GenomeNet

Database: UniProt
Entry: P11716
LinkDB: P11716
Original site: P11716 
ID   RYR1_RABIT              Reviewed;        5037 AA.
AC   P11716;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   20-DEC-2017, entry version 165.
DE   RecName: Full=Ryanodine receptor 1;
DE            Short=RYR-1;
DE            Short=RyR1;
DE   AltName: Full=Skeletal muscle calcium release channel;
DE   AltName: Full=Skeletal muscle ryanodine receptor;
DE   AltName: Full=Skeletal muscle-type ryanodine receptor;
DE   AltName: Full=Type 1 ryanodine receptor;
GN   Name=RYR1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, DOMAIN, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skeletal muscle;
RX   PubMed=2725677; DOI=10.1038/339439a0;
RA   Takeshima H., Nishimura S., Matsumoto T., Ishido H., Kangawa K.,
RA   Minamino N., Matsuo H., Ueda M., Hanaoka M., Hirose T., Numa S.;
RT   "Primary structure and expression from complementary DNA of skeletal
RT   muscle ryanodine receptor.";
RL   Nature 339:439-445(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=2298749;
RA   Zorzato F., Fujii J., Otsu K., Phillips M.S., Green N.M., Lai F.A.,
RA   Meissner G., Maclennan D.H.;
RT   "Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+
RT   release channel (ryanodine receptor) of skeletal muscle sarcoplasmic
RT   reticulum.";
RL   J. Biol. Chem. 265:2244-2256(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 3631-3650, S-NITROSYLATION AT CYS-3635, AND
RP   INTERACTION WITH CALM.
RX   PubMed=10601232; DOI=10.1074/jbc.274.52.36831;
RA   Porter Moore C., Zhang J.Z., Hamilton S.L.;
RT   "A role for cysteine 3635 of RYR1 in redox modulation and calmodulin
RT   binding.";
RL   J. Biol. Chem. 274:36831-36834(1999).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=3722165;
RA   Pessah I.N., Francini A.O., Scales D.J., Waterhouse A.L., Casida J.E.;
RT   "Calcium-ryanodine receptor complex. Solubilization and partial
RT   characterization from skeletal muscle junctional sarcoplasmic
RT   reticulum vesicles.";
RL   J. Biol. Chem. 261:8643-8648(1986).
RN   [5]
RP   PHOSPHORYLATION AT SER-2843.
RX   PubMed=8380342; DOI=10.1016/0167-4889(93)90023-I;
RA   Suko J., Maurer-Fogy I., Plank B., Bertel O., Wyskovsky W.,
RA   Hohenegger M., Hellmann G.;
RT   "Phosphorylation of serine 2843 in ryanodine receptor-calcium release
RT   channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein
RT   kinase.";
RL   Biochim. Biophys. Acta 1175:193-206(1993).
RN   [6]
RP   INTERACTION WITH FKBP1A, AND TISSUE SPECIFICITY.
RX   PubMed=7669046; DOI=10.1006/bbrc.1995.2283;
RA   Xin H.B., Timerman A.P., Onoue H., Wiederrecht G.J., Fleischer S.;
RT   "Affinity purification of the ryanodine receptor/calcium release
RT   channel from fast twitch skeletal muscle based on its tight
RT   association with FKBP12.";
RL   Biochem. Biophys. Res. Commun. 214:263-270(1995).
RN   [7]
RP   INTERACTION WITH FKBP1A.
RX   PubMed=10603943; DOI=10.1111/j.1749-6632.1998.tb08263.x;
RA   Ondrias K., Marx S.O., Gaburjakova M., Marks A.R.;
RT   "FKBP12 modulates gating of the ryanodine receptor/calcium release
RT   channel.";
RL   Ann. N. Y. Acad. Sci. 853:149-156(1998).
RN   [8]
RP   INTERACTION WITH TRDN.
RX   PubMed=9737879; DOI=10.1021/bi972803d;
RA   Ohkura M., Furukawa K., Fujimori H., Kuruma A., Kawano S., Hiraoka M.,
RA   Kuniyasu A., Nakayama H., Ohizumi Y.;
RT   "Dual regulation of the skeletal muscle ryanodine receptor by triadin
RT   and calsequestrin.";
RL   Biochemistry 37:12987-12993(1998).
RN   [9]
RP   INTERACTION WITH CACNA1S, AND FUNCTION.
RX   PubMed=10388749; DOI=10.1016/S0006-3495(99)76881-5;
RA   Dulhunty A.F., Laver D.R., Gallant E.M., Casarotto M.G., Pace S.M.,
RA   Curtis S.;
RT   "Activation and inhibition of skeletal RyR channels by a part of the
RT   skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12.";
RL   Biophys. J. 77:189-203(1999).
RN   [10]
RP   FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP   ILE-4897, AND SUBUNIT.
RX   PubMed=10097181; DOI=10.1073/pnas.96.7.4164;
RA   Lynch P.J., Tong J., Lehane M., Mallet A., Giblin L., Heffron J.J.A.,
RA   Vaughan P., Zafra G., MacLennan D.H., McCarthy T.V.;
RT   "A mutation in the transmembrane/luminal domain of the ryanodine
RT   receptor is associated with abnormal Ca(2+) release channel function
RT   and severe central core disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:4164-4169(1999).
RN   [11]
RP   S-NITROSYLATION AT CYS-3635, MUTAGENESIS OF CYS-3635, AND INTERACTION
RP   WITH CALM.
RX   PubMed=11562475; DOI=10.1073/pnas.201289098;
RA   Sun J., Xin C., Eu J.P., Stamler J.S., Meissner G.;
RT   "Cysteine-3635 is responsible for skeletal muscle ryanodine receptor
RT   modulation by NO.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:11158-11162(2001).
RN   [12]
RP   INTERACTION WITH RYR2.
RX   PubMed=12213830; DOI=10.1074/jbc.M208210200;
RA   Xiao B., Masumiya H., Jiang D., Wang R., Sei Y., Zhang L.,
RA   Murayama T., Ogawa Y., Lai F.A., Wagenknecht T., Chen S.R.;
RT   "Isoform-dependent formation of heteromeric Ca2+ release channels
RT   (ryanodine receptors).";
RL   J. Biol. Chem. 277:41778-41785(2002).
RN   [13]
RP   SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX   PubMed=12486242; DOI=10.1073/pnas.012688999;
RA   Du G.G., Sandhu B., Khanna V.K., Guo X.H., MacLennan D.H.;
RT   "Topology of the Ca2+ release channel of skeletal muscle sarcoplasmic
RT   reticulum (RyR1).";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16725-16730(2002).
RN   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, AND MUTAGENESIS OF
RP   ARG-164; GLY-342; ARG-615; ARG-2163; VAL-2168; ARG-2458 AND THR-4825.
RX   PubMed=12732639; DOI=10.1074/jbc.M302165200;
RA   Yang T., Ta T.A., Pessah I.N., Allen P.D.;
RT   "Functional defects in six ryanodine receptor isoform-1 (RyR1)
RT   mutations associated with malignant hyperthermia and their impact on
RT   skeletal excitation-contraction coupling.";
RL   J. Biol. Chem. 278:25722-25730(2003).
RN   [15]
RP   INTERACTION WITH SELENON.
RX   PubMed=18713863; DOI=10.1073/pnas.0806015105;
RA   Jurynec M.J., Xia R., Mackrill J.J., Gunther D., Crawford T.,
RA   Flanigan K.M., Abramson J.J., Howard M.T., Grunwald D.J.;
RT   "Selenoprotein N is required for ryanodine receptor calcium release
RT   channel activity in human and zebrafish muscle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:12485-12490(2008).
RN   [16]
RP   INTERACTION WITH TRDN AND ASPH.
RX   PubMed=19398037; DOI=10.1016/j.biocel.2009.04.017;
RA   Wei L., Gallant E.M., Dulhunty A.F., Beard N.A.;
RT   "Junctin and triadin each activate skeletal ryanodine receptors but
RT   junctin alone mediates functional interactions with calsequestrin.";
RL   Int. J. Biochem. Cell Biol. 41:2214-2224(2009).
RN   [17]
RP   INTERACTION WITH CACNB1.
RX   PubMed=21320436; DOI=10.1016/j.bpj.2011.01.022;
RA   Rebbeck R.T., Karunasekara Y., Gallant E.M., Board P.G., Beard N.A.,
RA   Casarotto M.G., Dulhunty A.F.;
RT   "The beta(1a) subunit of the skeletal DHPR binds to skeletal RyR1 and
RT   activates the channel via its 35-residue C-terminal tail.";
RL   Biophys. J. 100:922-930(2011).
RN   [18]
RP   FUNCTION, ENZYME REGULATION, S-NITROSYLATION AT CYS-3635, AND
RP   MUTAGENESIS OF CYS-3635.
RX   PubMed=22036948; DOI=10.1038/emboj.2011.386;
RA   Kakizawa S., Yamazawa T., Chen Y., Ito A., Murayama T., Oyamada H.,
RA   Kurebayashi N., Sato O., Watanabe M., Mori N., Oguchi K., Sakurai T.,
RA   Takeshima H., Saito N., Iino M.;
RT   "Nitric oxide-induced calcium release via ryanodine receptors
RT   regulates neuronal function.";
RL   EMBO J. 31:417-428(2012).
RN   [19]
RP   STRUCTURE BY ELECTRON MICROSCOPY (10 ANGSTROMS), SUBUNIT, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15908964; DOI=10.1038/nsmb938;
RA   Samso M., Wagenknecht T., Allen P.D.;
RT   "Internal structure and visualization of transmembrane domains of the
RT   RyR1 calcium release channel by cryo-EM.";
RL   Nat. Struct. Mol. Biol. 12:539-544(2005).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3614-3643 IN COMPLEX WITH
RP   CALM.
RX   PubMed=17027503; DOI=10.1016/j.str.2006.08.011;
RA   Maximciuc A.A., Putkey J.A., Shamoo Y., Mackenzie K.R.;
RT   "Complex of calmodulin with a ryanodine receptor target reveals a
RT   novel, flexible binding mode.";
RL   Structure 14:1547-1556(2006).
RN   [21]
RP   STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS), AND SUBUNIT.
RX   PubMed=18621707; DOI=10.1073/pnas.0803189105;
RA   Serysheva I.I., Ludtke S.J., Baker M.L., Cong Y., Topf M., Eramian D.,
RA   Sali A., Hamilton S.L., Chiu W.;
RT   "Subnanometer-resolution electron cryomicroscopy-based domain models
RT   for the cytoplasmic region of skeletal muscle RyR channel.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:9610-9615(2008).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-210.
RX   PubMed=19541610; DOI=10.1073/pnas.0905186106;
RA   Amador F.J., Liu S., Ishiyama N., Plevin M.J., Wilson A.,
RA   MacLennan D.H., Ikura M.;
RT   "Crystal structure of type I ryanodine receptor amino-terminal beta-
RT   trefoil domain reveals a disease-associated mutation 'hot spot'
RT   loop.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:11040-11044(2009).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 9-205.
RX   PubMed=19913485; DOI=10.1016/j.str.2009.08.016;
RA   Lobo P.A., Van Petegem F.;
RT   "Crystal structures of the N-terminal domains of cardiac and skeletal
RT   muscle ryanodine receptors: insights into disease mutations.";
RL   Structure 17:1505-1514(2009).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-559.
RX   PubMed=21048710; DOI=10.1038/nature09471;
RA   Tung C.C., Lobo P.A., Kimlicka L., Van Petegem F.;
RT   "The amino-terminal disease hotspot of ryanodine receptors forms a
RT   cytoplasmic vestibule.";
RL   Nature 468:585-588(2010).
RN   [25] {ECO:0000244|PDB:3RQR}
RP   X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2733-2940.
RX   PubMed=22913516; DOI=10.1111/j.1742-4658.2012.08755.x;
RA   Sharma P., Ishiyama N., Nair U., Li W., Dong A., Miyake T., Wilson A.,
RA   Ryan T., MacLennan D.H., Kislinger T., Ikura M., Dhe-Paganon S.,
RA   Gramolini A.O.;
RT   "Structural determination of the phosphorylation domain of the
RT   ryanodine receptor.";
RL   FEBS J. 279:3952-3964(2012).
RN   [26] {ECO:0000244|PDB:4ERT, ECO:0000244|PDB:4ESU, ECO:0000244|PDB:4ETU}
RP   X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 2734-2940, AND MUTAGENESIS
RP   OF LEU-2867.
RX   PubMed=22705209; DOI=10.1016/j.str.2012.04.015;
RA   Yuchi Z., Lau K., Van Petegem F.;
RT   "Disease mutations in the ryanodine receptor central region: crystal
RT   structures of a phosphorylation hot spot domain.";
RL   Structure 20:1201-1211(2012).
RN   [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}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-536.
RX   PubMed=23422674; DOI=10.1038/ncomms2501;
RA   Kimlicka L., Lau K., Tung C.C., Van Petegem F.;
RT   "Disease mutations in the ryanodine receptor N-terminal region couple
RT   to a mobile intersubunit interface.";
RL   Nat. Commun. 4:1506-1506(2013).
RN   [28] {ECO:0000244|PDB:4P9J}
RP   X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 1070-1246, AND MUTAGENESIS
RP   OF ARG-1076.
RX   PubMed=25370123; DOI=10.1038/ncomms6397;
RA   Lau K., Van Petegem F.;
RT   "Crystal structures of wild type and disease mutant forms of the
RT   ryanodine receptor SPRY2 domain.";
RL   Nat. Commun. 5:5397-5397(2014).
RN   [29] {ECO:0000244|PDB:5C30}
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 857-1054, INTERACTION WITH
RP   FKBP1A, FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF
RP   674-PHE-LEU-675; ASN-760; ARG-1044; GLY-1050 AND VAL-2461.
RX   PubMed=26245150; DOI=10.1038/ncomms8947;
RA   Yuchi Z., Yuen S.M., Lau K., Underhill A.Q., Cornea R.L.,
RA   Fessenden J.D., Van Petegem F.;
RT   "Crystal structures of ryanodine receptor SPRY1 and tandem-repeat
RT   domains reveal a critical FKBP12 binding determinant.";
RL   Nat. Commun. 6:7947-7947(2015).
RN   [30] {ECO:0000244|PDB:4UWA, ECO:0000244|PDB:4UWE}
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.10 ANGSTROMS), SUBCELLULAR
RP   LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RX   PubMed=25470059; DOI=10.1038/NATURE13916;
RA   Efremov R.G., Leitner A., Aebersold R., Raunser S.;
RT   "Architecture and conformational switch mechanism of the ryanodine
RT   receptor.";
RL   Nature 517:39-43(2015).
RN   [31] {ECO:0000244|PDB:3J8H}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) IN COMPLEX WITH
RP   FKBP1A, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY,
RP   AND DOMAIN.
RX   PubMed=25517095; DOI=10.1038/nature14063;
RA   Yan Z., Bai X.C., Yan C., Wu J., Li Z., Xie T., Peng W., Yin C.C.,
RA   Li X., Scheres S.H., Shi Y., Yan N.;
RT   "Structure of the rabbit ryanodine receptor RyR1 at near-atomic
RT   resolution.";
RL   Nature 517:50-55(2015).
RN   [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}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 12-1275;
RP   1573-2479; 2734-2939 AND 3639-5037 IN COMPLEXES WITH CALCIUM; ATP;
RP   RYANODINE AND CAFFEINE, FUNCTION, ENZYME REGULATION, SUBUNIT,
RP   SUBCELLULAR LOCATION, DOMAIN, AND TOPOLOGY.
RX   PubMed=27662087; DOI=10.1016/j.cell.2016.08.075;
RA   des Georges A., Clarke O.B., Zalk R., Yuan Q., Condon K.J.,
RA   Grassucci R.A., Hendrickson W.A., Marks A.R., Frank J.;
RT   "Structural basis for gating and activation of RyR1.";
RL   Cell 167:145-157(2016).
RN   [33] {ECO:0000244|PDB:5J8V}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), SUBUNIT,
RP   SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RX   PubMed=27573175; DOI=10.1038/cr.2016.99;
RA   Wei R., Wang X., Zhang Y., Mukherjee S., Zhang L., Chen Q., Huang X.,
RA   Jing S., Liu C., Li S., Wang G., Xu Y., Zhu S., Williams A.J., Sun F.,
RA   Yin C.C.;
RT   "Structural insights into Ca(2+)-activated long-range allosteric
RT   channel gating of RyR1.";
RL   Cell Res. 26:977-994(2016).
RN   [34] {ECO:0000244|PDB:5GKY, ECO:0000244|PDB:5GKZ, ECO:0000244|PDB:5GL0, ECO:0000244|PDB:5GL1}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) IN COMPLEX WITH
RP   FKBP1A, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY,
RP   AND DOMAIN.
RX   PubMed=27468892; DOI=10.1038/cr.2016.89;
RA   Bai X.C., Yan Z., Wu J., Li Z., Yan N.;
RT   "The central domain of RyR1 is the transducer for long-range
RT   allosteric gating of channel opening.";
RL   Cell Res. 26:995-1006(2016).
CC   -!- FUNCTION: Calcium channel that mediates the release of Ca(2+) from
CC       the sarcoplasmic reticulum into the cytoplasm and thereby plays a
CC       key role in triggering muscle contraction following depolarization
CC       of T-tubules (PubMed:3722165, PubMed:10388749, PubMed:10097181,
CC       PubMed:12732639, PubMed:22036948, PubMed:26245150,
CC       PubMed:27662087). Repeated very high-level exercise increases the
CC       open probability of the channel and leads to Ca(2+) leaking into
CC       the cytoplasm (By similarity). Can also mediate the release of
CC       Ca(2+) from intracellular stores in neurons, and may thereby
CC       promote prolonged Ca(2+) signaling in the brain. Required for
CC       normal embryonic development of muscle fibers and skeletal muscle.
CC       Required for normal heart morphogenesis, skin development and
CC       ossification during embryogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:E9PZQ0, ECO:0000269|PubMed:10388749,
CC       ECO:0000269|PubMed:12732639, ECO:0000269|PubMed:22036948,
CC       ECO:0000269|PubMed:27662087, ECO:0000305|PubMed:10097181,
CC       ECO:0000305|PubMed:26245150, ECO:0000305|PubMed:3722165}.
CC   -!- ENZYME REGULATION: Channel activity is modulated by the alkaloid
CC       ryanodine that binds to the open Ca-release channel with high
CC       affinity (PubMed:27662087). At low concentrations, ryanodine
CC       maintains the channel in an open conformation (PubMed:27662087).
CC       High ryanodine concentrations inhibit channel activity
CC       (PubMed:27662087). Channel activity is regulated by calmodulin
CC       (CALM). The calcium release is activated by increased cytoplasmic
CC       calcium levels, by nitric oxyde (NO), caffeine and ATP
CC       (PubMed:12732639, PubMed:22036948, PubMed:26245150,
CC       PubMed:27662087). Channel activity is inhibited by magnesium ions,
CC       possibly by competition for calcium binding sites
CC       (PubMed:12732639). {ECO:0000269|PubMed:12732639,
CC       ECO:0000269|PubMed:22036948, ECO:0000269|PubMed:26245150,
CC       ECO:0000269|PubMed:27662087}.
CC   -!- SUBUNIT: Homotetramer (PubMed:10097181, PubMed:15908964,
CC       PubMed:17027503, PubMed:18621707, PubMed:25470059,
CC       PubMed:25517095, PubMed:27662087, PubMed:27573175,
CC       PubMed:27468892). Can also form heterotetramers with RYR2
CC       (PubMed:12213830). Identified in a complex composed of RYR1,
CC       PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Repeated very
CC       high-level exercise decreases interaction with PDE4D and protein
CC       phosphatase 1 (PP1) (By similarity). Interacts with CALM; CALM
CC       with bound calcium inhibits the RYR1 channel activity
CC       (PubMed:10601232, PubMed:11562475, PubMed:17027503). Interacts
CC       with S100A1 (By similarity). Interacts with FKBP1A; this
CC       stabilizes the closed conformation of the channel (PubMed:7669046,
CC       PubMed:10603943, PubMed:26245150, PubMed:25517095,
CC       PubMed:27468892). Interacts with CACNA1S; interaction with CACNA1S
CC       is important for activation of the RYR1 channel (PubMed:10388749).
CC       Interacts with CACNB1 (PubMed:21320436). Interacts with TRDN and
CC       ASPH; these interactions stimulate RYR1 channel activity
CC       (PubMed:9737879, PubMed:19398037). Interacts with SELENON
CC       (PubMed:18713863). {ECO:0000250|UniProtKB:E9PZQ0,
CC       ECO:0000250|UniProtKB:P21817, ECO:0000269|PubMed:10097181,
CC       ECO:0000269|PubMed:10388749, ECO:0000269|PubMed:10601232,
CC       ECO:0000269|PubMed:10603943, ECO:0000269|PubMed:11562475,
CC       ECO:0000269|PubMed:12213830, ECO:0000269|PubMed:15908964,
CC       ECO:0000269|PubMed:17027503, ECO:0000269|PubMed:18621707,
CC       ECO:0000269|PubMed:18713863, ECO:0000269|PubMed:19398037,
CC       ECO:0000269|PubMed:21320436, ECO:0000269|PubMed:25470059,
CC       ECO:0000269|PubMed:25517095, ECO:0000269|PubMed:26245150,
CC       ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
CC       ECO:0000269|PubMed:27662087, ECO:0000269|PubMed:7669046,
CC       ECO:0000269|PubMed:9737879}.
CC   -!- INTERACTION:
CC       Self; NbExp=7; IntAct=EBI-6477441, EBI-6477441;
CC       P28652:Camk2b (xeno); NbExp=4; IntAct=EBI-6477441, EBI-397029;
CC       P62943:FKBP1A; NbExp=2; IntAct=EBI-6477441, EBI-16134925;
CC       P68106-1:FKBP1B (xeno); NbExp=2; IntAct=EBI-6477441, EBI-15766566;
CC       P02639:S100A1 (xeno); NbExp=3; IntAct=EBI-6477441, EBI-6477285;
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12486242, ECO:0000269|PubMed:25517095,
CC       ECO:0000269|PubMed:2725677, ECO:0000269|PubMed:27468892,
CC       ECO:0000269|PubMed:27573175, ECO:0000269|PubMed:27662087,
CC       ECO:0000269|PubMed:3722165}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:25470059, ECO:0000269|PubMed:25517095,
CC       ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
CC       ECO:0000269|PubMed:27662087}. Sarcoplasmic reticulum
CC       {ECO:0000269|PubMed:18713863}. Membrane
CC       {ECO:0000269|PubMed:12732639}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:25470059, ECO:0000269|PubMed:25517095,
CC       ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
CC       ECO:0000269|PubMed:27662087}. Note=The number of predicted
CC       transmembrane domains varies between orthologs, but the 3D-
CC       structures show the presence of six transmembrane regions. Both N-
CC       terminus and C-terminus are cytoplasmic.
CC       {ECO:0000269|PubMed:12486242, ECO:0000269|PubMed:25470059,
CC       ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
CC       ECO:0000269|PubMed:27662087}.
CC   -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level)
CC       (PubMed:2725677, PubMed:3722165, PubMed:25470059, PubMed:25517095,
CC       PubMed:27573175, PubMed:27468892). Fast- or slow-twitch skeletal
CC       muscle. {ECO:0000269|PubMed:15908964, ECO:0000269|PubMed:25470059,
CC       ECO:0000269|PubMed:25517095, ECO:0000269|PubMed:2725677,
CC       ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
CC       ECO:0000269|PubMed:3722165, ECO:0000269|PubMed:7669046}.
CC   -!- DOMAIN: The calcium release channel activity resides in the C-
CC       terminal region while the remaining part of the protein
CC       constitutes the 'foot' structure spanning the junctional gap
CC       between the sarcoplasmic reticulum (SR) and the T-tubule
CC       (PubMed:2725677, PubMed:25517095, PubMed:27662087,
CC       PubMed:27573175, PubMed:27468892). Pore opening is mediated via
CC       the cytoplasmic calcium-binding domains that mediate a small
CC       rotation of the channel-forming transmembrane regions that then
CC       leads to channel opening (PubMed:27468892).
CC       {ECO:0000269|PubMed:25517095, ECO:0000269|PubMed:2725677,
CC       ECO:0000269|PubMed:27468892, ECO:0000269|PubMed:27573175,
CC       ECO:0000269|PubMed:27662087}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Channel activity is modulated by phosphorylation.
CC       Phosphorylation at Ser-2843 may increase channel activity.
CC       Repeated very high-level exercise increases phosphorylation at
CC       Ser-2843. {ECO:0000250|UniProtKB:P21817}.
CC   -!- PTM: Activated by reversible S-nitrosylation (PubMed:22036948).
CC       Repeated very high-level exercise increases S-nitrosylation (By
CC       similarity). {ECO:0000250|UniProtKB:P21817,
CC       ECO:0000269|PubMed:22036948}.
CC   -!- MISCELLANEOUS: Coexpression of normal and mutant Thr-4897 RYR1 in
CC       a 1:1 ratio produces RYR1 channels with normal halothane and
CC       caffeine sensitivities, but maximal levels of Ca(2+) release are
CC       reduced by 67%. Binding of [3H]ryanodine indicates that the
CC       heterozygous channel is activated by Ca(2+) concentrations 4-fold
CC       lower than normal. Single-cell analysis of cotransfected cells
CC       shows a significantly increased resting cytoplasmic Ca(2+) level
CC       and a significantly reduced luminal Ca(2+) level. These data
CC       indicated a leaky channel, possibly caused by a reduction in the
CC       Ca(2+) concentration required for channel activation.
CC       {ECO:0000269|PubMed:10097181}.
CC   -!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family.
CC       RYR1 subfamily. {ECO:0000305}.
DR   EMBL; X15209; CAA33279.1; -; mRNA.
DR   EMBL; X15750; CAA33762.1; -; mRNA.
DR   PIR; S04654; B35041.
DR   RefSeq; NP_001095188.1; NM_001101718.1.
DR   UniGene; Ocu.2092; -.
DR   PDB; 2BCX; X-ray; 2.00 A; B=3614-3643.
DR   PDB; 2XOA; X-ray; 2.50 A; A=1-559.
DR   PDB; 3HSM; X-ray; 2.50 A; A/B=1-210.
DR   PDB; 3ILA; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I=9-205.
DR   PDB; 3J8H; EM; 3.80 A; A/C/E/G=1-5037.
DR   PDB; 3RQR; X-ray; 2.16 A; A=2733-2940.
DR   PDB; 4ERT; X-ray; 1.95 A; A=2734-2940.
DR   PDB; 4ESU; X-ray; 1.59 A; A=2734-2940.
DR   PDB; 4ETT; X-ray; 2.20 A; A=2734-2940.
DR   PDB; 4ETU; X-ray; 2.19 A; A=2734-2938.
DR   PDB; 4I0Y; X-ray; 2.80 A; A=1-536.
DR   PDB; 4I1E; X-ray; 2.40 A; A=1-536.
DR   PDB; 4I2S; X-ray; 2.50 A; A=1-536.
DR   PDB; 4I37; X-ray; 2.95 A; A=1-536.
DR   PDB; 4I3N; X-ray; 2.95 A; A=1-536.
DR   PDB; 4I6I; X-ray; 2.50 A; A=1-559.
DR   PDB; 4I7I; X-ray; 2.90 A; A=1-536.
DR   PDB; 4I8M; X-ray; 2.80 A; A=1-536.
DR   PDB; 4I96; X-ray; 2.73 A; A=217-536.
DR   PDB; 4P9J; X-ray; 1.84 A; A/B/C=1070-1246.
DR   PDB; 4UWA; EM; 6.10 A; A/B/C/D=1-5037.
DR   PDB; 4UWE; EM; 8.50 A; A/B/C/D=1-5037.
DR   PDB; 5C30; X-ray; 1.55 A; A=857-1054.
DR   PDB; 5GKY; EM; 3.80 A; A/C/E/G=1-5037.
DR   PDB; 5GKZ; EM; 4.00 A; A/C/E/G=1-5037.
DR   PDB; 5GL0; EM; 4.20 A; A/C/E/G=1-5037.
DR   PDB; 5GL1; EM; 5.70 A; A/C/E/G=1-5037.
DR   PDB; 5J8V; EM; 4.90 A; A/B/C/D=1-5037.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   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.
DR   PDB; 5TB0; EM; 3.80 A; B/E/G/I=1-5037.
DR   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.
DR   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.
DR   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.
DR   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.
DR   PDBsum; 2BCX; -.
DR   PDBsum; 2XOA; -.
DR   PDBsum; 3HSM; -.
DR   PDBsum; 3ILA; -.
DR   PDBsum; 3J8H; -.
DR   PDBsum; 3RQR; -.
DR   PDBsum; 4ERT; -.
DR   PDBsum; 4ESU; -.
DR   PDBsum; 4ETT; -.
DR   PDBsum; 4ETU; -.
DR   PDBsum; 4I0Y; -.
DR   PDBsum; 4I1E; -.
DR   PDBsum; 4I2S; -.
DR   PDBsum; 4I37; -.
DR   PDBsum; 4I3N; -.
DR   PDBsum; 4I6I; -.
DR   PDBsum; 4I7I; -.
DR   PDBsum; 4I8M; -.
DR   PDBsum; 4I96; -.
DR   PDBsum; 4P9J; -.
DR   PDBsum; 4UWA; -.
DR   PDBsum; 4UWE; -.
DR   PDBsum; 5C30; -.
DR   PDBsum; 5GKY; -.
DR   PDBsum; 5GKZ; -.
DR   PDBsum; 5GL0; -.
DR   PDBsum; 5GL1; -.
DR   PDBsum; 5J8V; -.
DR   PDBsum; 5T15; -.
DR   PDBsum; 5T9M; -.
DR   PDBsum; 5T9N; -.
DR   PDBsum; 5T9R; -.
DR   PDBsum; 5T9S; -.
DR   PDBsum; 5T9V; -.
DR   PDBsum; 5TA3; -.
DR   PDBsum; 5TAL; -.
DR   PDBsum; 5TAM; -.
DR   PDBsum; 5TAN; -.
DR   PDBsum; 5TAP; -.
DR   PDBsum; 5TAQ; -.
DR   PDBsum; 5TAS; -.
DR   PDBsum; 5TAT; -.
DR   PDBsum; 5TAU; -.
DR   PDBsum; 5TAV; -.
DR   PDBsum; 5TAW; -.
DR   PDBsum; 5TAX; -.
DR   PDBsum; 5TAY; -.
DR   PDBsum; 5TAZ; -.
DR   PDBsum; 5TB0; -.
DR   PDBsum; 5TB1; -.
DR   PDBsum; 5TB2; -.
DR   PDBsum; 5TB3; -.
DR   PDBsum; 5TB4; -.
DR   ProteinModelPortal; P11716; -.
DR   SMR; P11716; -.
DR   DIP; DIP-41872N; -.
DR   IntAct; P11716; 8.
DR   MINT; MINT-158193; -.
DR   BindingDB; P11716; -.
DR   ChEMBL; CHEMBL3288; -.
DR   iPTMnet; P11716; -.
DR   SwissPalm; P11716; -.
DR   PRIDE; P11716; -.
DR   GeneID; 100009540; -.
DR   KEGG; ocu:100009540; -.
DR   CTD; 6261; -.
DR   HOVERGEN; HBG006699; -.
DR   InParanoid; P11716; -.
DR   KO; K04961; -.
DR   EvolutionaryTrace; P11716; -.
DR   PRO; PR:P11716; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0031301; C:integral component of organelle membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:AgBase.
DR   GO; GO:1990425; C:ryanodine receptor complex; IDA:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0014802; C:terminal cisterna; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0035381; F:ATP-gated ion channel activity; IDA:CAFA.
DR   GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0015278; F:calcium-release channel activity; IMP:AgBase.
DR   GO; GO:0005516; F:calmodulin binding; IDA:BHF-UCL.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR   GO; GO:0008144; F:drug binding; IDA:AgBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
DR   GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IDA:UniProtKB.
DR   GO; GO:0015643; F:toxic substance binding; IDA:AgBase.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0071313; P:cellular response to caffeine; IDA:UniProtKB.
DR   GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
DR   GO; GO:0043931; P:ossification involved in bone maturation; ISS:UniProtKB.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISS:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:CAFA.
DR   GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:UniProtKB.
DR   GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
DR   GO; GO:0043588; P:skin development; ISS:UniProtKB.
DR   CDD; cd12877; SPRY1_RyR; 1.
DR   CDD; cd12878; SPRY2_RyR; 1.
DR   CDD; cd12879; SPRY3_RyR; 1.
DR   Gene3D; 1.25.10.30; -; 2.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR035910; IP3R_RIH_dom_sf.
DR   InterPro; IPR036300; MIR_dom_sf.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR013662; RIH_assoc-dom.
DR   InterPro; IPR000699; RIH_dom.
DR   InterPro; IPR013333; Ryan_recept.
DR   InterPro; IPR003032; Ryanodine_rcpt.
DR   InterPro; IPR015925; Ryanodine_recept-rel.
DR   InterPro; IPR009460; Ryanrecept_TM4-6.
DR   InterPro; IPR033215; RyR1.
DR   InterPro; IPR035761; SPRY1_RyR.
DR   InterPro; IPR035764; SPRY2_RyR.
DR   InterPro; IPR035762; SPRY3_RyR.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR13715; PTHR13715; 1.
DR   PANTHER; PTHR13715:SF15; PTHR13715:SF15; 1.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   Pfam; PF08709; Ins145_P3_rec; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF08454; RIH_assoc; 1.
DR   Pfam; PF06459; RR_TM4-6; 1.
DR   Pfam; PF01365; RYDR_ITPR; 2.
DR   Pfam; PF02026; RyR; 4.
DR   Pfam; PF00622; SPRY; 3.
DR   PRINTS; PR00795; RYANODINER.
DR   SMART; SM00472; MIR; 4.
DR   SMART; SM00449; SPRY; 3.
DR   SUPFAM; SSF100909; SSF100909; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF49899; SSF49899; 3.
DR   SUPFAM; SSF82109; SSF82109; 2.
DR   PROSITE; PS50188; B302_SPRY; 3.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Calcium; Calcium channel;
KW   Calcium transport; Calmodulin-binding; Complete proteome;
KW   Developmental protein; Direct protein sequencing; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; S-nitrosylation; Sarcoplasmic reticulum; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   5037       Ryanodine receptor 1.
FT                                /FTId=PRO_0000219360.
FT   TOPO_DOM      1   4558       Cytoplasmic.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TRANSMEM   4559   4579       Helical; Name=1.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TOPO_DOM   4580   4640       Lumenal. {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TRANSMEM   4641   4661       Helical; Name=2.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TOPO_DOM   4662   4779       Cytoplasmic.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TRANSMEM   4780   4802       Helical; Name=3.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TOPO_DOM   4803   4803       Lumenal. {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TRANSMEM   4804   4820       Helical; Name=4.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TOPO_DOM   4821   4835       Cytoplasmic.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TRANSMEM   4836   4856       Helical; Name=5.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TOPO_DOM   4857   4879       Lumenal. {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   INTRAMEM   4880   4899       Pore-forming.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TOPO_DOM   4900   4919       Lumenal. {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TRANSMEM   4920   4940       Helical; Name=6.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   TOPO_DOM   4941   5037       Cytoplasmic.
FT                                {ECO:0000269|PubMed:25470059,
FT                                ECO:0000269|PubMed:25517095,
FT                                ECO:0000269|PubMed:27468892,
FT                                ECO:0000269|PubMed:27573175}.
FT   DOMAIN       98    153       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      160    205       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      211    265       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      271    334       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      336    394       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      582    798       B30.2/SPRY 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT      842    955       1.
FT   REPEAT      956   1069       2.
FT   DOMAIN     1014   1209       B30.2/SPRY 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT     1345   1360       3; truncated.
FT   DOMAIN     1358   1571       B30.2/SPRY 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT     1373   1388       4; truncated.
FT   REPEAT     2726   2845       5.
FT   REPEAT     2846   2959       6.
FT   DOMAIN     4075   4103       EF-hand. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448,
FT                                ECO:0000269|PubMed:27573175}.
FT   NP_BIND    4211   4215       ATP. {ECO:0000244|PDB:5T9V,
FT                                ECO:0000244|PDB:5TA3,
FT                                ECO:0000244|PDB:5TAL,
FT                                ECO:0000244|PDB:5TAM,
FT                                ECO:0000244|PDB:5TAN,
FT                                ECO:0000244|PDB:5TAS,
FT                                ECO:0000244|PDB:5TAT,
FT                                ECO:0000244|PDB:5TAU,
FT                                ECO:0000305|PubMed:27662087}.
FT   NP_BIND    4954   4959       ATP. {ECO:0000244|PDB:5T9V,
FT                                ECO:0000244|PDB:5TA3,
FT                                ECO:0000244|PDB:5TAL,
FT                                ECO:0000244|PDB:5TAM,
FT                                ECO:0000244|PDB:5TAN,
FT                                ECO:0000244|PDB:5TAS,
FT                                ECO:0000244|PDB:5TAT,
FT                                ECO:0000244|PDB:5TAU,
FT                                ECO:0000305|PubMed:27662087}.
FT   NP_BIND    4979   4985       ATP. {ECO:0000244|PDB:5T9V,
FT                                ECO:0000244|PDB:5TA3,
FT                                ECO:0000244|PDB:5TAL,
FT                                ECO:0000244|PDB:5TAM,
FT                                ECO:0000244|PDB:5TAN,
FT                                ECO:0000244|PDB:5TAS,
FT                                ECO:0000244|PDB:5TAT,
FT                                ECO:0000244|PDB:5TAU,
FT                                ECO:0000305|PubMed:27662087}.
FT   REGION      670    681       Interaction with FKBP1A.
FT                                {ECO:0000269|PubMed:26245150}.
FT   REGION      842   2959       6 X approximate repeats.
FT   REGION     3614   3643       Interaction with CALM.
FT   MOTIF      4894   4900       Selectivity filter.
FT                                {ECO:0000305|PubMed:25517095,
FT                                ECO:0000305|PubMed:27573175,
FT                                ECO:0000305|PubMed:27662087}.
FT   COMPBIAS   1873   1913       Glu-rich (acidic).
FT   METAL      3893   3893       Calcium. {ECO:0000244|PDB:5TA3,
FT                                ECO:0000244|PDB:5TAL,
FT                                ECO:0000244|PDB:5TAM,
FT                                ECO:0000244|PDB:5TAN,
FT                                ECO:0000305|PubMed:27662087}.
FT   METAL      3967   3967       Calcium. {ECO:0000244|PDB:5TA3,
FT                                ECO:0000244|PDB:5TAL,
FT                                ECO:0000244|PDB:5TAM,
FT                                ECO:0000244|PDB:5TAN,
FT                                ECO:0000305|PubMed:27662087}.
FT   METAL      5001   5001       Calcium; via carbonyl oxygen.
FT                                {ECO:0000244|PDB:5TA3,
FT                                ECO:0000244|PDB:5TAL,
FT                                ECO:0000244|PDB:5TAM,
FT                                ECO:0000244|PDB:5TAN,
FT                                ECO:0000305|PubMed:27662087}.
FT   BINDING    4716   4716       Caffeine. {ECO:0000244|PDB:5TAN,
FT                                ECO:0000305|PubMed:27662087}.
FT   MOD_RES    1338   1338       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    2345   2345       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    2843   2843       Phosphoserine; by PKA and PKG.
FT                                {ECO:0000269|PubMed:8380342}.
FT   MOD_RES    3635   3635       S-nitrosocysteine.
FT                                {ECO:0000269|PubMed:10601232,
FT                                ECO:0000269|PubMed:11562475,
FT                                ECO:0000269|PubMed:22036948}.
FT   MOD_RES    4466   4466       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    4470   4470       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    4863   4863       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P21817}.
FT   MOD_RES    4866   4866       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P21817}.
FT   MUTAGEN     164    164       R->C: Decreases threshold for channel
FT                                activation by K(+), caffeine and 4-
FT                                chloro-m-cresol. Decreases inhibition by
FT                                Mg(2+). {ECO:0000269|PubMed:12732639}.
FT   MUTAGEN     342    342       G->R: Decreases threshold for channel
FT                                activation by K(+), caffeine and 4-
FT                                chloro-m-cresol. Decreases inhibition by
FT                                Mg(2+). {ECO:0000269|PubMed:12732639}.
FT   MUTAGEN     615    615       R->C: Decreases threshold for channel
FT                                activation by K(+), caffeine and 4-
FT                                chloro-m-cresol. Decreases inhibition by
FT                                Mg(2+). {ECO:0000269|PubMed:12732639}.
FT   MUTAGEN     674    675       FL->AA: Loss of interaction with FKBP1A.
FT                                {ECO:0000269|PubMed:26245150}.
FT   MUTAGEN     760    760       N->D: Impairs interaction with FKBP1A.
FT                                {ECO:0000269|PubMed:26245150}.
FT   MUTAGEN    1044   1044       R->C: Decreases protein stability.
FT                                {ECO:0000269|PubMed:26245150}.
FT   MUTAGEN    1050   1050       G->S: Decreases protein stability.
FT                                {ECO:0000269|PubMed:26245150}.
FT   MUTAGEN    1076   1076       R->W: Decreases protein stability.
FT                                {ECO:0000269|PubMed:25370123}.
FT   MUTAGEN    2163   2163       R->C: Decreases threshold for channel
FT                                activation by K(+), caffeine and 4-
FT                                chloro-m-cresol. Decreases inhibition by
FT                                Mg(2+). {ECO:0000269|PubMed:12732639}.
FT   MUTAGEN    2168   2168       V->M: Decreases threshold for channel
FT                                activation by K(+), caffeine and 4-
FT                                chloro-m-cresol. Decreases inhibition by
FT                                Mg(2+). {ECO:0000269|PubMed:12732639}.
FT   MUTAGEN    2458   2458       R->H: Decreases threshold for channel
FT                                activation by K(+), caffeine and 4-
FT                                chloro-m-cresol. Decreases inhibition by
FT                                Mg(2+). {ECO:0000269|PubMed:12732639}.
FT   MUTAGEN    2461   2461       V->G: Impairs interaction with FKBP1A.
FT                                {ECO:0000269|PubMed:26245150}.
FT   MUTAGEN    2867   2867       L->G: Decreases protein stability.
FT                                {ECO:0000269|PubMed:22705209}.
FT   MUTAGEN    3635   3635       C->A: Abolishes S-nitrosocysteine
FT                                formation. {ECO:0000269|PubMed:11562475,
FT                                ECO:0000269|PubMed:22036948}.
FT   MUTAGEN    4825   4825       T->I: Decreases threshold for channel
FT                                activation by K(+), caffeine and 4-
FT                                chloro-m-cresol. Decreases inhibition by
FT                                Mg(2+). {ECO:0000269|PubMed:12732639}.
FT   MUTAGEN    4897   4897       I->T: Loss of channel activation by
FT                                halothane and caffeine due to Ca(2+)
FT                                store depletion, probably due to constant
FT                                Ca(2+) leakage through the mutant
FT                                channel. {ECO:0000269|PubMed:10097181}.
FT   CONFLICT   2015   2015       E -> D (in Ref. 2; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT   3481   3485       Missing (in Ref. 2; no nucleotide entry).
FT                                {ECO:0000305}.
FT   STRAND       19     28       {ECO:0000244|PDB:4I1E}.
FT   STRAND       31     38       {ECO:0000244|PDB:4I1E}.
FT   STRAND       42     44       {ECO:0000244|PDB:3HSM}.
FT   STRAND       48     51       {ECO:0000244|PDB:4I1E}.
FT   TURN         53     57       {ECO:0000244|PDB:4I1E}.
FT   TURN         63     65       {ECO:0000244|PDB:4I1E}.
FT   STRAND       67     73       {ECO:0000244|PDB:4I1E}.
FT   HELIX        75     83       {ECO:0000244|PDB:4I1E}.
FT   STRAND      106    111       {ECO:0000244|PDB:4I1E}.
FT   TURN        112    114       {ECO:0000244|PDB:4I1E}.
FT   STRAND      117    120       {ECO:0000244|PDB:4I1E}.
FT   STRAND      133    140       {ECO:0000244|PDB:4I1E}.
FT   HELIX       144    146       {ECO:0000244|PDB:4I6I}.
FT   STRAND      147    154       {ECO:0000244|PDB:4I1E}.
FT   STRAND      164    166       {ECO:0000244|PDB:3ILA}.
FT   STRAND      168    173       {ECO:0000244|PDB:4I1E}.
FT   TURN        174    176       {ECO:0000244|PDB:4I1E}.
FT   STRAND      179    183       {ECO:0000244|PDB:4I1E}.
FT   STRAND      186    188       {ECO:0000244|PDB:4I8M}.
FT   STRAND      190    196       {ECO:0000244|PDB:4I1E}.
FT   STRAND      200    206       {ECO:0000244|PDB:4I1E}.
FT   STRAND      219    223       {ECO:0000244|PDB:4I1E}.
FT   STRAND      225    233       {ECO:0000244|PDB:4I1E}.
FT   TURN        239    242       {ECO:0000244|PDB:4I1E}.
FT   STRAND      245    250       {ECO:0000244|PDB:4I1E}.
FT   HELIX       251    254       {ECO:0000244|PDB:4I1E}.
FT   HELIX       256    258       {ECO:0000244|PDB:4I1E}.
FT   STRAND      260    265       {ECO:0000244|PDB:4I1E}.
FT   TURN        268    271       {ECO:0000244|PDB:4I1E}.
FT   STRAND      280    284       {ECO:0000244|PDB:4I1E}.
FT   TURN        285    287       {ECO:0000244|PDB:4I1E}.
FT   STRAND      290    294       {ECO:0000244|PDB:4I1E}.
FT   TURN        295    297       {ECO:0000244|PDB:4I1E}.
FT   STRAND      298    302       {ECO:0000244|PDB:4I1E}.
FT   HELIX       304    306       {ECO:0000244|PDB:4I1E}.
FT   HELIX       309    312       {ECO:0000244|PDB:4I1E}.
FT   STRAND      314    319       {ECO:0000244|PDB:4I1E}.
FT   STRAND      332    334       {ECO:0000244|PDB:2XOA}.
FT   TURN        341    343       {ECO:0000244|PDB:4I1E}.
FT   STRAND      346    350       {ECO:0000244|PDB:4I1E}.
FT   TURN        351    353       {ECO:0000244|PDB:4I1E}.
FT   STRAND      356    359       {ECO:0000244|PDB:4I1E}.
FT   STRAND      373    381       {ECO:0000244|PDB:4I1E}.
FT   STRAND      388    392       {ECO:0000244|PDB:4I1E}.
FT   HELIX       395    420       {ECO:0000244|PDB:4I1E}.
FT   TURN        421    423       {ECO:0000244|PDB:4I1E}.
FT   HELIX       438    451       {ECO:0000244|PDB:4I1E}.
FT   HELIX       461    480       {ECO:0000244|PDB:4I1E}.
FT   HELIX       483    494       {ECO:0000244|PDB:4I1E}.
FT   STRAND      497    499       {ECO:0000244|PDB:4I1E}.
FT   HELIX       500    504       {ECO:0000244|PDB:4I1E}.
FT   HELIX       509    512       {ECO:0000244|PDB:4I1E}.
FT   HELIX       515    530       {ECO:0000244|PDB:4I1E}.
FT   HELIX       865    867       {ECO:0000244|PDB:5C30}.
FT   HELIX       868    888       {ECO:0000244|PDB:5C30}.
FT   TURN        899    902       {ECO:0000244|PDB:5C30}.
FT   HELIX       910    912       {ECO:0000244|PDB:5C30}.
FT   HELIX       915    934       {ECO:0000244|PDB:5C30}.
FT   STRAND      939    941       {ECO:0000244|PDB:5C30}.
FT   HELIX       946    949       {ECO:0000244|PDB:5C30}.
FT   HELIX       957    959       {ECO:0000244|PDB:5C30}.
FT   HELIX       979    990       {ECO:0000244|PDB:5C30}.
FT   STRAND      994    997       {ECO:0000244|PDB:5C30}.
FT   TURN        998   1001       {ECO:0000244|PDB:5C30}.
FT   STRAND     1002   1005       {ECO:0000244|PDB:5C30}.
FT   STRAND     1021   1023       {ECO:0000244|PDB:5C30}.
FT   HELIX      1024   1026       {ECO:0000244|PDB:5C30}.
FT   HELIX      1029   1048       {ECO:0000244|PDB:5C30}.
FT   STRAND     1051   1053       {ECO:0000244|PDB:5C30}.
FT   STRAND     1073   1075       {ECO:0000244|PDB:4P9J}.
FT   HELIX      1079   1081       {ECO:0000244|PDB:4P9J}.
FT   STRAND     1083   1096       {ECO:0000244|PDB:4P9J}.
FT   STRAND     1098   1105       {ECO:0000244|PDB:4P9J}.
FT   STRAND     1121   1125       {ECO:0000244|PDB:4P9J}.
FT   TURN       1126   1129       {ECO:0000244|PDB:4P9J}.
FT   STRAND     1130   1140       {ECO:0000244|PDB:4P9J}.
FT   STRAND     1148   1154       {ECO:0000244|PDB:4P9J}.
FT   TURN       1155   1158       {ECO:0000244|PDB:4P9J}.
FT   STRAND     1159   1164       {ECO:0000244|PDB:4P9J}.
FT   STRAND     1178   1181       {ECO:0000244|PDB:4P9J}.
FT   STRAND     1188   1194       {ECO:0000244|PDB:4P9J}.
FT   STRAND     1200   1203       {ECO:0000244|PDB:4P9J}.
FT   HELIX      1208   1210       {ECO:0000244|PDB:4P9J}.
FT   TURN       1214   1222       {ECO:0000244|PDB:4P9J}.
FT   HELIX      1226   1229       {ECO:0000244|PDB:4P9J}.
FT   HELIX      1242   1244       {ECO:0000244|PDB:4P9J}.
FT   HELIX      2749   2751       {ECO:0000244|PDB:4ESU}.
FT   HELIX      2752   2772       {ECO:0000244|PDB:4ESU}.
FT   TURN       2783   2786       {ECO:0000244|PDB:4ESU}.
FT   HELIX      2794   2796       {ECO:0000244|PDB:4ESU}.
FT   HELIX      2799   2818       {ECO:0000244|PDB:4ESU}.
FT   STRAND     2822   2825       {ECO:0000244|PDB:4ESU}.
FT   HELIX      2862   2864       {ECO:0000244|PDB:4ETT}.
FT   HELIX      2869   2897       {ECO:0000244|PDB:4ESU}.
FT   HELIX      2908   2910       {ECO:0000244|PDB:4ESU}.
FT   HELIX      2913   2932       {ECO:0000244|PDB:4ESU}.
FT   STRAND     2935   2938       {ECO:0000244|PDB:4ESU}.
FT   HELIX      3617   3638       {ECO:0000244|PDB:2BCX}.
SQ   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
//
DBGET integrated database retrieval system