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

 RYR2_RAT                Reviewed;        4953 AA.
B0LPN4; D7UNT3;
22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
22-FEB-2012, sequence version 2.
25-OCT-2017, entry version 85.
RecName: Full=Ryanodine receptor 2;
Short=RYR-2;
Short=RyR2;
AltName: Full=Cardiac muscle ryanodine receptor;
AltName: Full=Cardiac muscle ryanodine receptor-calcium release channel;
AltName: Full=Type 2 ryanodine receptor;
Name=Ryr2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Cerebral artery;
PubMed=20445169; DOI=10.1152/ajpcell.00318.2009;
Vaithianathan T., Narayanan D., Asuncion-Chin M.T., Jeyakumar L.H.,
Liu J., Fleischer S., Jaggar J.H., Dopico A.M.;
"Subtype identification and functional characterization of ryanodine
receptors in rat cerebral artery myocytes.";
Am. J. Physiol. 299:C264-C278(2010).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Pancreatic islet;
PubMed=20471962; DOI=10.1016/j.bbrc.2010.05.051;
Takasawa S., Kuroki M., Nata K., Noguchi N., Ikeda T., Yamauchi A.,
Ota H., Itaya-Hironaka A., Sakuramoto-Tsuchida S., Takahashi I.,
Yoshikawa T., Shimosegawa T., Okamoto H.;
"A novel ryanodine receptor expressed in pancreatic islets by
alternative splicing from type 2 ryanodine receptor gene.";
Biochem. Biophys. Res. Commun. 397:140-145(2010).
[3]
PHOSPHORYLATION AT SER-2798 AND SER-2804, AND TISSUE SPECIFICITY.
PubMed=18755143; DOI=10.1016/j.bbrc.2008.08.084;
Huke S., Bers D.M.;
"Ryanodine receptor phosphorylation at serine 2030, 2808 and 2814 in
rat cardiomyocytes.";
Biochem. Biophys. Res. Commun. 376:80-85(2008).
[4]
FUNCTION, INTERACTION WITH FKBP1A AND FKBP1B, AND TISSUE SPECIFICITY.
PubMed=20431056; DOI=10.1161/CIRCRESAHA.110.219816;
Guo T., Cornea R.L., Huke S., Camors E., Yang Y., Picht E.,
Fruen B.R., Bers D.M.;
"Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized
cardiac myocytes and effects on Ca sparks.";
Circ. Res. 106:1743-1752(2010).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1334; SER-1863;
SER-2021; SER-2687; SER-2798; SER-2801 AND SER-2804, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
STRUCTURE BY NMR OF 3561-3572 IN COMPLEX WITH S100A1, AND INTERACTION
WITH CALM AND S100A1.
PubMed=18650434; DOI=10.1074/jbc.M804432200;
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
Weber D.J.;
"S100A1 and calmodulin compete for the same binding site on ryanodine
receptor.";
J. Biol. Chem. 283:26676-26683(2008).
-!- FUNCTION: Calcium channel that mediates the release of Ca(2+) from
the sarcoplasmic reticulum into the cytoplasm and thereby plays a
key role in triggering cardiac muscle contraction. Aberrant
channel activation can lead to cardiac arrhythmia. In cardiac
myocytes, calcium release is triggered by increased Ca(2+) levels
due to activation of the L-type calcium channel CACNA1C. The
calcium channel activity is modulated by formation of
heterotetramers with RYR3. Required for cellular calcium ion
homeostasis. Required for embryonic heart development (By
similarity). {ECO:0000250, ECO:0000269|PubMed:20431056,
ECO:0000269|PubMed:20471962}.
-!- SUBUNIT: Homotetramer. Can also form heterotetramers with RYR3.
Identified in a complex composed of RYR2, FKBP1B, PKA catalytic
subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and
PP1. Interacts directly with FKBP1B, PKA, PP1 and PP2A (By
similarity). Interacts with FKBP1A and FKBP1B; these interactions
may stabilize the channel in its closed state and prevent Ca(2+)
leaks. Interacts with CALM and S100A1; these interactions regulate
channel activity. Interacts with SELENON (By similarity).
{ECO:0000250|UniProtKB:P30957, ECO:0000250|UniProtKB:Q92736,
ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:20431056}.
-!- INTERACTION:
P62161:Calm3; NbExp=2; IntAct=EBI-6694167, EBI-397530;
-!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Membrane
{ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P30957}. Note=The
number of predicted transmembrane domains varies between
orthologs, but both N-terminus and C-terminus seem to be
cytoplasmic. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=B0LPN4-1; Sequence=Displayed;
Name=2;
IsoId=B0LPN4-2; Sequence=VSP_042299, VSP_042300;
-!- TISSUE SPECIFICITY: Detected in heart muscle myocytes (at protein
level). Widely expressed. Detected in heart muscle and cerebral
artery smooth muscle. Detected in pancreatic islet cells.
{ECO:0000269|PubMed:18755143, ECO:0000269|PubMed:20431056,
ECO:0000269|PubMed:20445169, ECO:0000269|PubMed:20471962}.
-!- DOMAIN: The calcium release channel activity resides in the C-
terminal region while the remaining part of the protein resides in
the cytoplasm. {ECO:0000305}.
-!- PTM: Channel activity is modulated by phosphorylation.
Phosphorylation at Ser-2798 and Ser-2804 increases the open
probability of the calcium channel. Phosphorylation is increased
in failing heart, leading to calcium leaks and increased
cytoplasmic Ca(2+) levels (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-2021 by PKA enhances the response to
lumenal calcium. {ECO:0000250}.
-!- MISCELLANEOUS: Channel activity is modulated by the alkaloid
ryanodine that binds to the open Ca-release channel with high
affinity. At low concentrations, ryanodine maintains the channel
in an open conformation. High ryanodine concentrations inhibit
channel activity. Channel activity is regulated by calmodulin
(CALM). The calcium release is activated by increased cytoplasmic
calcium levels, by nitric oxyde (NO), caffeine and ATP. Channel
activity is inhibited by magnesium ions, possibly by competition
for calcium binding sites (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family.
RYR2 subfamily. {ECO:0000305}.
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EMBL; EU346200; ABY79796.1; -; mRNA.
EMBL; AB204523; BAJ10276.1; -; mRNA.
RefSeq; NP_001177972.1; NM_001191043.1.
RefSeq; NP_114467.1; NM_032078.2.
UniGene; Rn.20442; -.
PDB; 2K2F; NMR; -; C/D=3561-3572.
PDBsum; 2K2F; -.
SMR; B0LPN4; -.
BioGrid; 604379; 1.
CORUM; B0LPN4; -.
IntAct; B0LPN4; 1.
STRING; 10116.ENSRNOP00000059019; -.
BindingDB; B0LPN4; -.
ChEMBL; CHEMBL3388; -.
iPTMnet; B0LPN4; -.
PhosphoSitePlus; B0LPN4; -.
PaxDb; B0LPN4; -.
PeptideAtlas; B0LPN4; -.
PRIDE; B0LPN4; -.
GeneID; 689560; -.
KEGG; rno:689560; -.
CTD; 6262; -.
RGD; 620314; Ryr2.
eggNOG; KOG2243; Eukaryota.
eggNOG; ENOG410YCNW; LUCA.
HOGENOM; HOG000231428; -.
HOVERGEN; HBG006699; -.
InParanoid; B0LPN4; -.
KO; K04962; -.
EvolutionaryTrace; B0LPN4; -.
PRO; PR:B0LPN4; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031672; C:A band; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005635; C:nuclear envelope; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:BHF-UCL.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
GO; GO:0048763; F:calcium-induced calcium release activity; IDA:RGD.
GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IDA:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; IMP:RGD.
GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0071313; P:cellular response to caffeine; ISS:UniProtKB.
GO; GO:0003143; P:embryonic heart tube morphogenesis; ISS:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; IMP:RGD.
GO; GO:0071421; P:manganese ion transmembrane transport; IMP:RGD.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IDA:RGD.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:0051592; P:response to calcium ion; IDA:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032026; P:response to magnesium ion; IDA:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; IMP:RGD.
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; IPR035761; SPRY1_RyR.
InterPro; IPR035764; SPRY2_RyR.
InterPro; IPR035762; SPRY3_RyR.
InterPro; IPR003877; SPRY_dom.
PANTHER; PTHR13715; PTHR13715; 1.
Pfam; PF13833; EF-hand_8; 1.
Pfam; PF08709; Ins145_P3_rec; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF02815; MIR; 1.
Pfam; PF08454; RIH_assoc; 1.
Pfam; PF06459; RR_TM4-6; 1.
Pfam; PF01365; RYDR_ITPR; 2.
Pfam; PF02026; RyR; 4.
Pfam; PF00622; SPRY; 3.
PRINTS; PR00795; RYANODINER.
SMART; SM00472; MIR; 4.
SMART; SM00449; SPRY; 3.
SUPFAM; SSF100909; SSF100909; 2.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49899; SSF49899; 2.
SUPFAM; SSF82109; SSF82109; 2.
PROSITE; PS50188; B302_SPRY; 3.
PROSITE; PS50919; MIR; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Calcium channel;
Calcium transport; Calmodulin-binding; Complete proteome;
Developmental protein; Ion channel; Ion transport;
Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Sarcoplasmic reticulum; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 4953 Ryanodine receptor 2.
/FTId=PRO_0000415583.
TOPO_DOM 1 4218 Cytoplasmic. {ECO:0000255}.
TRANSMEM 4219 4239 Helical. {ECO:0000255}.
TRANSMEM 4265 4285 Helical. {ECO:0000255}.
TRANSMEM 4489 4509 Helical. {ECO:0000255}.
TRANSMEM 4566 4586 Helical. {ECO:0000255}.
TRANSMEM 4716 4736 Helical. {ECO:0000255}.
TRANSMEM 4755 4775 Helical. {ECO:0000255}.
INTRAMEM 4806 4815 Pore-forming. {ECO:0000250}.
TRANSMEM 4836 4856 Helical. {ECO:0000255}.
TOPO_DOM 4857 4953 Cytoplasmic. {ECO:0000255}.
DOMAIN 103 158 MIR 1. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 165 210 MIR 2. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 218 273 MIR 3. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 279 336 MIR 4. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 344 401 MIR 5. {ECO:0000255|PROSITE-
ProRule:PRU00131}.
DOMAIN 592 802 B30.2/SPRY 1. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
REPEAT 846 959 1.
REPEAT 960 1073 2.
DOMAIN 1018 1215 B30.2/SPRY 2. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
DOMAIN 1350 1556 B30.2/SPRY 3. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
REPEAT 2682 2800 3.
REPEAT 2802 2915 4.
REGION 846 2915 4 X approximate repeats.
REGION 3559 3588 Interaction with CALM. {ECO:0000250}.
MOD_RES 1334 1334 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1863 1863 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2021 2021 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2359 2359 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q401}.
MOD_RES 2687 2687 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2787 2787 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q401}.
MOD_RES 2798 2798 Phosphoserine; by CaMK2D and PKA.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:18755143}.
MOD_RES 2801 2801 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2804 2804 Phosphoserine; by CaMK2D.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:18755143}.
MOD_RES 2937 2937 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q401}.
VAR_SEQ 1952 1952 R -> RKT (in isoform 2).
{ECO:0000303|PubMed:20471962}.
/FTId=VSP_042299.
VAR_SEQ 3694 3701 Missing (in isoform 2).
{ECO:0000303|PubMed:20471962}.
/FTId=VSP_042300.
CONFLICT 40 40 E -> G (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 364 364 W -> R (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 1838 1838 Q -> R (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 2691 2691 F -> S (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 3216 3216 I -> T (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 3226 3226 E -> G (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 3355 3355 D -> N (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 3541 3541 V -> I (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 3751 3751 I -> T (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 3885 3885 D -> G (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 3990 3990 V -> A (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 4196 4196 D -> G (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 4262 4262 V -> A (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 4536 4536 S -> G (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 4667 4667 D -> G (in Ref. 1; ABY79796).
{ECO:0000305}.
CONFLICT 4930 4930 Y -> H (in Ref. 1; ABY79796).
{ECO:0000305}.
HELIX 3562 3571 {ECO:0000244|PDB:2K2F}.
SEQUENCE 4953 AA; 562955 MW; 2C2798E8A2C4564A CRC64;
MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP
DLSICTFVLE QSLSVRALQE MLANTVEKSE GKFMMKTAQG GGHRTLLYGH AILLRHSYSG
MYLCCLSTSR SSTDKLAFDV GLQEDTTGEA CWWTIHPASK QRSEGEKVRV GDDLILVSVS
SERYLHLSYG NSSWRVDAAF QQTLWSVAPI SSGSEAAQGY LIGGDVLRLL HGHMDECLTV
PSGEHGEEQR RTVHYEGGAV SVHARSLWRL ETLRVAWSGS HIRWGQPFRL RHVTTGKYLS
LMEDKNLLLM DKEKADVKST AFAFRSSKEK LDAGVRKEVD GMGTSEIKYG DSICYIQHVD
TGLWLTYQAV DVKSARMGSI QRKAIMHHEG HMDDGLNLSR SQHEESRTAR VIRSTVFLFN
RFIRGLDALS KRAKLPTVDL PIESVSLSLQ DLIGYFHPPD EHLEHEDKQN RLRALKNRQN
LFQEEGMINL VLECIDRLHV YSSAAHFADV AGREAGESWK SILNSLYELL AALIRGNRKN
CAQFSGSLDW LISRLERLEA SSGILEVLHC VLVESPEALN IIKEGHIKSI ISLLDKHGRN
HKVLDVLCSL CVCHGVAVRS NQHLICDNLL PGRDLLLQTR LVNHVSSMRP NIFLGVSEGS
AQYKKWYYEL MVDHTEPFVT AEATHLRVGW ASTEGYSPYP GGGEEWGGNG VGDDLFSYGF
DGLHLWSGCI ARTVSSPNQH LLRTDDVISC CLDLSAPSIS FRINGQPVQG MFENFNIDGL
FFPVVSFSAG IKVRFLLGGR HGEFKFLPPP GYAACYEAVL PKEKLKVEHS REYKQERTYT
RDLLGPTVSL TQAAFTPVPV DTSQIVLPPH LERIRERLAE NIHELWVMNK IELGWQYGPV
RDDNKRQHPC LVEFCKLPEQ ERNYNLQMSL ETLKTLLALG CHVGIADEHA EEKVKKMKLP
KNYQLTSGYK PAPMDLSFIK LTPSQEAMVD KLAENAHNVW ARDRIRQGWT YGIQQDVKNR
RNPRLVPYTL LDDRTKKSNK DSLREAVRTL LGYGYHLEAP DQDHASRAEV CSGTGERFRI
FRAEKTYAVK AGRWYFEFEA VTAGDMRVGW SRPGCQPDLE LGSDERAFAF DGFKAQRWHQ
GNEHYGRSWQ AGDVVGCMVD MNEHTMMFTL NGEILLDDSG SELAFKDFDV GDGFIPVCSL
GVAQVGRMNF GKDVSTLKYF TICGLQEGYE PFAVNTNRDI TMWLSKRLPQ FLQVPSNHEH
IEVTRIDGTI DSSPCLKVTQ KSFGSQNSNT DIMFYRLSMP IECAEVFSKS VAGGIPGAGF
YGPKNDLEDF DVDSDFEVLM KTAHGHLVPD RMDKDKETPK PEFNNHKDYA QEKPSRLKQR
FLLRRTKPDY STSHSARLTE DVLADDRDDY EYLMQTSTYY YSVRIFPGQE PANVWVGWIT
SDFHQYDTGF DLDRVRTVTV TLGDEKGKVH ESIKRSNCYM VCAGESMSPG QGRNNSNGLE
IGCVVDAASG LLTFIANGKE LSTYYQVEPS TKLFPAVFAQ ATSPNVFQFE LGRIKNVMPL
SAGLFKSEHK NPVPQCPPRL HVQFLSHVLW SRMPNQFLKV DVSRISERQG WLVQCLDPLQ
FMSLHIPEEN RSVDILELTE QEELLQFHYH TLRLYSAVCA LGNHRVAHAL CSHVDEPQLL
YAIENKYMPG LLRAGYYDLL IDIHLSSYAT ARLMMNNEFI VPMTEETKSI TLFPDENKKH
GLPGIGLSTS LRPRMCFSSP SFVSISNECY QYSPEFPLDI LKAKTIQMLT EAVKEGSLHA
RDPVGGTTEF LFVPLIKLFY TLLIMGIFHN EDLKHILQLI EPSVFKEAAT PEEEGGAPEK
EISIDDSKLE VKEEAKAGKR PKEGLLQMKL PEPVKLQMCL LLQYLCDCQV RHRIEAIVAF
SDDFVAKLQD NQRFRYNEVM QALNMSAALT ARKEFRSPPQ EQINMLLNFK DDKSECPCPE
EIRDQLLDFH EDLMTHCGIE LDEDGSLDGS NDLTIRGRLL SLVEKVTYLK KKQAEKPVAS
DSRKSSSLQQ LISETMVRWA QESVIEDPEL VRAMFVLLHR QYDGIGGLVR ALPKTYTING
VSVEDTINLL ASLGQIRSLL SVRMGKEEEK LMIRGLGDIM NNKVFYQHPN LMRALGMHET
VMEVMVNVLG GGESKEITFP KMVANCCRFL CYFCRISRQN QKAMFDHLSY LLENSSVGLA
SPAMRGSTPL DVAAASVMDN NELALALREP DLEKVVRYLA GCGLQSCQML VSKGYPDIGW
NPVEGERYLD FLRFAVFCNG ESVEENANVV VRLLIRRPEC FGPALRGEGG NGLLAAMEEA
IKIAEDPSRD GPSPTSGSSK TLDAEEEEDD TIHMGNAIMT FYAALIDLLG RCAPEMHLIH
AGKGEAIRIR SILRSLIPLG DLVGVISIAF QMPTIAKDGK VVEPDMSAGF CPDHKAAMVL
FLDRVYGIEV QDFLLHLLEV GFLPDLRAAA SLDTAALSAT DMALALNRYL CTAVLPLLTR
CAPLFAGTEH HASLIDSLLH TVYRLSKGCS LTKAQRDSIE VCLLSICGQL RPSMMQHLLR
RLVFDVPLLN EHAKMPLKLL TNHYERCWKY YCLPGGWSNF GAASEEELHL SRKLFWGIFD
ALSQKKYEQE LFKLALPCLS AVAGALPPDY MESNYVSMME KQSSMDSEGN FNPQPVDTSN
ITIPEKLEYF INKYAEHSHD KWSMDKLANG WIYGEIYSDS SKIQPLMKPY KLLSEKEKEI
YRWPIKESLK TMLAWGWRIE RTREGDSMAL YNRTRRISQT SQVSIDAAHG YSPRAIDMSN
VTLSRDLHAM AEMMAENYHN IWAKKKKMEL ESKGGGNHPL LVPYDTLTAK EKAKDREKAQ
DIFKFLQISG YAVSRGFKDL DLDTPSIEKR FAYSFLQQLI RYVDEAHQYI LEFDGGSRSK
GEHFPYEQEI KFFAKVVLPL IDQYFKNHRL YFLSAASRPL CTGGHASNKE KEMVTSLFCK
LGVLVRHRIS LFGNDATSIV NCLHILGQTL DARTVMKTGL DSVKSALRAF LDNAAEDLEK
TMENLKQGQF THTRSQPKGV TQIINYTTVA LLPMLSSLFE HIGQHQFGED LILEDVQVSC
YRILTSLYAL GTSKSIYVER QRSALGECLA AFAGAFPIAF LETHLDKHNV YSIYNTRSSR
ERAALSLPAN VEDVCPNIPS LEKLMTEIIE LAESGIRYTQ MPHMMEVVLP MLCSYMSRWW
EHGPENHPER AEMCCTALNS EHMNTLLGNI LKIIYNNLGI DEGAWMKRLA VFSQPIINKV
KPQLLKTHFL PLMEKLKKKA AMVVSEEDHL KAEARGDMSE AELLILDEFT TLARDLYAFY
PLLIRFVDYN RAKWLKEPNP EAEELFRMVA EVFIYWSKSH NFKREEQNFV VQNEINNMSF
LITDTKSKMS KAAISDQERK KMKRKGDRYS MQTSLIVAAL KRLLPIGLNI CAPGDQELIA
LAKNRFSLKD TEEEVRDVIR SNIHLQGKLE DPAIRWQMAL YKDLPNRAED TSDPERTVER
VLDIANVLFH LEQVEHPQRS KKAVWHKLLS KQRKRAVVAC FRMAPLYNLP RHRAVNLFLQ
GYEKSWIETE EHYFEDKLIE DLAKPGSELP EEDEAMKRVD PLHQLILLFS RTALTEKCKL
EEDFLYMAYA DIMAKSCHDE EDDDGEEEVK SFEVTGSQRS KEKEMEKQKL LYQQARLHDR
GAAEMVLQTF SASKGETGPM VAATLKLGIA ILNGGNSTVQ QKMLDYLKEK KDVGFFQSLA
GLMQSCSVLD LNAFERQNKA EGLGMVTEEG SGEKVLQDDE FTCDLFRFLQ LLCEGHNSDF
QNYLRTQTGN NTTVNIIIST VDYLLRVQES ISDFYWYYSG KDIIDEQGQR NFSKAIQVAK
QVFNTLTEYI QGPCTGNQQS LAHSRLWDAV VGFLHVFAHM QMKLSQDSSQ IELLKELMDL
QKDMVVMLLS MLEGNVVNGT IGKQMVDMLV ESSNNVEMIL KFFDMFLKLK DLTSSDTFKE
YDPDGKGVIS KRDFHKAMES HKHYTQSETE FLLSCAETDE NETLDYEEFV KRFHEPAKDI
GFNVAVLLTN LSEHMPNDTR LQTFLELAES VLNYFQPFLG RIEIMGSAKR IERVYFEISE
SSRTQWEKPQ VKESKRQFIF DVVNEGGEKE KMELFVNFCE DTIFEMQLAA QISESDLNER
SANKEESEKE RPEEQAPRMG FFSLLTVQSA LFALRYNVLT LVRMLSLKSL KKQMKRMKKM
TVKDMVSAFF SSYWSVFVTL LHFVASVCRG FFRIVSSLLL GGSLVEGAKK IKVAELLANM
PDPTQDEVRG DEEEGERKPL ESALPSEDLT DLKELTEESD LLSDIFGLDL KREGGQYKLI
PHNPNAGLSD LMTNPIPVPE VQEKFQEQKV KEEKEGKEET KSEPEKAEGE DGEKEEKAKD
DKGKQKLRQL HTHRYGEPEV PESAFWKKII AYQQKLLNYF ARNFYNMRML ALFVAFAINF
ILLFYKVSTS SVVEGKELPT RTSSDAAKVT TSLDSSPHRI IAVHYVLEES SGYMEPTLRI
LAILHTIISF FCIIGYYCLK VPLVIFKREK EVARKLEFDG LYITEQPSED DIKGQWDRLV
INTQSFPNNY WDKFVKRKVM DKYGEFYGRD RISELLGMDK AALDFSDARE KKKPKKDSSL
SAVLNSIDVK YQMWKLGVVF TDNSFLYLAW YMTMSVLGHY NNFFFAAHLL DIAMGFKTLR
TILSSVTHNG KQLVLTVGLL AVVVYLYTVV AFNFFRKFYN KSEDGDTPDM KCDDMLTCYM
FHMYVGVRAG GGIGDEIEDP AGDEYEIYRI IFDITFFFFV IVILLAIIQG LIIDAFGELR
DQQEQVKEDM ETKCFICGIG NDYFDTVPHG FETHTLQEHN LANYLFFLMY LINKDETEHT
GQESYVWKMY QERCWEFFPA GDCFRKQYED QLN


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