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Peripheral plasma membrane protein CASK (dCASK) (EC 2.7.11.17) (Calcium/calmodulin-dependent protein kinase) (CAKI) (Camguk)

 CSKP_DROME              Reviewed;         898 AA.
Q24210; B5X553; Q24272; Q86P03; Q86P17; Q8SX09; Q9VD77; Q9VD78;
Q9VD79;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
22-AUG-2003, sequence version 4.
30-AUG-2017, entry version 183.
RecName: Full=Peripheral plasma membrane protein CASK;
Short=dCASK;
EC=2.7.11.17;
AltName: Full=Calcium/calmodulin-dependent protein kinase;
Short=CAKI;
Short=Camguk;
Name=CASK; Synonyms=Caki, cmg; ORFNames=CG6703;
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 [MRNA] (ISOFORM B).
STRAIN=Oregon-R;
PubMed=9178262; DOI=10.1016/S0925-4773(97)00668-0;
Dimitratos S.D., Woods D.F., Bryant P.J.;
"Camguk, Lin-2, and CASK: novel membrane-associated guanylate kinase
homologs that also contain CaM kinase domains.";
Mech. Dev. 63:127-130(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND TISSUE SPECIFICITY.
TISSUE=Embryo;
PubMed=8617233;
Martin J.-R., Ollo R.;
"A new Drosophila Ca2+/calmodulin-dependent protein kinase (Caki) is
localized in the central nervous system and implicated in walking
speed.";
EMBO J. 15:1865-1876(1996).
[3]
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).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
STRAIN=Berkeley; TISSUE=Embryo, and Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
STRAIN=Berkeley; TISSUE=Embryo, and Head;
Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C.,
Celniker S.E.;
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, AND INTERACTION WITH CAMKII.
PubMed=14687552; DOI=10.1016/S0896-6273(03)00786-4;
Lu C.S., Hodge J.J., Mehren J., Sun X.X., Griffith L.C.;
"Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-
dependent autophosphorylation.";
Neuron 40:1185-1197(2003).
[8]
FUNCTION, INTERACTION WITH EAG, AND SUBCELLULAR LOCATION.
PubMed=15901771; DOI=10.1523/JNEUROSCI.4566-04.2005;
Marble D.D., Hegle A.P., Snyder E.D. II, Dimitratos S., Bryant P.J.,
Wilson G.F.;
"Camguk/CASK enhances Ether-a-go-go potassium current by a
phosphorylation-dependent mechanism.";
J. Neurosci. 25:4898-4907(2005).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16880127; DOI=10.1016/j.neuron.2006.06.020;
Hodge J.J., Mullasseril P., Griffith L.C.;
"Activity-dependent gating of CaMKII autonomous activity by Drosophila
CASK.";
Neuron 51:327-337(2006).
-!- FUNCTION: May regulate transmembrane proteins that bind calcium,
calmodulin, or nucleotides. Functionally modulates eag potassium
channels; increases eag current and whole-cell conductance. Also
regulates autophosphorylation of CaMKII.
{ECO:0000269|PubMed:14687552, ECO:0000269|PubMed:15901771,
ECO:0000269|PubMed:16880127}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with eag. Interacts with CaMKII.
{ECO:0000269|PubMed:14687552, ECO:0000269|PubMed:15901771}.
-!- INTERACTION:
Q00168:CaMKII; NbExp=5; IntAct=EBI-214423, EBI-124595;
Q02280:eag; NbExp=10; IntAct=EBI-214423, EBI-85304;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15901771};
Peripheral membrane protein {ECO:0000269|PubMed:15901771}.
Note=Eag recruits CASK to the plasma membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=B;
IsoId=Q24210-3; Sequence=Displayed;
Name=A;
IsoId=Q24210-2; Sequence=VSP_008088, VSP_008089, VSP_008090;
Note=No experimental confirmation available.;
Name=G;
IsoId=Q24210-4; Sequence=VSP_008088, VSP_008089, VSP_008090,
VSP_041854;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: During embryogenesis, larval and pupal life,
found almost exclusively in the central nervous system. In the
adult head found in the lamina, the neuropil of the medulla,
lobula, lobula plate and in the central brain.
{ECO:0000269|PubMed:8617233}.
-!- DISRUPTION PHENOTYPE: Increases synapse-specific, activity-
dependent autophosphorylation of CaMKII Thr-287.
{ECO:0000269|PubMed:16880127}.
-!- SIMILARITY: In the N-terminal section; belongs to the protein
kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK
subfamily. {ECO:0000305}.
-!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM11269.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=AAO39536.1; Type=Frameshift; Positions=114; Evidence={ECO:0000305};
Sequence=CAA63940.1; Type=Frameshift; Positions=537, 667; Evidence={ECO:0000305};
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EMBL; U53190; AAC80169.1; -; mRNA.
EMBL; X94264; CAA63940.1; ALT_FRAME; mRNA.
EMBL; AE014297; AAF55920.3; -; Genomic_DNA.
EMBL; AE014297; AAF55921.2; -; Genomic_DNA.
EMBL; AE014297; AAF55922.2; -; Genomic_DNA.
EMBL; AY094916; AAM11269.1; ALT_SEQ; mRNA.
EMBL; BT003532; AAO39536.1; ALT_FRAME; mRNA.
EMBL; BT003550; AAO39554.1; -; mRNA.
EMBL; BT046172; ACI49771.1; -; mRNA.
PIR; S69210; S69210.
RefSeq; NP_001097862.1; NM_001104392.3. [Q24210-2]
RefSeq; NP_524441.2; NM_079717.4. [Q24210-3]
RefSeq; NP_732661.1; NM_169970.2. [Q24210-2]
RefSeq; NP_732662.2; NM_169971.3. [Q24210-4]
UniGene; Dm.7404; -.
ProteinModelPortal; Q24210; -.
SMR; Q24210; -.
BioGrid; 67530; 10.
DIP; DIP-19769N; -.
IntAct; Q24210; 7.
STRING; 7227.FBpp0303394; -.
TCDB; 9.B.106.3.2; the pock size-determining protein (psdp) family.
PaxDb; Q24210; -.
PRIDE; Q24210; -.
EnsemblMetazoa; FBtr0084161; FBpp0083559; FBgn0013759. [Q24210-3]
EnsemblMetazoa; FBtr0084162; FBpp0083560; FBgn0013759. [Q24210-2]
EnsemblMetazoa; FBtr0112872; FBpp0111785; FBgn0013759. [Q24210-2]
EnsemblMetazoa; FBtr0301328; FBpp0290543; FBgn0013759. [Q24210-4]
GeneID; 42567; -.
KEGG; dme:Dmel_CG6703; -.
CTD; 8573; -.
FlyBase; FBgn0013759; CASK.
eggNOG; KOG0033; Eukaryota.
eggNOG; KOG0609; Eukaryota.
eggNOG; COG0194; LUCA.
GeneTree; ENSGT00760000118866; -.
InParanoid; Q24210; -.
KO; K06103; -.
OMA; HCSWFGR; -.
OrthoDB; EOG091G065I; -.
PhylomeDB; Q24210; -.
BRENDA; 2.7.11.17; 1994.
Reactome; R-DME-212676; Dopamine Neurotransmitter Release Cycle.
Reactome; R-DME-6794361; Interactions of neurexins and neuroligins at synapses.
SignaLink; Q24210; -.
GenomeRNAi; 42567; -.
PRO; PR:Q24210; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0013759; -.
Genevisible; Q24210; DM.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0031594; C:neuromuscular junction; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0061174; C:type I terminal bouton; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
GO; GO:0042043; F:neurexin family protein binding; IPI:BHF-UCL.
GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
GO; GO:0007628; P:adult walking behavior; IMP:FlyBase.
GO; GO:0007615; P:anesthesia-resistant memory; IMP:FlyBase.
GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0007163; P:establishment or maintenance of cell polarity; NAS:FlyBase.
GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
GO; GO:0040011; P:locomotion; IMP:BHF-UCL.
GO; GO:0007616; P:long-term memory; IMP:FlyBase.
GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
GO; GO:0072375; P:medium-term memory; IMP:FlyBase.
GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:BHF-UCL.
GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:FlyBase.
GO; GO:0040012; P:regulation of locomotion; IMP:FlyBase.
GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IMP:FlyBase.
GO; GO:0046928; P:regulation of neurotransmitter secretion; IDA:FlyBase.
GO; GO:0008582; P:regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:2000331; P:regulation of terminal button organization; IMP:BHF-UCL.
GO; GO:0016081; P:synaptic vesicle docking; NAS:FlyBase.
GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:BHF-UCL.
GO; GO:0016080; P:synaptic vesicle targeting; NAS:FlyBase.
CDD; cd12081; SH3_CASK; 1.
Gene3D; 1.10.287.650; -; 2.
InterPro; IPR035473; CASK_SH3.
InterPro; IPR008145; GK/Ca_channel_bsu.
InterPro; IPR008144; Guanylate_kin-like_dom.
InterPro; IPR020590; Guanylate_kinase_CS.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR014775; L27_C.
InterPro; IPR004172; L27_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001478; PDZ.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR011511; SH3_2.
InterPro; IPR001452; SH3_domain.
Pfam; PF00625; Guanylate_kin; 1.
Pfam; PF02828; L27; 2.
Pfam; PF00595; PDZ; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF07653; SH3_2; 1.
SMART; SM00072; GuKc; 1.
SMART; SM00569; L27; 2.
SMART; SM00228; PDZ; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF101288; SSF101288; 2.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
PROSITE; PS51022; L27; 2.
PROSITE; PS50106; PDZ; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane;
Complete proteome; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat;
Serine/threonine-protein kinase; SH3 domain; Transferase.
CHAIN 1 898 Peripheral plasma membrane protein CASK.
/FTId=PRO_0000094571.
DOMAIN 12 278 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 343 397 L27 1. {ECO:0000255|PROSITE-
ProRule:PRU00365}.
DOMAIN 402 461 L27 2. {ECO:0000255|PROSITE-
ProRule:PRU00365}.
DOMAIN 495 576 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 582 651 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 711 883 Guanylate kinase-like.
{ECO:0000255|PROSITE-ProRule:PRU00100}.
NP_BIND 18 26 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00100, ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 306 316 Calmodulin-binding.
ACT_SITE 141 141 {ECO:0000250}.
BINDING 41 41 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 292 292 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
VAR_SEQ 1 317 Missing (in isoform A and isoform G).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_008088.
VAR_SEQ 318 443 MDPLYATDADMPITGATDEWADEEAGIEAVQRILDCLDDIY
SLQDAHVDADVLRDMLRDNRLHQFLQLFDRIAATVVTSNGR
APAAEAVGRCRDVLEQLSSTSGGNSLGGKYAKEELMRLLAA
PHM -> MCQHHGLTSQSLMSGGSHISLLGSSGSSGMSGSG
VGSSGQSVPQCPAAVAAADAAMMGSNAGGHCRSLSGLSSIS
IPPPPPALFNPCSSALSLQQAAVTRWGPRTSCPVHSPFRVR
VPNGSICSGH (in isoform A and isoform G).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_008089.
VAR_SEQ 584 584 E -> ELFRIRPAPVL (in isoform A and
isoform G).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_008090.
VAR_SEQ 663 663 Q -> QGEPGAGCSAHADGCDGSA (in isoform G).
{ECO:0000305}.
/FTId=VSP_041854.
CONFLICT 7 7 L -> V (in Ref. 1; AAC80169).
{ECO:0000305}.
CONFLICT 136 136 D -> E (in Ref. 1; AAC80169).
{ECO:0000305}.
CONFLICT 463 463 L -> A (in Ref. 1; AAC80169).
{ECO:0000305}.
CONFLICT 465 477 VTPPPMVPYLNGD -> HPAPDGALPQWR (in Ref. 1;
AAC80169). {ECO:0000305}.
CONFLICT 497 497 Q -> H (in Ref. 1; AAC80169).
{ECO:0000305}.
CONFLICT 523 523 I -> L (in Ref. 1; AAC80169).
{ECO:0000305}.
CONFLICT 632 632 D -> G (in Ref. 1; AAC80169).
{ECO:0000305}.
CONFLICT 740 740 A -> V (in Ref. 1; AAC80169).
{ECO:0000305}.
CONFLICT 759 759 S -> N (in Ref. 5; AAO39554).
{ECO:0000305}.
CONFLICT 886 892 HTTPQWV -> DIPPRSGC (in Ref. 2;
CAA63940). {ECO:0000305}.
SEQUENCE 898 AA; 100911 MW; 5B16014EC66E0E9B CRC64;
MTEDEILFDD VYELCEVIGK GPFSIVRRCI HRESNQQFAV KIVDVAKFTA SPGLSTADLK
REATICHMLK HPHIVELLET YSSEGMLYMV FEFMEGSDLC FEVVRRAVAG FVYSEAVACH
YMRQILEALR YCHENDILHR DVRPACALLA TVDNSAPVKL GGFGSAIQLP GTRETIETHG
RVGCPHYMAP EVVTRRLYGK GCDVWGAGVM LHVLLSGRLP FLGSGVRLQQ SVARGRLSFE
APEWKSISAN AKDLVMKMLA ANPHHRLSIT EVLDHPWIRD RDKLQRTHLA DTVEELKRYN
ARRKLKGAVQ AIAGGTNMDP LYATDADMPI TGATDEWADE EAGIEAVQRI LDCLDDIYSL
QDAHVDADVL RDMLRDNRLH QFLQLFDRIA ATVVTSNGRA PAAEAVGRCR DVLEQLSSTS
GGNSLGGKYA KEELMRLLAA PHMQALLHSH DVVARDVYGE EALRVTPPPM VPYLNGDELD
NVEGGELQHV TRVRLVQFQK NTDEPMGITL KMTEDGRCIV ARIMHGGMIH RQATLHVGDE
IREINGQPVQ HQSVGQLQRM LREARGSVTF KIVPSYRSAP PPCEIFVRAQ FDYNPLDDEL
IPCAQAGISF QVGDILQIIS KDDHHWWQAR LDTVGGSAGL IPSPELQEWR IACQTVDKTK
QEQVNCSIFG RKKKQCRDKY LAKHNAIFDT LDVVTYEEVV KVPVGDPNFQ RKTLVLLGAH
GVGRRHIKNT LISKYPDKYA YPIPHTTRPA KPEEENGRSY YFVSHDEMMA DIGANEYLEY
GTHEDAMYGT KLDTIRRIHT EGKMAILDVE PQALKILRTA EFTPYVVFIA APSLQNIADY
DGSLERLAKE SEMLRQLYGH FFDLTIVNND ISETIATLET AIDRVHTTPQ WVPVSWLY


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