEQGKRN FSKAMSVAKQ
VFNSLTEYIQ GPCTGNQQSL AHSRLWDAVV GFLHVFAHMM MKLAQDSSQI ELLKELLDLQ
KDMVVMLLSL LEGNVVNGMI ARQMVDMLVE SSSNVEMILK FFDMFLKLKD IVGSEAFQDY
VTDPRGLISK KDFQKAMDSQ KQFTGPEIQF LLSCSEADEN EMINFEEFAN RFQEPARDIG
FNVAVLLTNL SEHVPHDPRL RNFLELAESI LEYFRPYLGR IEIMGASRRI ERIYFEISET
NRAQWEMPQV KESKRQFIFD VVNEGGEAEK MELFVSFCED TIFEMQIAAQ ISEPEGEPEA
DEDEGMGEAA AEGAEEGAAG AEGAAGTVAA GATARLAAAA ARALRGLSYR SLRRRVRRLR
RLTAREAATA LAALLWAVVA RAGAAGAGAA AGALRLLWGS LFGGGLVEGA KKVTVTELLA
GMPDPTSDEV HGEQPAGPGG DADGAGEGEG EGDAAEGDGD EEVAGHEAGP GGAEGVVAVA
DGGPFRPEGA GGLGDMGDTT PAEPPTPEGS PILKRKLGVD GEEEELVPEP EPEPEPEPEK
ADEENGEKEE VPEAPPEPPK KAPPSPPAKK EEAGGAGMEF WGELEVQRVK FLNYLSRNFY
TLRFLALFLA FAINFILLFY KVSDSPPGED DMEGSAAGDL AGAGSGGGSG WGSGAGEEAE
GDEDENMVYY FLEESTGYME PALWCLSLLH TLVAFLCIIG YNCLKVPLVI FKREKELARK
LEFDGLYITE QPGDDDVKGQ WDRLVLNTPS FPSNYWDKFV KRKVLDKHGD IFGRERIAEL
LGMDLASLEI TAHNERKPDP PPGLLTWLMS IDVKYQIWKF GVIFTDNSFL YLGWYMVMSL
LGHYNNFFFA AHLLDIAMGV KTLRTILSSV THNGKQLVMT VGLLAVVVYL YTVVAFNFFR
KFYNKSEDED EPDMKCDDMM TCYLFHMYVG VRAGGGIGDE IEDPAGDEYE LYRVVFDITF
FFFVIVILLA IIQGLIIDAF GELRDQQEQV KEDMETKCFI CGIGSDYFDT TPHGFETHTL
EEHNLANYMF FLMYLINKDE TEHTGQESYV WKMYQERCWD FFPAGDCFRK QYEDQLS


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