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Database: UniProt
Entry: RYR3_RABIT
LinkDB: RYR3_RABIT
Original site: 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   16-JAN-2019, entry version 122.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   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
RT   receptor/calcium 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;
RP   MAGNESIUM; 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
RT   channel (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
RP   SPLICING, FUNCTION, SUBUNIT, INTERACTION WITH RYR2, AND TISSUE
RP   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
RT   variant of 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
RP   LOCATION, MEMBRANE TOPOLOGY, ELECTRON MICROSCOPY, REGULATION BY
RP   RYANODINE; CALCIUM LEVELS; MAGNESIUM; ATP AND CAFFEINE, AND TISSUE
RP   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)
RT   purified 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.,
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   [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
RT   cephalic 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
RT   of 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
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 in muscle and
CC       thereby plays a role in triggering muscle contraction. May
CC       regulate Ca(2+) release by other calcium channels. Calcium channel
CC       that mediates Ca(2+)-induced Ca(2+) release from the endoplasmic
CC       reticulum in non-muscle cells. Plays a role in cellular calcium
CC       signaling. Contributes to cellular calcium ion homeostasis.
CC       Isoform 2 lacks a predicted transmembrane segment and does not
CC       form functional calcium channels by itself; however, it can form
CC       tetramers with isoforms that contain the full complement of
CC       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
CC       1. Heterotetramer with RYR2. Interacts with FKBP1A. Interacts with
CC       CALM. Interacts with SELENON (PubMed:18713863).
CC       {ECO:0000269|PubMed:10358090, ECO:0000269|PubMed:12213830,
CC       ECO:0000269|PubMed:12471029, ECO:0000269|PubMed:16274254,
CC       ECO:0000269|PubMed:18713863, ECO:0000269|PubMed:9614063}.
CC   -!- INTERACTION:
CC       Self; 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-
CC       terminus and 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         Note=Lacks a predicted transmembrane segment and does not form
CC         functional calcium channels.;
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
CC       and in adult diaphragm muscle (at protein level). Detected in
CC       brain, especially in corpus striatum, thalamus and hippocampus.
CC       Detected in taenia coli, uterus, vas deferens, aorta, stomach,
CC       small intestine, heart, diaphragm and ureter. Isoform 2 is highly
CC       expressed in uterus and aorta, and at much lower levels in heart,
CC       brain and diaphragm. {ECO:0000269|PubMed:10358090,
CC       ECO:0000269|PubMed:12471029, ECO:0000269|PubMed:1330694,
CC       ECO:0000269|PubMed:16176801, ECO:0000269|PubMed:16274254,
CC       ECO:0000269|PubMed:9305876}.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitous in skeletal muscle in neonates and
CC       in 15 day old rabbits. In adult, detected in diaphragm muscle, and
CC       in a subset of skeletal muscles including digastricus,
CC       pterygoideus, tongue and masseter. {ECO:0000269|PubMed:16176801}.
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|PubMed:10358090}.
CC   -!- MISCELLANEOUS: Channel activity is modulated by the alkaloid
CC       ryanodine that binds to the open calcium-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 elevated cytoplasmic
CC       calcium levels in the micromolar range, by caffeine and adenine
CC       nucleotides, such as AMP and ATP. Inhibited by Mg(2+) and
CC       ruthenium red.
CC   -!- SIMILARITY: Belongs to the ryanodine receptor (TC 1.A.3.1) family.
CC       RYR3 subfamily. {ECO:0000305}.
DR   EMBL; X68650; CAC16153.1; -; mRNA.
DR   PIR; S27272; S27272.
DR   RefSeq; NP_001076231.1; NM_001082762.1. [Q9TS33-1]
DR   UniGene; Ocu.3278; -.
DR   ProteinModelPortal; Q9TS33; -.
DR   ComplexPortal; CPX-3157; Ryanodine 3 complex. [Q9TS33-1]
DR   STRING; 9986.ENSOCUP00000024658; -.
DR   PRIDE; Q9TS33; -.
DR   GeneID; 100009545; -.
DR   KEGG; ocu:100009545; -.
DR   CTD; 6263; -.
DR   eggNOG; KOG2243; Eukaryota.
DR   eggNOG; ENOG410YCNW; LUCA.
DR   HOGENOM; HOG000231428; -.
DR   HOVERGEN; HBG006699; -.
DR   KO; K04963; -.
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   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; IPR035762; SPRY3_RyR.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR13715; PTHR13715; 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   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Calmodulin-binding; Complete proteome; Endoplasmic reticulum;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Microsome; Receptor; Reference proteome; Repeat;
KW   Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   4872       Ryanodine receptor 3.
FT                                /FTId=PRO_0000415649.
FT   TOPO_DOM      1   4188       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   4189   4209       Helical. {ECO:0000255}.
FT   TRANSMEM   4412   4432       Helical. {ECO:0000255}.
FT   TRANSMEM   4487   4507       Helical. {ECO:0000255}.
FT   TRANSMEM   4612   4632       Helical. {ECO:0000255}.
FT   TRANSMEM   4635   4655       Helical. {ECO:0000255}.
FT   TRANSMEM   4674   4694       Helical. {ECO:0000255}.
FT   INTRAMEM   4725   4734       Pore-forming. {ECO:0000250}.
FT   TRANSMEM   4755   4775       Helical. {ECO:0000255}.
FT   TOPO_DOM   4776   4872       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      100    155       MIR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      162    207       MIR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      215    269       MIR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      275    333       MIR 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      343    400       MIR 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00131}.
FT   DOMAIN      585    796       B30.2/SPRY 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT      840    953       1.
FT   REPEAT      954   1068       2.
FT   DOMAIN     1012   1208       B30.2/SPRY 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   DOMAIN     1254   1466       B30.2/SPRY 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00548}.
FT   REPEAT     2592   2710       3.
FT   REPEAT     2711   2823       4.
FT   REGION      840   2823       4 X approximate repeats.
FT   REGION     2325   2338       Interaction with FKBP1A. {ECO:0000250}.
FT   REGION     3472   3501       Interaction with CALM.
FT                                {ECO:0000269|PubMed:16274254}.
FT   SITE       3885   3885       Important for activation by Ca(2+).
FT   VAR_SEQ    3341   3345       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:12471029,
FT                                ECO:0000303|PubMed:9305876}.
FT                                /FTId=VSP_042305.
FT   VAR_SEQ    4406   4434       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12471029}.
FT                                /FTId=VSP_042306.
FT   VAR_SEQ    4791   4841       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:12471029}.
FT                                /FTId=VSP_042307.
FT   MUTAGEN    3885   3885       E->A: Reduces calcium-sensitivity by over
FT                                10000-fold. {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
//
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