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Serine/threonine-protein kinase Tor (EC 2.7.11.1) (Target of rapamycin)

 TOR_DROME               Reviewed;        2470 AA.
Q9VK45;
16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-DEC-2018, entry version 154.
RecName: Full=Serine/threonine-protein kinase Tor;
EC=2.7.11.1;
AltName: Full=Target of rapamycin;
Name=Tor; ORFNames=CG5092;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-1956.
PubMed=11069885; DOI=10.1101/gad.845700;
Oldham S., Montagne J., Radimerski T., Thomas G., Hafen E.;
"Genetic and biochemical characterization of dTOR, the Drosophila
homolog of the target of rapamycin.";
Genes Dev. 14:2689-2694(2000).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11069888; DOI=10.1101/gad.835000;
Zhang H., Stallock J.P., Ng J.C., Reinhard C., Neufeld T.P.;
"Regulation of cellular growth by the Drosophila target of rapamycin
dTOR.";
Genes Dev. 14:2712-2724(2000).
[5]
FUNCTION.
PubMed=14505573; DOI=10.1016/S0092-8674(03)00713-X;
Colombani J., Raisin S., Pantalacci S., Radimerski T., Montagne J.,
Leopold P.;
"A nutrient sensor mechanism controls Drosophila growth.";
Cell 114:739-749(2003).
[6]
REVIEW.
PubMed=12559758; DOI=10.1016/S0962-8924(02)00042-9;
Oldham S., Hafen E.;
"Insulin/IGF and target of rapamycin signaling: a TOR de force in
growth control.";
Trends Cell Biol. 13:79-85(2003).
[7]
FUNCTION.
PubMed=15454083; DOI=10.1016/j.cell.2004.08.028;
Bateman J.M., McNeill H.;
"Temporal control of differentiation by the insulin receptor/tor
pathway in Drosophila.";
Cell 119:87-96(2004).
[8]
REVIEW.
PubMed=16469695; DOI=10.1016/j.cell.2006.01.016;
Wullschleger S., Loewith R., Hall M.N.;
"TOR signaling in growth and metabolism.";
Cell 124:471-484(2006).
[9]
SUBUNIT.
PubMed=16219781; DOI=10.1534/genetics.105.051979;
Zhang Y., Billington C.J. Jr., Pan D., Neufeld T.P.;
"Drosophila target of rapamycin kinase functions as a multimer.";
Genetics 172:355-362(2006).
[10]
FUNCTION.
PubMed=18604198; DOI=10.1038/ncb1753;
Kim E., Goraksha-Hicks P., Li L., Neufeld T.P., Guan K.L.;
"Regulation of TORC1 by Rag GTPases in nutrient response.";
Nat. Cell Biol. 10:935-945(2008).
[11]
FUNCTION, AND INDUCTION.
PubMed=19211682; DOI=10.1242/dev.027466;
Demontis F., Perrimon N.;
"Integration of Insulin receptor/Foxo signaling and dMyc activity
during muscle growth regulates body size in Drosophila.";
Development 136:983-993(2009).
[12]
REVIEW.
PubMed=18992839; DOI=10.1016/j.biocel.2008.10.010;
Grewal S.S.;
"Insulin/TOR signaling in growth and homeostasis: a view from the fly
world.";
Int. J. Biochem. Cell Biol. 41:1006-1010(2009).
[13]
FUNCTION.
PubMed=19225150; DOI=10.1091/mbc.E08-12-1250;
Chang Y.Y., Neufeld T.P.;
"An Atg1/Atg13 complex with multiple roles in TOR-mediated autophagy
regulation.";
Mol. Biol. Cell 20:2004-2014(2009).
[14]
FUNCTION.
PubMed=25920570; DOI=10.1016/j.devcel.2015.03.013;
Tiebe M., Lutz M., De La Garza A., Buechling T., Boutros M.,
Teleman A.A.;
"REPTOR and REPTOR-BP regulate organismal metabolism and transcription
downstream of TORC1.";
Dev. Cell 33:272-284(2015).
-!- FUNCTION: Promotes cell and tissue growth, maintains tissue
homeostatis and controls responses to environmental stress and
aging (PubMed:11069885, PubMed:11069888, PubMed:19211682,
PubMed:19225150). Regulates growth during animal development by
coupling growth factor signaling to nutrient availability
(PubMed:11069888). Central regulators of autophagy
(PubMed:18604198, PubMed:19225150). May be involved in atg1
phosphorylation (PubMed:19225150). May also be involved, directly
or indirectly, in the control of neuronal function
(PubMed:15454083). Phosphorylates S6K/p70S6K, in vitro
(PubMed:11069888). May regulate the activity of S6K
(PubMed:11069885). Overexpression inhibits growth and reduces cell
size (PubMed:14505573). Affects the timing of neuronal cell
differentiation (PubMed:15454083). Hyperactivation of the
signaling leads to accelerated differentiation, whereas inhibition
of the signaling retards differentiation (PubMed:15454083). Thus,
in addition to controlling growth of the cell in which it resides,
it can also influence growth of distant cells and organs during
development via a humoral mechanism (PubMed:14505573). As part of
the TORC1 complex regulates energy homeostasis and promotes
certain aspects of larval growth by negatively regulating REPTOR
(PubMed:25920570). REPTOR functions downstream of TORC1 to
regulate the expression of stress response genes in response to
TORC1 inhibition resulting from nutrient deprivation
(PubMed:25920570). When TORC1 activity is high it phosphorylates
REPTOR which inhibits its recruitment into the nucleus and
antagonizes their function (PubMed:25920570). This function is
essential under normal feeding conditions to promote TORC1-
dependent growth during larval development and, in adults and
larvae to prevent the REPTOR-dependent expression of nutrient
stress response genes (PubMed:25920570). In short, during
development, it primarily controls growth, whereas in the adult,
where there is relatively little growth, it controls aging and
other aspects of nutrient-related physiology (PubMed:11069885,
PubMed:11069888, PubMed:19211682, PubMed:19225150). Rag GTPases
act as activators of TORC1 in response to amino acid signals
(PubMed:18604198). {ECO:0000269|PubMed:11069885,
ECO:0000269|PubMed:11069888, ECO:0000269|PubMed:14505573,
ECO:0000269|PubMed:15454083, ECO:0000269|PubMed:18604198,
ECO:0000269|PubMed:19211682, ECO:0000269|PubMed:19225150,
ECO:0000269|PubMed:25920570}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- SUBUNIT: May be part of a minimal complex, TORC1, consisting of
tor, raptor and lst8. May be part of a minimal complex, TORC2,
consisting of tor, rictor and lst8 (By similarity). Self-
associates; assembles into homomultimeric complexes. Component of
a multiprotein complex. {ECO:0000250,
ECO:0000269|PubMed:16219781}.
-!- INDUCTION: By PI3K/Akt signaling, or by nutrients such as amino
acids, and by high cellular energy levels.
{ECO:0000269|PubMed:19211682}.
-!- DISRUPTION PHENOTYPE: Not lethal. Displays phenotypes
characteristic of amino acid deprivation, including reduced
nucleolar size, lipid vesicle aggregation in the larval fat body,
and a cell type-specific pattern of cell cycle arrest that can be
bypassed by overexpression of the S-phase regulator cyclin E.
Reach only the size of second instar larvae, at which point they
undergo cell cycle arrest. {ECO:0000269|PubMed:11069885,
ECO:0000269|PubMed:11069888}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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EMBL; AE014134; AAF53237.1; -; Genomic_DNA.
RefSeq; NP_524891.1; NM_080152.3.
UniGene; Dm.1502; -.
ProteinModelPortal; Q9VK45; -.
SMR; Q9VK45; -.
BioGrid; 70789; 44.
IntAct; Q9VK45; 16.
STRING; 7227.FBpp0080003; -.
PaxDb; Q9VK45; -.
PRIDE; Q9VK45; -.
EnsemblMetazoa; FBtr0080422; FBpp0080003; FBgn0021796.
GeneID; 47396; -.
KEGG; dme:Dmel_CG5092; -.
UCSC; CG5092-RA; d. melanogaster.
FlyBase; FBgn0021796; Tor.
eggNOG; KOG0891; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00930000151037; -.
InParanoid; Q9VK45; -.
KO; K07203; -.
OMA; LNIQRYP; -.
OrthoDB; EOG091G0046; -.
PhylomeDB; Q9VK45; -.
Reactome; R-DME-1257604; PIP3 activates AKT signaling.
Reactome; R-DME-1632852; Macroautophagy.
Reactome; R-DME-165159; mTOR signalling.
Reactome; R-DME-166208; mTORC1-mediated signalling.
Reactome; R-DME-3371571; HSF1-dependent transactivation.
Reactome; R-DME-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-DME-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
SignaLink; Q9VK45; -.
ChiTaRS; Egfr; fly.
GenomeRNAi; 47396; -.
PRO; PR:Q9VK45; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0021796; Expressed in 30 organ(s), highest expression level in eye disc (Drosophila).
ExpressionAtlas; Q9VK45; baseline and differential.
Genevisible; Q9VK45; DM.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0031931; C:TORC1 complex; IMP:UniProtKB.
GO; GO:0031932; C:TORC2 complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0031490; F:chromatin DNA binding; IDA:FlyBase.
GO; GO:0043621; F:protein self-association; IDA:FlyBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:FlyBase.
GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
GO; GO:0006914; P:autophagy; IMP:FlyBase.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0031670; P:cellular response to nutrient; IDA:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0032456; P:endocytic recycling; IDA:FlyBase.
GO; GO:0048142; P:germarium-derived cystoblast division; IMP:FlyBase.
GO; GO:0008406; P:gonad development; IMP:FlyBase.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:FlyBase.
GO; GO:0035171; P:lamellocyte differentiation; IDA:FlyBase.
GO; GO:0035096; P:larval midgut cell programmed cell death; IMP:FlyBase.
GO; GO:0035264; P:multicellular organism growth; IMP:FlyBase.
GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
GO; GO:0010507; P:negative regulation of autophagy; IBA:GO_Central.
GO; GO:0016242; P:negative regulation of macroautophagy; IMP:FlyBase.
GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IDA:FlyBase.
GO; GO:1902669; P:positive regulation of axon guidance; IGI:FlyBase.
GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:FlyBase.
GO; GO:0030307; P:positive regulation of cell growth; TAS:FlyBase.
GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:FlyBase.
GO; GO:0040018; P:positive regulation of multicellular organism growth; TAS:FlyBase.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:FlyBase.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:FlyBase.
GO; GO:0090070; P:positive regulation of ribosome biogenesis; IMP:FlyBase.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IGI:FlyBase.
GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:FlyBase.
GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
GO; GO:0001558; P:regulation of cell growth; IDA:FlyBase.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IGI:FlyBase.
GO; GO:2001023; P:regulation of response to drug; IMP:FlyBase.
GO; GO:2000331; P:regulation of terminal button organization; IMP:FlyBase.
GO; GO:0007584; P:response to nutrient; TAS:FlyBase.
GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
GO; GO:0038202; P:TORC1 signaling; IMP:UniProtKB.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 1.20.120.150; -; 1.
Gene3D; 1.25.10.10; -; 3.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR024585; DUF3385_TOR.
InterPro; IPR003152; FATC_dom.
InterPro; IPR009076; FRB_dom.
InterPro; IPR036738; FRB_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003151; PIK-rel_kinase_FAT.
InterPro; IPR014009; PIK_FAT.
InterPro; IPR026683; TOR.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR11139:SF9; PTHR11139:SF9; 1.
Pfam; PF11865; DUF3385; 1.
Pfam; PF02259; FAT; 1.
Pfam; PF02260; FATC; 1.
Pfam; PF08771; FRB_dom; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
SMART; SM01346; DUF3385; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF47212; SSF47212; 1.
SUPFAM; SSF48371; SSF48371; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51189; FAT; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
PROSITE; PS50005; TPR; 2.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Complete proteome; Kinase;
Nucleotide-binding; Reference proteome; Repeat; TPR repeat;
Transferase.
CHAIN 1 2470 Serine/threonine-protein kinase Tor.
/FTId=PRO_0000377458.
REPEAT 172 209 HEAT 1. {ECO:0000255}.
REPEAT 746 785 HEAT 2. {ECO:0000255}.
REPEAT 791 829 HEAT 3. {ECO:0000255}.
REPEAT 835 873 HEAT 4. {ECO:0000255}.
REPEAT 962 999 HEAT 5. {ECO:0000255}.
REPEAT 1043 1080 HEAT 6. {ECO:0000255}.
REPEAT 1083 1122 HEAT 7. {ECO:0000255}.
REPEAT 1124 1160 HEAT 8. {ECO:0000255}.
DOMAIN 1349 1903 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
REPEAT 1407 1440 TPR 1. {ECO:0000255, ECO:0000255|PROSITE-
ProRule:PRU00339}.
REPEAT 1718 1751 TPR 2. {ECO:0000255|PROSITE-
ProRule:PRU00339}.
REPEAT 1854 1891 HEAT 9. {ECO:0000255}.
DOMAIN 2103 2470 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 2438 2470 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
COMPBIAS 293 297 Poly-Ser.
MUTAGEN 1956 1956 S->T: Rapamycin resistance and loss of
activity. {ECO:0000269|PubMed:11069885}.
SEQUENCE 2470 AA; 281033 MW; 5D78D2ECC07C7FF9 CRC64;
MSTTSVVQQF VNGLKSRNRN VQNKATQDLL FYVKTELREM SQEELAQFFD EFDHHIFTMV
NATDINEKKG GALAMKCLIN CEGSLTARKG ISPYLNRLRD LLLINDVSVM EIAARSLVKL
ANMPTSKGAD SFDFDIKKAF EVLRGERQEY RRHSAVFILR ELAIALPTYF YQHILTFFEV
IFNAIFDPKP AIRESAGEAL RAALIVTAQR ESTKQSSEPQ WYRICYDEAN GSFNADLGSS
KDQKGVTRDD RIHGGLVVFN ELFRCANATW ERRYTSLKTL FPKTQHNKFL EASSSSSMGS
QLNTLVPRLK VPFIDKLGST QTHLGEGEHH KGVAKFASHN VLESAYAQEI LQEHYTSICD
NVLEQRTSKS PYVQQALLQI LPRLAAFNRA VFVEKYLQTC VSHLMQILRG KEKDRTVAYI
TIGYMAVAVQ SAIEVHLSSI MTSVKVALPS KDLTSKRKVP VDPAVFACIT LLAHAVKSEI
ADDVKDILEQ MFYTGLSPAL TVCLRELSEN VPQLKSAITE GLIGILSQVL MNKAAILPYT
ALPTIAIDGS LMQNGDGATT VLALKTLGTF NFEEQNMLDF VQRCADYFIV HEQQEIRLEA
VQTCTRLLKL AVQSSESMEN SKTLSDTVSH VIERLLMVAI TDMDCNVRIR ILRSLDETFD
GKLAQPESLN SLFITLHDEI FEIRELAMVT IGRLSSINPA YVMPKLRTTM IELITDLKYS
GMSRNKEQSA KMLDHLVIST PRLISSYMNP ILKALVPKLH EPESNPGVIL NVLRTIGDLA
EVNGGSDEME LWADDLLSIL LEMLGDAGSP DKRGVALWTL GQLISATGRV VTPYHKYPVL
IDILINFLKT EQRRSIRRET IRVLGLLGAM DPYKHKMNKG LIDSQKDNVL IAYSDGKVDE
SQDISTAELL VNMGNALDEY YPAVAIAALM RILRDPTLST RHTSVVQAVT FIFQSLGIKC
VPYLAQVLPN LLDNVRTADN NLREFLFQQL AILVAFVKLH IISYMGDIFK LIKEFWTINT
PLQNTLINLI EQIAVALGCE FRDYLAELIP QILRVLQHDN SKDRMVTRRL LQALQKFGST
LGYYLPLILP PIVKLFDSPY VPQQVSMVAL ETINNLACQL DFTDFSSRII HPLVRVLDAE
PELRDQAMTT LRSLAKQLGK KYLVFVPMVQ RTLNKHRIVD PEYEELLSKI KSCSTLADSY
GAGESELRPS RFKNNEPFVT DRNSNNKNLQ VTTNELRTAW QVTRRVSKDD WVEWLKRLSI
GLLKESPSHA LRACRSLAQE YDTLLRDLFN AAFISCWTEL SPDLKNELTQ SLIQALQVTD
MPEITQTILN LAEFMEHCDR DPIPIETKLL GTRAMACRAY AKALRYKEEE FLLREDSQVF
ESLILINNKL QQREAAEGLL TRYRNAANEL NVQGRWYEKL HNWDEALEHY ERNLKTDSSD
LEARLGHMRC LEALGDWSEL SNVTKHEWEN FGTEAKSRAG PLAAVAAWGL QDWEAMREYV
RCIPEDTQDG SYYRAVLAVH HDDFETAQRL IDETRDLLDT ELTSMAGESY ERAYGAMVCV
QMLAELEEVI QYKLIPERRE PLKTMWWKRL QGGQRLVEDW RRIIQVHSLV VKPHEDIHTW
LKYASLCRKS GSLHLSHKTL VMLLGTDPKL NPNQPLPCNQ PQVTYAYTKY MAANNQLQEA
YEQLTHFVST YSQELSCLPP EALKQQDQRL MARCYLRMAT WQNKLQDSIR PDAIQGALEC
FEKATSYDPN WYKAWHLWAY MNFKVVQAQK SALDKQQPPG ASMGMTMGSG LDSDLMIIQR
YAVPAVQGFF RSISLIKGNS LQDTLRLLTL WFDYGNHAEV YEALLSGMKL IEINTWLQVI
PQLIARIDTH RQLVGQLIHQ LLMDIGKNHP QALVYPLTVA SKSASLARRN AAFKILDSMR
KHSPTLVEQA VMCSEELIRV AILWHEQWHE GLEEASRLYF GDRNVKGMFE ILEPLHAMLE
RGPQTLKETS FSQAYGRELT EAYEWSQRYK TSAVVMDLDR AWDIYYHVFQ KISRQLPQLT
SLELPYVSPK LMTCKDLELA VPGSYNPGQE LIRISIIKTN LQVITSKQRP RKLCIRGSNG
KDYMYLLKGH EDLRQDERVM QLFSLVNTLL LDDPDTFRRN LAIQRYAVIP LSTNSGLIGW
VPHCDTLHTL IRDYRDKKKV PLNQEHRTML NFAPDYDHLT LMQKVEVFEH ALGQTQGDDL
AKLLWLKSPS SELWFERRNN YTRSLAVMSM VGYILGLGDR HPSNLMLDRM SGKILHIDFG
DCFEVAMTRE KFPEKIPFRL TRMLIKAMEV TGIEGTYRRT CESVMLVLRR NKDSLMAVLE
AFVYDPLLNW RLLDVDKKGN DAVAGAGAPG GRGGSGMQDS LSNSVEDSLP MAKSKPYDPT
LQQGGLHNNV ADETNSKASQ VIKRVKCKLT GTDFQTEKSV NEQSQVELLI QQATNNENLC
QCYIGWCPFW


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