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Database: UniProt
Entry: RYR1_PIG
LinkDB: RYR1_PIG
Original site: RYR1_PIG 
ID   RYR1_PIG                Reviewed;        5035 AA.
AC   P16960;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   28-FEB-2018, entry version 149.
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; Synonyms=CRC;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Norwegian Landrace; TISSUE=Skeletal muscle;
RX   PubMed=1329581;
RA   Harbitz I., Kristensen T., Bosnes M., Kran S., Davies W.;
RT   "DNA sequence of the skeletal muscle calcium release channel cDNA and
RT   verification of the Arg615-->Cys615 mutation, associated with porcine
RT   malignant hyperthermia, in Norwegian landrace pigs.";
RL   Anim. Genet. 23:395-402(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1129-2801.
RA   Brenig B.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1129-2643.
RC   STRAIN=German Landrace; TISSUE=Liver;
RX   PubMed=8288238; DOI=10.1006/geno.1993.1475;
RA   Leeb T., Schmolzl S., Brem G., Brenig B.;
RT   "Genomic organization of the porcine skeletal muscle ryanodine
RT   receptor (RYR1) gene coding region 4624 to 7929.";
RL   Genomics 18:349-354(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4785-5035.
RX   PubMed=2174405; DOI=10.1016/0888-7543(90)90278-3;
RA   Harbitz I., Chowdhary B., Thomsen P.D., Davies W., Kaufman U.,
RA   Kran S., Gustavsson I., Christensen K., Hauge J.G.;
RT   "Assignment of the porcine calcium release channel gene, a candidate
RT   for the malignant hyperthermia locus, to the 6p11-->q21 segment of
RT   chromosome 6.";
RL   Genomics 8:243-248(1990).
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 (By similarity). Repeated very high-level exercise
CC       increases the open probability of the channel and leads to Ca(2+)
CC       leaking into the cytoplasm (By similarity). Can also mediate the
CC       release of Ca(2+) from intracellular stores in neurons, and may
CC       thereby promote prolonged Ca(2+) signaling in the brain. Required
CC       for normal embryonic development of muscle fibers and skeletal
CC       muscle. Required for normal heart morphogenesis, skin development
CC       and ossification during embryogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:E9PZQ0, ECO:0000250|UniProtKB:P11716}.
CC   -!- ENZYME REGULATION: Channel activity is modulated by the alkaloid
CC       ryanodine that binds to the open Ca-release channel with high
CC       affinity. At low concentrations, ryanodine maintains the channel
CC       in an open conformation. High ryanodine concentrations inhibit
CC       channel activity. 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. Channel
CC       activity is inhibited by magnesium ions, possibly by competition
CC       for calcium binding sites. {ECO:0000250|UniProtKB:P11716}.
CC   -!- SUBUNIT: Homotetramer. Can also form heterotetramers with RYR2 (By
CC       similarity). Identified in a complex composed of RYR1, PDE4D, PKA,
CC       FKBP1A and protein phosphatase 1 (PP1). Repeated very high-level
CC       exercise decreases interaction with PDE4D and protein phosphatase
CC       1 (PP1) (By similarity). Interacts with CALM; CALM with bound
CC       calcium inhibits the RYR1 channel activity (By similarity).
CC       Interacts with S100A1 (By similarity). Interacts with FKBP1A; this
CC       stabilizes the closed conformation of the channel. Interacts with
CC       CACNA1S; interaction with CACNA1S is important for activation of
CC       the RYR1 channel. Interacts with CACNB1. Interacts with TRDN and
CC       ASPH; these interactions stimulate RYR1 channel activity.
CC       Interacts with SELENON (By similarity).
CC       {ECO:0000250|UniProtKB:E9PZQ0, ECO:0000250|UniProtKB:P11716,
CC       ECO:0000250|UniProtKB:P21817}.
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P11716}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P11716}. Sarcoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P11716}. Membrane
CC       {ECO:0000250|UniProtKB:P11716}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P11716}. 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:0000250|UniProtKB:P11716}.
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. Pore
CC       opening is mediated via the cytoplasmic calcium-binding domains
CC       that mediate a small rotation of the channel-forming transmembrane
CC       regions that then leads to channel opening.
CC       {ECO:0000250|UniProtKB:P11716}.
CC   -!- PTM: Channel activity is modulated by phosphorylation.
CC       Phosphorylation at Ser-2844 may increase channel activity.
CC       Repeated very high-level exercise increases phosphorylation at
CC       Ser-2844. {ECO:0000250|UniProtKB:P21817}.
CC   -!- PTM: Activated by reversible S-nitrosylation (By similarity).
CC       Repeated very high-level exercise increases S-nitrosylation (By
CC       similarity). {ECO:0000250|UniProtKB:P11716,
CC       ECO:0000250|UniProtKB:P21817}.
CC   -!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family.
CC       RYR1 subfamily. {ECO:0000305}.
DR   EMBL; X62880; CAA44674.1; ALT_SEQ; mRNA.
DR   EMBL; X68247; CAA48318.1; -; Genomic_DNA.
DR   EMBL; X69465; CAA49225.1; -; Genomic_DNA.
DR   EMBL; M32501; AAA31022.1; -; mRNA.
DR   UniGene; Ssc.8; -.
DR   ProteinModelPortal; P16960; -.
DR   STRING; 9823.ENSSSCP00000003203; -.
DR   PaxDb; P16960; -.
DR   PeptideAtlas; P16960; -.
DR   PRIDE; P16960; -.
DR   eggNOG; KOG2243; Eukaryota.
DR   eggNOG; ENOG410YCNW; LUCA.
DR   HOVERGEN; HBG006699; -.
DR   InParanoid; P16960; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0031301; C:integral component of organelle membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0014802; C:terminal cisterna; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; ISS:UniProtKB.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0071313; P:cellular response to caffeine; ISS:UniProtKB.
DR   GO; GO:0071277; P:cellular response to calcium ion; ISS: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; ISS:UniProtKB.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISS: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   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; 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; IPR035910; RyR/IP3R_RIH_dom_sf.
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; 2.
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   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Calcium channel; Calcium transport;
KW   Calmodulin-binding; Complete proteome; Developmental protein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; S-nitrosylation; Sarcoplasmic reticulum;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   5035       Ryanodine receptor 1.
FT                                /FTId=PRO_0000219359.
FT   TOPO_DOM      1   4556       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4557   4577       Helical; Name=1.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4578   4638       Lumenal. {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4639   4659       Helical; Name=2.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4660   4777       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4778   4800       Helical; Name=3.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4801   4801       Lumenal. {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4802   4818       Helical; Name=4.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4819   4833       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4834   4854       Helical; Name=5.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4855   4877       Lumenal. {ECO:0000250|UniProtKB:P11716}.
FT   INTRAMEM   4878   4897       Pore-forming.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4898   4917       Lumenal. {ECO:0000250|UniProtKB:P11716}.
FT   TRANSMEM   4918   4938       Helical; Name=6.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   TOPO_DOM   4939   5035       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P11716}.
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    393       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     2727   2846       5.
FT   REPEAT     2847   2960       6.
FT   DOMAIN     4070   4098       EF-hand. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   NP_BIND    4206   4210       ATP. {ECO:0000250|UniProtKB:P11716}.
FT   NP_BIND    4952   4957       ATP. {ECO:0000250|UniProtKB:P11716}.
FT   NP_BIND    4977   4983       ATP. {ECO:0000250|UniProtKB:P11716}.
FT   REGION      670    681       Interaction with FKBP1A.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   REGION      842   2960       6 X approximate repeats.
FT   REGION     3610   3639       Interaction with CALM. {ECO:0000250}.
FT   MOTIF      4892   4898       Selectivity filter.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   COMPBIAS   1874   1925       Glu-rich (acidic).
FT   COMPBIAS   4458   4526       Pro-rich.
FT   METAL      3888   3888       Calcium. {ECO:0000250|UniProtKB:P11716}.
FT   METAL      3962   3962       Calcium. {ECO:0000250|UniProtKB:P11716}.
FT   METAL      4999   4999       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   BINDING    4714   4714       Caffeine. {ECO:0000250|UniProtKB:P11716}.
FT   MOD_RES    1338   1338       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    2346   2346       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    2844   2844       Phosphoserine; by PKA and PKG.
FT                                {ECO:0000250|UniProtKB:E9PZQ0}.
FT   MOD_RES    3631   3631       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P11716}.
FT   MOD_RES    4463   4463       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    4467   4467       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1LMY4}.
FT   MOD_RES    4861   4861       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P21817}.
FT   MOD_RES    4864   4864       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P21817}.
FT   CONFLICT   2092   2092       A -> P (in Ref. 3; CAA49225).
FT                                {ECO:0000305}.
SQ   SEQUENCE   5035 AA;  565332 MW;  E00613F2027B94A4 CRC64;
     MGDGGEGEDE VQFLRTDDEV VLQCNATVLK EQLKLCLAAE GFGNRLCFLE PTSNAQNVPP
     DLAICCFVLE QSLSVRALQE MLANTVEAGV ESSQGGGHRT LLYGHAILLR HAHSGMYLSC
     LTTSRSMTDK LAFDVGLQED ATGEACWWTT HPASKQRSEG EKVRVGDDLI LVSVSSERYL
     HLSTASGELQ VDASFMQTLW NMNPICSGCE EGYVTGGHVL RLFHGHMDEC LTISPADSDD
     QRRLVYYEGG SVCTHARSLW RLEPLRISWS GSHLRWGQPL RIRHVTTGRY LALIEDQGLV
     VVDASKAHTK ATSFCFRISK EKLDTAPKRD VEGMGPPEIK YGESLCFVQH VASGLWLTYA
     APDPKALRLG VLKKKAILHQ EGHMDDALSL TRCQQEESQA ARMIYSTAGL YNHFIKGLDS
     FSGKPRGSGA PAGTALPLEG VILSLQDLIG YFEPPSEELQ HEEKQSKLRS LRNRQSLFQE
     EGMLSLVLNC IDRLNVYTTA AHFAEFAGEE AAESWKEIVN LLYEILASLI RGNRANCALF
     SNNLDWLVSK LDRLEASSGI LEVLYCVLIE SPEVLNIIQE NHIKSIISLL DKHGRNHKVL
     DVLCSLCVCN GVAVRSNQDL ITENLLPGRE LLLQTNLINY VTSIRPNIFV GRAEGTTQYS
     KWYFEVMVDE VVPFLTAQAT HLRVGWALTE GYSPYPGGGE GWGGNGVGDD LYSYGFDGLH
     LWTGHVPRLV TSPGQHLLAP EDVVSCCLDL SVPSISFRIN GCPVQGVFEA FNLNGLFFPV
     VSFSAGVKVR FLLGGRHGEF KFLPPPGYAP CHEAVLPRER LRLEPIKEYR REGPRGPHLV
     GPSRCLSHTD FVPCPVDTVQ IVLPPHLERI REKLAENIHE LWALTRIEQG WTYGPVRDDN
     KRLHPCLVDF HSLPEPERNY NLQMSGETLK TLLALGCHVG MADEKAEDNL RKTKLPKTYM
     MSNGYKPAPL DLSHVRLTPA QTTLVDRLAE NGHNVWARDR VAQGWSYSAV QDIPARRNPR
     LVPYRLLDEA TKRSNRDSLC QAVRTLLGYG YNIEPPDQEP SQVESQSRWD RVRIFRAEKS
     YAVQSGRWYF EFEAVTTGEM RVGWARPELR PDVELGADEL AYVFNGHRGQ RWHLGSELFG
     RPWQSGDVVG CMIDLTENTI IFTLNGEVLM SDSGSETAFR DIEVGDGFLP VCSLGPGQVG
     HLNLGQDVSS LRFFAICGLQ EGFEPFAINM QRPVTTWFSK SLPQFEAVPL EHPHYEVSRV
     DGTVDTPPCL RLTHRTWGSQ NSLVEMLFLR LSLPVQFHQH FRCTAGATPL APPGLQPPAE
     DEARAAEPDP DYENLRRSAG RWGEAEGGKE GTAKEGAPGG TAQAGVEAQP PRAENEKDAT
     TEKNKKRGFL FKAKKAAMMT QPPATPTLPR LPHEVVPADD RDDPDIILNT TTYYYSVRVF
     AGQEPSCVWV GWVTPDYHQH DMNFDLTKVR AVTVTMGDEQ GNIHSSLKCS NCYMVWGGDF
     VSPGQQGRIS HTDLVIGCLV DLATGLMTFT ANGKESNTFF QVEPNTKLFP AVFVLPTHQN
     VIQFELGKQK NIMPLSAAMF LSERKNPAPQ CPPRLEMQML MPVSWSRMPN HFLRVETRRA
     GERLGWAVQC QEPLTMMALH IPEENRCMDI LELSERLDLQ QFHSHTLRLY RAVCALGNNR
     VAHALCSHVD QAQLLHALED AHLPGPLRAG YYDLLISIHL ESACRSRRSM LSEYIVPLTP
     ETRAITLFPP GKRTENGPRR HGLPGVGVTT SLRPPHHFSA PCFVAALPAV GAAEAPARLS
     PSIPLEALRD KALRMLGEAV RDGGQHARDP VGGSVEFQFV PVLKLVSTLL VMGIFGDEDV
     KQILKMIEPE VFTEEEEEEE EEEEEEEEDE EEKEEDEEEE AREKEDEEKE EEETAEGEKE
     EYLEEGLLQM KLPESVKLQM CNLLEYFCDQ ELQHRVESLA AFAERYVDKL QANQRDRYGI
     LMKAFTMTAA ETARRTREFR SPPQEQINML LHFKDGEDEE DCPLPDEIRQ DLLEFHQDLL
     THCGIQLEGE EEEPEEEATL GSRLMSLLEK VRLVKKKEEK SEEEPPAEES KAQSLQELVS
     HTVVRWAQED FVQSPELVRA MFSLLHRQYD GLGELLRALP RAYTISPSSV EDTMSLLECL
     GQIRSLLIVQ MGPQEENLMI QSIGNIMNNK VFYQHPNLMR ALGMHETVME VMVNVLGGGE
     SKEIRFPKMV TSCCRFLCYF CRISRQNQRS MFDHLSYLLE NSGIGLGMQG STPLDVAAAS
     VIDNNELALA LQEQDLEKVV SYLAGCGLQS CPMLLAKGYP DIGWNPCGGE RYLDFLRFAV
     FVNGESVEEN ANVVVRLLIR KPECFGPALR GEGGSGLLAT IEEAIRISED PARDGPGVRR
     DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE MHLIQAGKGE ALRIRAILRS
     LVPLDDLVGI ISLPLQIPTL GKDGALVQPK MSASFVPDHK ASMVLFLDRV YGIENQDFLL
     HVLDVGFLPD MRAAASLDTA TFSTTEMALA LNRYLCLAVL PLITKCAPLF AGTEHRAIMV
     DSMLHTVYRL SRGRSLTKAQ RDVIEECLMA LCRYIRPSML QHLLRRLVFD VPILNEFAKM
     PLKLLTNHYE RCWKYYCLPT GWANFGVTSE EELHLTRKLF WGIFDSLAHK KYDPELYRMA
     MPCLCAIAGA LPPDYVDASY SSKAEKKATV DAEGNFDPRP VETLNVIIPE KLDSFINKFA
     EYTHEKWAFD KIQNNWSYGE NIDEELKTHP MLRPYKTFSE KDKEIYRWPI KESLKAMIAW
     EWTIEKAREG EEEKTEKKKT RKISQSAQTY DAREGYNPQP PDLSGVTLSR ELQAMAEQLA
     ENYHNTWGRK KKQELEAKGG GTHPLLVPYD TLTAKEKARD REKAQELLKF LQMNGYAVTR
     GLKDMELDTS SIEKRFAFGF LQQLLRWMDI SQEFIAHLEA VVSSGRVEKS PHEQEIKFFA
     KILLPLINQY FTNHCLYFLS TPAKVLGSGG HASNKEKEMI TSLFCKLAAL VRHRVSLFGT
     DAPAVVNCLH ILARSLDART VMKSGPEIVK AGLRSFFESA SEDIEKMVEN LRLGKVSQAR
     TQVKGVGQNL TYTTVALLPV LTTLFQHIAQ HQFGDDVILD DVQVSCYRTL CSIYSLGTTR
     NPYVEKLRPA LGECLARLAA AMPVAFLEPQ LNEYNACSVY TTKSPRERAI LGLPNSVEEM
     CPDIPVLERL MADIGGLAES GARYTEMPHV IEITLPMLCS YLPRWWERGP EAPPPALPAG
     APPPCTAVTS DHLNSLLGNI LRIIVNNLGI DEASWMKRLA VFAQPIVSRA RPELLHSHFI
     PTIGRLRKRA GKVVAEEEQL RLEAKAEAEE GELLVRDEFS VLCRDLYALY PLLIRYVDNN
     RAHWLTEPNP SAEELFRMVG EIFIYWSKSH NFKREEQNFV VQNEINNMSF LTADNKSKMA
     KSGGSDQERT KKKRLGDRYS VQTSLIVATL KKMLPIGLNM CAPTDQELIT LAKTRYALKD
     TDEEVREFLQ NNLHLQGKVE GSPSLRWQMA LYRGLPGREE DADDPEKIVR RVQEVSAVLY
     HLEQMEHPYK SKKAVWHKLL SKQRRRAVVA CFRMTPLYNL PTHRACNMFL ESYKAAWILT
     EDHSFEDRMI DDLSKAGEQE EEEEEVEEKK PDPLHQLVLH FSRTALTEKS KLDEDYLYMA
     YADIMAKSCH LEEGGENGEA QEEVEVSFEE KEMEKQRLLY QQARLHNRGA AEMVLQMISA
     CKGETGAMVS STLKLGISIL NGGNADVQQK MLDYLKDKKE VGFFQSIQAL MQTCSVLDLN
     AFERQNKAEG LGMVNEDGTV INRQNGEKVM ADDEFTQDLF RFLQLLCEGH NNDFQNYLRT
     QTGNTTTINI IICTVDYLLR LQESISDFYW YYSGKDVIEE QGKRNFSKAM SVAKQVFNSL
     TEYIQGPCTG NQQSLAHSRL WDAVVGFLHV FAHMMMKLAQ DSSQIELLKE LLDLQKDMVV
     MLLSLLEGNV VNGMIARQMV DMLVESSSNV EMILKFFDMF LKLKDIVGSE AFQDYVTDPR
     GLISKKDFQK AMDSQKQFTG PEIQFLLSCS EADENEMIDC EEFANRFQEP ARDIGFNVAV
     LLTNLSEHVP HDPRLRNFLE LAESILEYFR PYLGRIEIMG ASRRIERIYF EISETNRAQW
     EMPQVKESKR QFIFDVVNEG GESEKMELFV SFCEDTIFEM QIAAQISEPE GEPEEDEDEG
     AGLAEAGAEG AEEGAVGPEG AAGTAAAGLT ARLAAATSRA LRGLSYRSLR RRVRRLRRLT
     AREAATALAA LLWAALAHAG AAGAGAAAGA LRLLWGSLFG GGLVEGAKKV TVTELLAGMP
     DPTGDEVHGE QPAGPGGEAD GEGAGEGAGE AWEGAGDEEV AVQEAGPGGA DGAVAVAEGG
     PFRPEGAGGL GDMGDTTPAE PPTPEGSPII KRKLGVDGEE EELPPEPEPE PEPEPEKADA
     ENGEKEEVPK PPPEPPKKTA PPPPPPKKEE GGSGGLEFWG ELEVQRVKFL NYLSRNFYTL
     RFLALFLAFA INFILLFYKV SDSPPGEDDM EGSAAGDLSG AGSGGGSGWG SGAGEEVEGD
     EDENMVYYFL EESTGYMEPA LRCLSLLHTL VAFLCIIGYN CLKVPLVIFK REKELARKLE
     FDGLYITEQP EDDDVKGQWD RLVLNTPSFP SNYWDKFVKR KVLDKHGDIY GRERIAELLG
     MDLATLEITA HNERKPEPPP GLLTWLMSID VKYQIWKFGV IFTDNSFLYL GWYMVMSLLG
     HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT VVAFNFFRKF
     YNKSEDEDEP DMKCDDMMTC YLFHMYVGVR AGGGIGDEIE DPAGDEYELY RVVFDITFFF
     FVIVILLAII QGLIIDAFGE LRDQQEQVRE DMETKCFICG IGSDYFDTTP HRFETHTLEE
     HNLANYMFFL MYLINKDETE HTGQESYVWK MYQERCWDFF PAGDCFRKQY EDQLS
//
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