RYR3_RABIT
ID RYR3_RABIT Reviewed; 4872 AA.
AC Q9TS33;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 02-JUN-2021, entry version 134.
DE RecName: Full=Ryanodine receptor 3;
DE Short=RYR-3;
DE Short=RyR3;
DE AltName: Full=Brain ryanodine receptor-calcium release channel;
DE AltName: Full=Brain-type ryanodine receptor;
DE AltName: Full=Type 3 ryanodine receptor;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1330694; DOI=10.1016/0014-5793(92)80941-9;
RA Hakamata Y., Nakai J., Takeshima H., Imoto K.;
RT "Primary structure and distribution of a novel ryanodine receptor/calcium
RT release channel from rabbit brain.";
RL FEBS Lett. 312:229-235(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, REGULATION BY RYANODINE; CALMODULIN; CALCIUM LEVELS; MAGNESIUM;
RP ATP; CAFFEINE AND RUTHENIUM RED, AND TISSUE SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=9305876; DOI=10.1074/jbc.272.39.24234;
RA Chen S.R., Li X., Ebisawa K., Zhang L.;
RT "Functional characterization of the recombinant type 3 Ca2+ release channel
RT (ryanodine receptor) expressed in HEK293 cells.";
RL J. Biol. Chem. 272:24234-24246(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE SPLICING,
RP FUNCTION, SUBUNIT, INTERACTION WITH RYR2, AND TISSUE SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=12471029; DOI=10.1074/jbc.m210410200;
RA Jiang D., Xiao B., Li X., Chen S.R.;
RT "Smooth muscle tissues express a major dominant negative splice variant of
RT the type 3 Ca2+ release channel (ryanodine receptor).";
RL J. Biol. Chem. 278:4763-4769(2003).
RN [4]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-3885.
RX PubMed=9614063; DOI=10.1074/jbc.273.24.14675;
RA Chen S.R., Ebisawa K., Li X., Zhang L.;
RT "Molecular identification of the ryanodine receptor Ca2+ sensor.";
RL J. Biol. Chem. 273:14675-14678(1998).
RN [5]
RP FUNCTION, SUBUNIT, DOMAIN, INTERACTION WITH FKBP1A, SUBCELLULAR LOCATION,
RP MEMBRANE TOPOLOGY, ELECTRON MICROSCOPY, REGULATION BY RYANODINE; CALCIUM
RP LEVELS; MAGNESIUM; ATP AND CAFFEINE, AND TISSUE SPECIFICITY.
RX PubMed=10358090; DOI=10.1074/jbc.274.24.17297;
RA Murayama T., Oba T., Katayama E., Oyamada H., Oguchi K., Kobayashi M.,
RA Otsuka K., Ogawa Y.;
RT "Further characterization of the type 3 ryanodine receptor (RyR3) purified
RT from rabbit diaphragm.";
RL J. Biol. Chem. 274:17297-17308(1999).
RN [6]
RP INTERACTION WITH RYR2, AND FUNCTION.
RX PubMed=12213830; DOI=10.1074/jbc.m208210200;
RA Xiao B., Masumiya H., Jiang D., Wang R., Sei Y., Zhang L., Murayama T.,
RA 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 [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16176801; DOI=10.1016/j.bbrc.2005.09.027;
RA Conti A., Reggiani C., Sorrentino V.;
RT "Selective expression of the type 3 isoform of ryanodine receptor Ca2+
RT release channel (RyR3) in a subset of slow fibers in diaphragm and cephalic
RT muscles of adult rabbits.";
RL Biochem. Biophys. Res. Commun. 337:195-200(2005).
RN [8]
RP FUNCTION, INTERACTION WITH CALM, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16274254; DOI=10.1021/bi051251t;
RA Yamaguchi N., Xu L., Pasek D.A., Evans K.E., Chen S.R., Meissner G.;
RT "Calmodulin regulation and identification of calmodulin binding region of
RT type-3 ryanodine receptor calcium release channel.";
RL Biochemistry 44:15074-15081(2005).
RN [9]
RP INTERACTION WITH SELENON, AND SUBCELLULAR LOCATION.
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 channel
RT activity in human and zebrafish muscle.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12485-12490(2008).
CC -!- FUNCTION: Calcium channel that mediates the release of Ca(2+) from the
CC sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a
CC role in triggering muscle contraction. May regulate Ca(2+) release by
CC other calcium channels. Calcium channel that mediates Ca(2+)-induced
CC Ca(2+) release from the endoplasmic reticulum in non-muscle cells.
CC Plays a role in cellular calcium signaling. Contributes to cellular
CC calcium ion homeostasis. Isoform 2 lacks a predicted transmembrane
CC segment and does not form functional calcium channels by itself;
CC however, it can form tetramers with isoforms that contain the full
CC complement of transmembrane segments and modulate their activity.
CC {ECO:0000269|PubMed:10358090, ECO:0000269|PubMed:12213830,
CC ECO:0000269|PubMed:12471029, ECO:0000269|PubMed:16274254,
CC ECO:0000269|PubMed:9305876, ECO:0000269|PubMed:9614063}.
CC -!- SUBUNIT: Homotetramer. Isoform 2 can form tetramers with isoform 1.
CC Heterotetramer with RYR2. Interacts with FKBP1A. Interacts with CALM.
CC Interacts with SELENON (PubMed:18713863). {ECO:0000269|PubMed:10358090,
CC ECO:0000269|PubMed:12213830, ECO:0000269|PubMed:12471029,
CC ECO:0000269|PubMed:16274254, ECO:0000269|PubMed:18713863,
CC ECO:0000269|PubMed:9614063}.
CC -!- INTERACTION:
CC Q9TS33; Q9TS33: -; NbExp=2; IntAct=EBI-9542578, EBI-9542578;
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Multi-pass
CC membrane protein. Membrane; Multi-pass membrane protein. Microsome
CC membrane; Multi-pass membrane protein. Sarcoplasmic reticulum
CC {ECO:0000269|PubMed:18713863}. Note=The number of predicted
CC transmembrane domains varies between orthologs, but both N-terminus and
CC C-terminus seem to be cytoplasmic. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9TS33-1; Sequence=Displayed;
CC Name=2; Synonyms=AS-8a;
CC IsoId=Q9TS33-2; Sequence=VSP_042306;
CC Name=3;
CC IsoId=Q9TS33-3; Sequence=VSP_042305;
CC Name=4;
CC IsoId=Q9TS33-4; Sequence=VSP_042307;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle from young rabbits and
CC in adult diaphragm muscle (at protein level). Detected in brain,
CC especially in corpus striatum, thalamus and hippocampus. Detected in
CC taenia coli, uterus, vas deferens, aorta, stomach, small intestine,
CC heart, diaphragm and ureter. Isoform 2 is highly expressed in uterus
CC and aorta, and at much lower levels in heart, brain and diaphragm.
CC {ECO:0000269|PubMed:10358090, ECO:0000269|PubMed:12471029,
CC ECO:0000269|PubMed:1330694, ECO:0000269|PubMed:16176801,
CC ECO:0000269|PubMed:16274254, ECO:0000269|PubMed:9305876}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitous in skeletal muscle in neonates and in
CC 15 day old rabbits. In adult, detected in diaphragm muscle, and in a
CC subset of skeletal muscles including digastricus, pterygoideus, tongue
CC and masseter. {ECO:0000269|PubMed:16176801}.
CC -!- DOMAIN: The calcium release channel activity resides in the C-terminal
CC region while the remaining part of the protein resides in the
CC cytoplasm. {ECO:0000305|PubMed:10358090}.
CC -!- MISCELLANEOUS: Channel activity is modulated by the alkaloid ryanodine
CC that binds to the open calcium-release channel with high affinity. At
CC low concentrations, ryanodine maintains the channel in an open
CC conformation. High ryanodine concentrations inhibit channel activity.
CC Channel activity is regulated by calmodulin (CALM). The calcium release
CC is activated by elevated cytoplasmic calcium levels in the micromolar
CC range, by caffeine and adenine nucleotides, such as AMP and ATP.
CC Inhibited by Mg(2+) and ruthenium red.
CC -!- MISCELLANEOUS: [Isoform 2]: Lacks a predicted transmembrane segment and
CC does not form functional calcium channels. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR3
CC subfamily. {ECO:0000305}.
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DR EMBL; X68650; CAC16153.1; -; mRNA.
DR PIR; S27272; S27272.
DR RefSeq; NP_001076231.1; NM_001082762.1. [Q9TS33-1]
DR SMR; Q9TS33; -.
DR ComplexPortal; CPX-3157; Ryanodine 3 complex. [Q9TS33-1]
DR STRING; 9986.ENSOCUP00000009882; -.
DR PRIDE; Q9TS33; -.
DR GeneID; 100009545; -.
DR KEGG; ocu:100009545; -.
DR CTD; 6263; -.
DR eggNOG; KOG2243; Eukaryota.
DR OrthoDB; 5161at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:UniProtKB.
DR GO; GO:0071318; P:cellular response to ATP; 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:0071286; P:cellular response to magnesium ion; IDA:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; NAS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR CDD; cd12877; SPRY1_RyR; 1.
DR CDD; cd12879; SPRY3_RyR; 1.
DR Gene3D; 2.60.120.920; -; 3.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
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; IPR009460; Ryanrecept_TM4-6.
DR InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR InterPro; IPR035761; SPRY1_RyR.
DR InterPro; IPR035762; SPRY3_RyR.
DR InterPro; IPR003877; SPRY_dom.
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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Endoplasmic reticulum; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Microsome; Receptor;
KW Reference proteome; Repeat; Sarcoplasmic reticulum; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..4872
FT /note="Ryanodine receptor 3"
FT /id="PRO_0000415649"
FT TOPO_DOM 1..4188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4189..4209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4412..4432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4487..4507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4612..4632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4635..4655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 4674..4694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 4725..4734
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TRANSMEM 4755..4775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4776..4872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 100..155
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 162..207
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 215..269
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 275..333
FT /note="MIR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 343..400
FT /note="MIR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 585..796
FT /note="B30.2/SPRY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REPEAT 840..953
FT /note="1"
FT REPEAT 954..1068
FT /note="2"
FT DOMAIN 1012..1208
FT /note="B30.2/SPRY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 1254..1466
FT /note="B30.2/SPRY 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REPEAT 2592..2710
FT /note="3"
FT REPEAT 2711..2823
FT /note="4"
FT REGION 840..2823
FT /note="4 X approximate repeats"
FT REGION 2325..2338
FT /note="Interaction with FKBP1A"
FT /evidence="ECO:0000250"
FT REGION 3472..3501
FT /note="Interaction with CALM"
FT /evidence="ECO:0000269|PubMed:16274254"
FT REGION 3587..3615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4104..4124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4305..4358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4110..4124
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4316..4358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 3885
FT /note="Important for activation by Ca(2+)"
FT VAR_SEQ 3341..3345
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12471029,
FT ECO:0000303|PubMed:9305876"
FT /id="VSP_042305"
FT VAR_SEQ 4406..4434
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12471029"
FT /id="VSP_042306"
FT VAR_SEQ 4791..4841
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12471029"
FT /id="VSP_042307"
FT MUTAGEN 3885
FT /note="E->A: Reduces calcium-sensitivity by over 10000-
FT fold."
FT /evidence="ECO:0000269|PubMed:9614063"
SQ SEQUENCE 4872 AA; 551929 MW; D1DC6B85CD6B93E6 CRC64;
MAEGGEGGED EIQFLRTEDE VVLQCIATVH KEQRKFCLAA EGLGNRLCFL EPTSEAKFIP
PDLCVCNFVL EQSLSVRALQ EMLANTGENG GEGAAQGGGH RTLLYGHAIL LRHSFSGMYL
TCLTTSRSQT DKLAFDVGLR EHATGEACWW TIHPASKQRS EGEKVRIGDD LILVSVSSER
YLHLSISNGN IQVDASFMQT LWNVHPTCSG SSIEEGYLLG GHVVRLFHGH DECLTIPSTD
QNDSQHRRIF YEAGGAGTRA RSLWRVEPLR ISWSGSNIRW GQAFRLRHLT TGHYLALTED
QGLLLQDRGK ADTKSTAFSF RPSKETKEKL DSSHKRDIEG MGVPEIKYGD SVCFVQHIAS
GLWVTYKAQD AKTSRLGPLK RKVILHQEGH MDDGLTLQRC QREESQAARI IRNTTALFSQ
FVSGNNRTAA PVTLPIEEVL QTLHDLIAYF QPPEEEMQHE DKQNKLRSLK NRQNLFKEEG
MLALVLNCID RLNIYNSVAH FAGIAREESG MAWKEVLSLL YKLLAALIRG NRNTCAQFSN
NLDWLISKLD RLESSSGILE VLHCILIESP EALNLIAEGH IKSIISLLDK HGRNHKVLDV
LCSLCLCNGV AVRANQNLIC DNLLPRRNLL LQTRLINDVT SIRPNIFLGV AEGSAQYKKW
YFELIIDQVD PFLTAEPTHL RVGWASSSGY APYPGGGEGW GGNGVGDDLY SYGFDGLHLW
SGRIPRAVAS INQHLLKSDD VVSCCLDLGV PSISFRINGQ PVQGMFENFN TDGLFFPVMS
FSAGVKVRFL MGGRHGEFKF LPPSGYAPCY EALLPKEKMR LEPVKEYKRD AEGVRDLLGT
TQFLSQASFI PCPIDTSQVV LPPHLEKIRD RLAENIHELW GMNKIELGWT FGKMRDDNKR
QHPCLVEFSK LPETEKNYNL QMSTETLKTL LALGCHIAHV NPAAEEDLKK VKLPKNYMMS
NGYKPAPLDL SDVKLLPPQE ILVDKLAENA HNVWAKDRIK QGWTYGIQQD LKNKRNPRLV
PYALLDERTK KSNRDSLREA VRTFVGYGYN IEPSDQELAD PAVEKVSIDK IRFFRVERSY
AVRSGKWYFE FEVVTGGDMR VGWARPGCRP DIELGPMTKP LCLKAAGASV GTKVVGILGV
PWQPGDVVGC MINLDDASMI FTLNGELLIT NKGSELAFAD YEIENGFVPI CSLGLSQIGR
MNLGTDASTF KFYTMCGLQE GFEPFAVNMN RDVAMWFSKR LPTFVNVPKD HPHIEVVRID
GTMDSPPCLK VTHKTFGTQN SNANMIYCRL SMPVECHSSF SHSPCLDSEA FQKRKQMQEI
LSHTTTQCFY SIRIFAGQDP SCVWVGWVTP DYHLYSEKFD LNKNCTVTVT LGDERGRVHE
SVKRSNCYMV WGGDVVASSQ RSSRSNVDLE IGCLVDLAMG MLSFSANGKE LGTCYQVEPN
TKVFPAVFLQ PTSTSLFQFE LGKLKNAMPL SAAIFKSEEK NPVPQCPPRL DVQTIQPVLW
SRMPNSFLKV ETERVSERHG WVVQCLEPLQ MMALHIPEEN RCVDILELCE QEDLMQFHYH
TLRLYSAVCA LGNSRVAYAL CSHVDLSQLF HAIDNKYLPG LLRSGFYDLL ISIHLANAKE
RKLMMKNEYI IPITSTTRNI RLYPDESKKH GLPGVGPRTC LKPGFKFSTP CFVVTNEERQ
KQSPEIPLEI LKMKALSMLT EAVQCSGAHI RDPVGGSVEF QFVPVLKLVG TLLVMGVFCD
DDVRQILLLI DPSVFGEHSA DTEEGAEKEE VSQVEEKAVE AGEKTSKEAR KEAPVRGLLQ
TRLPESVKLQ MCELLSYLCD CELQHRVEAI VAFGDIYVSK LQANQKFRYN ELMQALNMSA
ALTARKTREF RSPPQEQINM LLNFQLGENC PCPEEIREEL YDFHEDLLVH CGVPLEEEEE
EEEDTSWTGK LRTLVYKIKG PPKPEKEQPT EEEERCPTTL KELISQTMIR WAQEDQIQDA
ELVRMMFNLL RRQYDSIGEL LQALRKTYTI SHASVSDTIN LLAALGQIRS LLSVRMGREE
ELLMINGLGD IMNNKVFYQH PNLMRVLGMH ETVMEVMVNV LGTEKSQIAF PKMVASCCRF
LCYFCRISRQ NQKAMFEHLS YLLENSSVGL ASPSMRGSTP LDVAASSVMD NNELALGLEE
PDLEKVVTYL AGCGLQSCPM LLAKGYPDVG WNPIEGERYL SFLRFAVFVN SESVEENASV
VVKLLIRRPE CFGPALRGEG GNGLLAAMQG AIKISESPAL DLPSQGYKRE VPEDGEEEEE
IVHMGNAIMS FYSALIDLLG RCAPEMHLIQ TGKGEAIRIR SILRSLVPTE DLVGIISIPL
KLPSLNKDGS VSEPDMAANF CPDHKAPMVL FLDRVYGIKD QTFLLHLLEV GFLPDLRASA
SLDTVALSTT ESALALNRYI CSAVLPLLTR CAPLFAGTEH YTSLIDSTLQ TIYRLSKGRS
LTKAQRDTIE ECLLAICNHL RPSMLQQLLR RLVFDVPQLN DYCKMPLKLL TNHFEQCWKY
YCLPSGWGSY GLAVEEELHL TEKLFWGIFD SLSHKKYDPD LFRMSLPCLS AIAGALPPDY
LDTRITATLE KQVSVDADGN FDPKPINTIN FSLPEKLEYI VTKYAEHSHD KWACEKSQSG
WKYGISLDEN VKTHPLIRPF KTLTEKEKEI YRWPARESLK TMLAVGWTVE RTKEGEALVQ
LRENEKLRSV SQTSQGNSYN PAPLDLSNVV LSRELQGMVE VVAENYHNIW AKKKKLELES
KGGGSHPLLV PYDTLTAKEK FRDREKAQDL FKFLQVNGVI VSRGMKDMEL DAFSMEKRFA
YKFLKKILKY VDSAQEFIAH LEAIVSSGKT EKSPHDQEIK FFAKVLLPLV DQYFTNHRLY
FLSSPLKPLS SSGYASHKEK EMVASLFCKL AALVRHRISL FGSDSTTMVS CLHILAQTLD
TRTVMKSGSE LVKAGLRAFF ESAAEDLEKT SENLKLGKFT HSRTQIKGVS QNINYTTVAL
LPILTSIFEH VAQHQFGVDL LLGDVQISCY RILCSLYSLG TGKNIYVERQ RPALGECLAS
LAAAIPVAFL EPTLNRYNAL SVFNTKTPRE RSILGMPDTV EEMCPDIPQL EGLMKEINDL
AESGARYTEM PHVIEVILPM LCNYLSYWWE RGPENLSPST GPCCSKVTSE HLSLILGNIL
KIINNNLGID EASWMKRIAV YAQPIISKAR PDLLRSHFIP TLEKLKKKAV KTVQEEEQLK
ADGKGDTQEA ELLILDEFAI LCRDLYAFYP MLIRYVDNNR SNWLKSPDGD SDQLFRMVAE
VFILWCKSHN FKREEQNFVI QNEINNLAFL TGDSKSKMSK AMQVKSGGQD QERKKTKRRG
DLYSIQTSLI VAALKKMLPI GLNMCTPGDQ ELISLAKSRY SYRDTDEEVK EHLRNNLHLQ
EKSDDPAVKW QLNLYKDVLK SEEPSNPEKT VERVQRISAA VFHLEQVEQP LRSKKAVWHK
LLSKQRKRAV VACFRMAPLY NLPRHRSINL FLHGYQRFWI ETEEYSFEEK LVQDLAKSPK
VEEEEEEEME KQPDPLHQII LHFSRNALTE RSKLEDDPLY TSYSSMMAKS CQSGEDEEEE
DKEKTFEEKE MEKQKTLYQQ ARLHERGAAE MVLQMISASK GEMSPMVVET LKLGIAILNG
GNAGVQQKML DYLKVKKDAG FFQSLSGLMQ SCSVLDLNAF ERQNKAEGLG MVTEEGTLIV
RERGEKVLQN DEFTRDLFRF LQLLCEGHNS DFQNFLRTQM GNTTTVNVII STVDYLLRLQ
ESISDFYWYY SGKDIIDESG QHNFSKALAV TKQIFNSLTE YIQGPCIGNQ QSLAHSRLWD
AVVGFLHVFA NMQMKLSQDS SQIELLKELL DLLQDMVVML LSLLEGNVVN GTIGKQMVDT
LVESSTNVEM ILKFFDMFLK LKDLTSSDTF KEYDPDGKGI ISKKEFQKAM EGQKQYTQSE
IDFLLSCAEA DENDMFNYID FVDRFHEPAK DIGFNVAVLL TNLSEHMPND SRLKCLLDPA
ESVLNYFEPY LGRIEIMGGA KKIERVYFEI SESSRTQWEK PQVKESKRQF IFDVVNEGGE
QEKMELFVNF CEDTIFEMQL ASQISESDSA DRPEEEEGDE ESSYVLEING EEEEDKSFES
ASAFAMACAS LKRNITNLLR KATLKNLRKQ YRNVKKMTAK ELVKVFFSFF WMLFVGLFQL
FFTIVGGIFQ ILWSTVFGGG LVEGAKNIRV TKILGDMPDP TQFGIHDDAM EAERAEVAEA
GITTELVHFV KGERGDTELM SDLFGLHPKK EGGVKHGPEV GLGDLSEIIG KDEPPTLEST
VRKKRKAQAA ETKAEHEAEG KVESEKADLE DGEKEDKAKE EERAEYLWAE VTKKKKRRRG
QKVEKPEAFM ANFFKGLEIY QTKLLHYLAR NFYNLRFLAL FVAFAINFIL LFYKVTEEPL
EEETEDVANL WNSLNDEEEE EAMVFFVLQE STGYMAPTLR ALAVVHTIIS LVCVVGYYCL
KVPLVVFKRE KEIARKLEFD GLYITEQPSE DDIKGQWDRL VINTPSFPHN YWDKFVKRKV
INKYGDLYGA ERIAELLGLD KNALDFSPVE ETTAEAASLV SWLSSIDMKY HIWKLGVVFT
DNSFLYLAWY TTMSVLGHYN NFFFAAHLLD IAMGFKTLRT ILSSVTHNGK QLVLTVGLLA
VVVYLYTVVA FNFFRKFYNK SEDDDEPDMK CDDMMTCYLF HMYVGVRAGG GIGDEIEDPA
GDPYEMYRIV FDITFFFFVI VILLAIIQGL IIDAFGELRD QQEQVREDME TKCFICGIGN
DYFDTTPHGF ETHTLQEHNL ANYLFFLMYL INKDETEHTG QESYVWKMYQ ERCWDFFPAG
DCFRKQYEDQ LG
