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Database: UniProt
Entry: RYR2_RABIT
LinkDB: RYR2_RABIT
Original site: RYR2_RABIT 
ID   RYR2_RABIT              Reviewed;        4969 AA.
AC   P30957;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   10-OCT-2018, entry version 140.
DE   RecName: Full=Ryanodine receptor 2;
DE            Short=RYR-2;
DE            Short=RyR2;
DE   AltName: Full=Cardiac muscle ryanodine receptor;
DE   AltName: Full=Cardiac muscle ryanodine receptor-calcium release channel;
DE   AltName: Full=Cardiac muscle-type ryanodine receptor;
DE   AltName: Full=Type 2 ryanodine receptor;
GN   Name=RYR2;
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].
RC   TISSUE=Heart muscle;
RX   PubMed=2380170;
RA   Otsu K., Willard H.F., Khanna V.K., Zorzato F., Green N.M.,
RA   Maclennan D.H.;
RT   "Molecular cloning of cDNA encoding the Ca2+ release channel
RT   (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic
RT   reticulum.";
RL   J. Biol. Chem. 265:13472-13483(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8841406; DOI=10.1111/j.1432-1033.1996.0408h.x;
RA   Nishida K., Otsu K., Hori M., Kuzuya T., Tada M.;
RT   "Cloning and characterization of the 5'-upstream regulatory region of
RT   the Ca(2+)-release channel gene of cardiac sarcoplasmic reticulum.";
RL   Eur. J. Biochem. 240:408-415(1996).
RN   [3]
RP   PHOSPHORYLATION AT SER-2809 BY CAMK2D.
RX   PubMed=1645727;
RA   Witcher D.R., Kovacs R.J., Schulman H., Cefali D.C., Jones L.R.;
RT   "Unique phosphorylation site on the cardiac ryanodine receptor
RT   regulates calcium channel activity.";
RL   J. Biol. Chem. 266:11144-11152(1991).
RN   [4]
RP   INTERACTION WITH RYR1 AND RYR3, AND FUNCTION.
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   [5]
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
RT   channel 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
CC       the sarcoplasmic reticulum into the cytoplasm and thereby plays a
CC       key role in triggering cardiac muscle contraction. Aberrant
CC       channel activation can lead to cardiac arrhythmia. In cardiac
CC       myocytes, calcium release is triggered by increased Ca(2+) levels
CC       due to activation of the L-type calcium channel CACNA1C. Required
CC       for cellular calcium ion homeostasis. Required for embryonic heart
CC       development (By similarity). The calcium channel activity is
CC       modulated by formation of heterotetramers with RYR3.
CC       {ECO:0000250|UniProtKB:Q92736, ECO:0000269|PubMed:12213830}.
CC   -!- ACTIVITY REGULATION: Channel activity is modulated by the alkaloid
CC       ryanodine that binds to the open Ca-release channel with high
CC       affinity and maintains the channel in an open conformation.
CC       Channel activity is regulated by calmodulin (CALM). The calcium
CC       release channel is activated by calcium ions and ATP. Channel
CC       activity is inhibited by magnesium ions (By similarity).
CC       {ECO:0000250|UniProtKB:P11716}.
CC   -!- SUBUNIT: Homotetramer. Can also form heterotetramers with RYR1 and
CC       RYR3. Interacts with FKBP1A and FKBP1B; these interactions may
CC       stabilize the channel in its closed state and prevent Ca(2+)
CC       leaks. Interacts with CALM and S100A1; these interactions regulate
CC       channel activity. Identified in a complex composed of RYR2,
CC       FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein
CC       phosphatases PP2A and PP1. Interacts directly with FKBP1B, PKA,
CC       PP1 and PP2A (By similarity). Interacts with SELENON
CC       (PubMed:18713863). In cardiac muscles, identified in a complex,
CC       composed of FSD2, CMYA5 and RYR2 (By similarity).
CC       {ECO:0000250|UniProtKB:E9Q401, ECO:0000250|UniProtKB:Q92736,
CC       ECO:0000269|PubMed:18713863}.
CC   -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC       Sarcoplasmic reticulum {ECO:0000269|PubMed:18713863}. Note=The
CC       number of predicted transmembrane domains varies between
CC       orthologs, but both N-terminus and C-terminus seem to be
CC       cytoplasmic. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Heart and brain.
CC   -!- DOMAIN: The calcium release channel activity resides in the C-
CC       terminal region while the remaining part of the protein resides in
CC       the cytoplasm. {ECO:0000305}.
CC   -!- PTM: Channel activity is modulated by phosphorylation.
CC       Phosphorylation at Ser-2809 and Ser-2815 increases the open
CC       probability of the calcium channel. Phosphorylation is increased
CC       in failing heart, leading to calcium leaks and increased
CC       cytoplasmic Ca(2+) levels. {ECO:0000269|PubMed:1645727}.
CC   -!- PTM: Phosphorylation at Ser-2031 by PKA enhances the response to
CC       lumenal calcium. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family.
CC       RYR2 subfamily. {ECO:0000305}.
DR   EMBL; M59743; AAA31179.1; -; mRNA.
DR   PIR; A37113; A37113.
DR   UniGene; Ocu.1832; -.
DR   ProteinModelPortal; P30957; -.
DR   IntAct; P30957; 1.
DR   MINT; P30957; -.
DR   STRING; 9986.ENSOCUP00000016860; -.
DR   iPTMnet; P30957; -.
DR   PRIDE; P30957; -.
DR   eggNOG; KOG2243; Eukaryota.
DR   eggNOG; ENOG410YCNW; LUCA.
DR   HOGENOM; HOG000231428; -.
DR   HOVERGEN; HBG006699; -.
DR   InParanoid; P30957; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:AgBase.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0008144; F:drug binding; IDA:AgBase.
DR   GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IEA:InterPro.
DR   GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0071313; P:cellular response to caffeine; ISS:UniProtKB.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; 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; IPR035761; SPRY1_RyR.
DR   InterPro; IPR035764; SPRY2_RyR.
DR   InterPro; IPR035762; SPRY3_RyR.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR13715; PTHR13715; 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; 2.
DR   SUPFAM; SSF82109; SSF82109; 2.
DR   PROSITE; PS50188; B302_SPRY; 3.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Calmodulin-binding;
KW   Coiled coil; Complete proteome; Developmental protein; Ion channel;
KW   Ion transport; Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Sarcoplasmic reticulum;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   4969       Ryanodine receptor 2.
FT                                /FTId=PRO_0000219362.
FT   TOPO_DOM      1   4282       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   4283   4303       Helical. {ECO:0000255}.
FT   TRANSMEM   4505   4525       Helical. {ECO:0000255}.
FT   TRANSMEM   4582   4602       Helical. {ECO:0000255}.
FT   TRANSMEM   4732   4752       Helical. {ECO:0000255}.
FT   TRANSMEM   4771   4791       Helical. {ECO:0000255}.
FT   INTRAMEM   4822   4831       Pore-forming. {ECO:0000250}.
FT   TRANSMEM   4852   4872       Helical. {ECO:0000255}.
FT   TOPO_DOM   4873   4969       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      110    165       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      172    217       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      225    280       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      286    345       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      351    408       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      599    809       B30.2/SPRY 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT      853    966       1.
FT   REPEAT      967   1080       2.
FT   DOMAIN     1025   1222       B30.2/SPRY 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   DOMAIN     1357   1562       B30.2/SPRY 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT     2693   2811       3.
FT   REPEAT     2813   2926       4.
FT   REGION      853   2926       4 X approximate repeats.
FT   REGION     3582   3611       Interaction with CALM. {ECO:0000250}.
FT   COILED     4413   4446       {ECO:0000255}.
FT   MOD_RES    1341   1341       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:E9Q401}.
FT   MOD_RES    1869   1869       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:B0LPN4}.
FT   MOD_RES    2031   2031       Phosphoserine; by PKA.
FT                                {ECO:0000250|UniProtKB:E9Q401}.
FT   MOD_RES    2370   2370       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:E9Q401}.
FT   MOD_RES    2698   2698       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:B0LPN4}.
FT   MOD_RES    2798   2798       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:E9Q401}.
FT   MOD_RES    2809   2809       Phosphoserine; by CaMK2D and PKA.
FT                                {ECO:0000269|PubMed:1645727}.
FT   MOD_RES    2812   2812       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:E9Q401}.
FT   MOD_RES    2815   2815       Phosphoserine; by CaMK2D.
FT                                {ECO:0000250|UniProtKB:Q92736}.
FT   MOD_RES    2948   2948       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:E9Q401}.
SQ   SEQUENCE   4969 AA;  565073 MW;  FF6E0684B974BB4D CRC64;
     MADGGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP
     DLSICTFVLE QSLLVRALQE MLANTVEKSE GQVDVEKWKF MMKTAQGGGH RTLLYGHAIL
     LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ EDTTGEACWW TIHPASKQRS EGEKVRVGDD
     LILVSVSSER YLHLSYGNGS LHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH
     MDECLTVPSG EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV
     TTGKYLSLME DKNLLLMDKE KADVKSTAFT FRSSKEKLDG GVRKEVDGMG TSEIKYGDSI
     CYIQHVDTGL WLTYQSVDVK SVRMGSIQRK AIMHHEGHMD DGLNLSRSQH EESRTARVIR
     STVFLFNRFI RGLDALSKKA KASSVDLPIE SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR
     ALKNRQNLFQ EEGMINLVLE CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL
     IRGNRKNCAQ FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL
     LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN HVSSMRPNIF
     LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST EGYSPYPGGG EEWGGNGVGD
     DLFSYGFDGL HLWSGCIART VSSPNQHLLR TDDVISCCLD LSAPSISFRI NGQPVQGMFE
     NFNIDGLFFP VVSFSAGIKV RFLLGGRHGE FKFLPPPGYA PCYEAVLPKE KLKVEHSREY
     KQERTYTRDL LGPTVSLTQA AFTPIPVDTS QIVLPPHLER IREKLAENIH ELWVMNKIEL
     GWQYGPVRDD NKRQHPCLVE FSKLPEQERN YNLQMSLETL KTLLALGCHV GISDEHAEEK
     VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA ENAHNVWARD RIRQGWTYGI
     QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL REAVRTLLGY GYNLEAPDQD HAARAEVCSG
     TGERFRIFRA EKTYAVKAGR WYFEFEAVTS GDMRVGWSRP GCQPDQELGS DERAFAFDGF
     KAQRWHQGNE HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG
     FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW LSKRLPQFLQ
     VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNSNTDIM FYRLSMPIEC AEVFSKTVPG
     GLPGAGLFGP KNDLEDYDAD SDFEVLMKTA HGHLVPDRVD KDKETTKAEF NNHKDYAQEK
     PSRLKQRFLL RRTKPDYSTS HSARLTEDVL ADDRDDYDFL MQTSTYYYSV RIFPGQEPAN
     VWVGWITSDF HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR
     NNNGLEIGCV VDAASGLLTF IANGKELSTY YQVEPSTKLF PAVFAQATSP NVFQFELGRI
     KNVMPLSAGL FKSEHKNPVP QCPPRLHVQF LSHVLWSRMP NQFLKVDVSR ISERQGWLVQ
     CLDPLQFMSL HIPEENRSVD ILELTEQEEL LKFHYHTLRL YSAVCALGNH RVAHALCSHV
     DEPQLLYAIE NKYMPGLLRT GYYDLLIDIH LSSYATARLM MNNEFIVPMT EETKSITLFP
     DENKKHGLPG IGLSTSLRPR MQFSSPSFVS INNECYQYSP EFPLDILKAK TIQMLTEAVK
     EGSLHGRDPV GGTTEFLFVP LIKLFYTLLI MGIFHNEDLR HILQLIEPSV FKDAATPEEE
     GDTLEEEPSV EDTKLEGAGE EEAKVGKRPK EGLLQMKLPE PVKLQMCLLL QYLCDCQVRH
     RIEAIVAFSD DFVAKLQDNQ RFRYNEVMQA LNMSAALTAR KTKEFRSPPQ EQINMLLNFK
     DDKSECPCPE EIRDQLLDFH EDLMTHCGIE LDEDGSLDGN SDLTIRGRLL SLVEKVTYLK
     KKQTEKPVES DSRKSSTLQQ LISETMVRWA QESVIEDPEL VRAMFVLLHR QYDGIGGLVR
     ALPKTYTING VSVEDTINLL ASLGQIRSLL SVRMGKEEEK LMIRGLGDIM NNKVFYQHPN
     LMRALGMHET VMEVMVNVLG GGESKEITFP KMVANCCRFL CYFCRISRQN QKAMFDHLSY
     LLENSSVGLA SPAMRGSTPL DVAAASVMDN NELALALREP DLEKVVVRYL AGCGLQSCQM
     LVSKGYPDIG WNPVEGERYL DFLRFAVFCN GESVEENANV VVRLLIRRPE CFGPALRGEG
     GNGLLAAMEE AIKIAEDPSR DGPSPTSGSS KTLDTEEEED DTIHMGNAIM TFYAALIDLL
     GRCAPEMHLI HAGKGEAIRI RSILRSLIPL GDLVGVISIA FQMPTIAKDG NVVEPDMSAG
     FCPDHKAAMV LFLDRVYGIE VQDFLLHLLE VGFLPDLRAA ASLDTAALSA TDMALALNRY
     LCTAVLPLLT RCAPLFAGTE HHASLIDSLL HTVYRLSKGC SLTKAQRDSI EVCLLSICGQ
     LRPSMMQHLL RRLVFDVPLL NEHAKMPLKL LTNHYERCWK YYCLPGGWGN FGAASEEELH
     LSRKLFWGIF DALSQKKYEQ ELFKLALPCL SAVAGALPPD YMESNYVSMM EKQSSMDSEG
     NFNPQPVDTS NIIIPEKLEY FINKYAEHSH DKWSMDKLAN GWIYGEIYSD SSKIQPLMKP
     YKLLSEKEKE IYRWPIKESL KTMLAWGWRI ERTREGDSMA LYNRTRRISQ TSQVSVDAAH
     GYSPRAIDMS NVTLSRDLHA MAEMMAENYH NIWAKKKKLE LESKGGGNHP LLVPYDTLTA
     KEKAKDREKA QDILKFLQIN GYAVSRGFKD LELDTPSIEK RFAYSFLQQL IRYVDEAHQY
     ILEFDGGSRS KGEHFPYEQE IKFFAKVVLP LIDQYFKNHR LYFLSAASRP LCSGGHASNK
     EKEMVTSLFC KLGVLVRHRI SLFGNDATSI VNCLHILGQT LDARTVMKTG LESVKSALRA
     FLDNAAEDLE KTMENLKQGQ FTHTRNQPRG VTQIINYTTV ALLPMLSSLF EHIGQHQFGE
     DLILEDVQVS CYRILTSLYA LGTSKSIYVE RQRSALGECL AAFAGAFPVA FLETHLNKHN
     IYSIYNTKSS RERAALSLPA NVEDVCPNIP SLEKLMEEIV ELAESGIRYT QMPHVMEVIL
     PMLCSYMSRW WEHGPESNPG RAEMCCTALN SEHMNTLLGN ILKIIYNNLG IDEGAWMKRL
     AVFSQPIINK VKPQLLKTHF LPLMEKLKKK AAMVVSEEDH LKAEARGDMS EAELLILDEF
     TTLARDLYAF YPLLIRFVDY NRAKWLKEPT PEAEELFRMV AEVFIYWSKS HNFKREEQNF
     VVQNEINNMS FLITDTKSKM SKAAVSDQER KKMKRKGDRY SMQTSLIVAA LKRLLPIGLN
     ICAPGDQELI ALAKNRFSLK ATEDEVRDII RNNIHLQGKL EDPAIRWQMA LYKDLPNRTE
     ETSDPEKTVE RVLDIANVLF HLEQKSKFIG RRYYNLVEHP QRSKKAVWHK LLSKQRKRAV
     VACFRMAPLY NLPRHRAVNL FLQGYEKSWI ETEEHYFEDK LIEDLAKPGA EPPEEDEVTK
     RVDPLHQLIL LFSRTALTEK CKLEEDFLYM AYADIMAKSC HDEEDDDGEE EVKSFEEKEM
     EKQKLLYQQA RLHDRGAAEM VLQTISASKG ETGPMVAATL KLGIAILNGG NSTVQQKMLD
     YLKEKKDVGF FQSLAGLMQS CSVLDLNAFE RQNKAEGLGM VTEEGSGEKV LQDDEFTCDL
     FRFLQLLCEG HNSDFQNYLR TQTGNNTTVN IIISTVDYLL RVQESISDFY WYYSGKDVID
     EQGQRNFSKA IQVAKQVFNT LTEYIQGPCT GNQQSLAHSR LWDAVVGFLH VFAHMQMKLS
     QDSSQIELLK ELMDLQKDMV VMLLSMLEGN VVNGTIGKQM VDMLVESSNN VEMILKFFDM
     FLKLKDLTSS DTFKEYDPDG KGIISKRDFH KAMESHKHYT QSETEFLLSC AETDENETLD
     YEEFVKRFHE PAKDIGFNVA VLLTNLSEHM PNDTRLQTFL ELAESVLNYF QPFLGRIEIM
     GSAKRIERVY FEISESSRTQ WEKPQVKESK RQFIFDVVNE GGEKEKMELF VNFCEDTIFE
     MQLAAQISES DLNERSANKE ESEKERPEEQ GPKMGFFSVL TVRSALFALR YNILTLMRML
     SLKSLKKQMK KMKKMTVKDM VTAFFSSYWS IFMTLLHFVA SVFRGFFRIV CSLLLGGSLV
     EGAKKIKVAE LLANMPDPTQ DEVRGDGEEG ERKPMETTLP SEDLTDLKEL TEESDLLSDI
     FGLDLKREGG QYKLIPHNPN AGLSDLMSNP VLIPEEQEKF QEQKTKEEEK EEKEETKSEP
     EKAEGEDGEK EEKVKEDKGK QKLRQLHTHR YGEPEVPESA FWKKIIAYQQ KLLNYLARNF
     YNMRMLALFV AFAINFILLF YKVSTSSVVE GKELPSRSTS ENAKVTTSLD SSSHRIIAVH
     YVLEESSGYM EPTLRILAIL HTVISFFCII GYYCLKVPLV IFKREKEVAR KLEFDGLYIT
     EQPSEDDIKG QWDRLVINTQ SFPNNYWDKF VKRKVMDKYG EFYGRDRISE LLGMDKAALD
     FSDAREKKKP KKDSSLSAVL NSIDVKYQMW KLGVVFTDNS FLYLAWYMTM SILGHYNNFF
     FAAHLLDIAM GFKTLRTILS SVTHNGKQLV LTVGLLAVVV YLYTVVAFNF FRKFYNKSED
     GDTPDMKCDD MLTCYMFHMY VGVRAGGGIG DEIEDPAGDE YEIYRIIFDI TFFFFVIVIL
     LAIIQGLIID AFGELRDQQE QVKEDMETKC FICGIGNDYF DTVPHGFETH TLQEHNLANY
     LFFLMYLINK DETEHTGQES YVWKMYQERC WEFFPAGDCF RKQYEDQLN
//
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