5HT1E_HUMAN
ID 5HT1E_HUMAN Reviewed; 365 AA.
AC P28566; E1P503; Q9P1Y1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=5-hydroxytryptamine receptor 1E;
DE Short=5-HT-1E;
DE Short=5-HT1E;
DE AltName: Full=S31;
DE AltName: Full=Serotonin receptor 1E;
GN Name=HTR1E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=1608964; DOI=10.1073/pnas.89.12.5517;
RA McAllister G., Charlesworth A., Snodin C., Beer M.S., Noble A.J.,
RA Middlemiss D.N., Iversen L.L., Whiting P.;
RT "Molecular cloning of a serotonin receptor from human brain (5HT1E): a
RT fifth 5HT1-like subtype.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5517-5521(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1733778; DOI=10.1016/0014-5793(92)80379-u;
RA Levy F.O., Gudermann T., Birnbaumer M., Kaumann A.J., Birnbaumer L.;
RT "Molecular cloning of a human gene (S31) encoding a novel serotonin
RT receptor mediating inhibition of adenylyl cyclase.";
RL FEBS Lett. 296:201-206(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1513320;
RA Zgombick J.M., Schechter L.E., Macchi M., Hartig P.R., Branchek T.A.,
RA Weinshank R.L.;
RT "Human gene S31 encodes the pharmacologically defined serotonin 5-
RT hydroxytryptamine1E receptor.";
RL Mol. Pharmacol. 42:180-185(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-363.
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14744596; DOI=10.1016/j.ejphar.2003.11.019;
RA Bai F., Yin T., Johnstone E.M., Su C., Varga G., Little S.P., Nelson D.L.;
RT "Molecular cloning and pharmacological characterization of the guinea pig
RT 5-HT1E receptor.";
RL Eur. J. Pharmacol. 484:127-139(2004).
RN [10]
RP REVIEW.
RX PubMed=18476671; DOI=10.1021/cr078224o;
RA Nichols D.E., Nichols C.D.;
RT "Serotonin receptors.";
RL Chem. Rev. 108:1614-1641(2008).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21422162; DOI=10.1124/jpet.111.179606;
RA Klein M.T., Dukat M., Glennon R.A., Teitler M.;
RT "Toward selective drug development for the human 5-hydroxytryptamine 1E
RT receptor: a comparison of 5-hydroxytryptamine 1E and 1F receptor structure-
RT affinity relationships.";
RL J. Pharmacol. Exp. Ther. 337:860-867(2011).
RN [12]
RP REVIEW.
RX PubMed=20945968; DOI=10.33549/physiolres.931903;
RA Pytliak M., Vargova V., Mechirova V., Felsoci M.;
RT "Serotonin receptors - from molecular biology to clinical applications.";
RL Physiol. Res. 60:15-25(2011).
RN [13]
RP VARIANT PHE-262.
RX PubMed=10391209; DOI=10.1038/10290;
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RT "Characterization of single-nucleotide polymorphisms in coding regions of
RT human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [14]
RP ERRATUM OF PUBMED:10391209.
RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA Lander E.S.;
RL Nat. Genet. 23:373-373(1999).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various alkaloids and
CC psychoactive substances. Ligand binding causes a conformation change
CC that triggers signaling via guanine nucleotide-binding proteins (G
CC proteins) and modulates the activity of down-stream effectors, such as
CC adenylate cyclase. Signaling inhibits adenylate cyclase activity.
CC {ECO:0000269|PubMed:14744596, ECO:0000269|PubMed:1513320,
CC ECO:0000269|PubMed:1608964, ECO:0000269|PubMed:1733778,
CC ECO:0000269|PubMed:21422162}.
CC -!- INTERACTION:
CC P28566; P50222: MEOX2; NbExp=3; IntAct=EBI-1043151, EBI-748397;
CC P28566; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1043151, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14744596,
CC ECO:0000269|PubMed:1513320, ECO:0000269|PubMed:1608964,
CC ECO:0000269|PubMed:1733778, ECO:0000269|PubMed:21422162}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14744596,
CC ECO:0000269|PubMed:1513320, ECO:0000269|PubMed:1608964,
CC ECO:0000269|PubMed:1733778, ECO:0000269|PubMed:21422162}.
CC -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:14744596}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M91467; AAA58353.1; -; mRNA.
DR EMBL; Z11166; CAA77558.1; -; Genomic_DNA.
DR EMBL; M92826; AAA58355.1; -; Genomic_DNA.
DR EMBL; AF498980; AAM21127.1; -; mRNA.
DR EMBL; AL157777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48616.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48617.1; -; Genomic_DNA.
DR EMBL; BC069751; AAH69751.1; -; mRNA.
DR EMBL; AB041373; BAA94458.1; -; Genomic_DNA.
DR CCDS; CCDS5006.1; -.
DR PIR; S20579; A45260.
DR RefSeq; NP_000856.1; NM_000865.2.
DR RefSeq; XP_011534091.1; XM_011535789.2.
DR PDB; 7E33; EM; 2.90 A; R=2-365.
DR PDBsum; 7E33; -.
DR AlphaFoldDB; P28566; -.
DR SMR; P28566; -.
DR BioGRID; 109586; 8.
DR IntAct; P28566; 7.
DR STRING; 9606.ENSP00000307766; -.
DR BindingDB; P28566; -.
DR ChEMBL; CHEMBL2182; -.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB14185; Aripiprazole lauroxil.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB11273; Dihydroergocornine.
DR DrugBank; DB13345; Dihydroergocristine.
DR DrugBank; DB00320; Dihydroergotamine.
DR DrugBank; DB01049; Ergoloid mesylate.
DR DrugBank; DB12141; Gilteritinib.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB00247; Methysergide.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB01224; Quetiapine.
DR DrugBank; DB09304; Setiptiline.
DR DrugBank; DB13025; Tiapride.
DR DrugBank; DB00246; Ziprasidone.
DR DrugBank; DB00315; Zolmitriptan.
DR DrugCentral; P28566; -.
DR GuidetoPHARMACOLOGY; 4; -.
DR GlyGen; P28566; 2 sites.
DR iPTMnet; P28566; -.
DR PhosphoSitePlus; P28566; -.
DR BioMuta; HTR1E; -.
DR DMDM; 112822; -.
DR MassIVE; P28566; -.
DR PaxDb; P28566; -.
DR PeptideAtlas; P28566; -.
DR PRIDE; P28566; -.
DR Antibodypedia; 1480; 192 antibodies from 31 providers.
DR DNASU; 3354; -.
DR Ensembl; ENST00000305344.7; ENSP00000307766.4; ENSG00000168830.8.
DR GeneID; 3354; -.
DR KEGG; hsa:3354; -.
DR MANE-Select; ENST00000305344.7; ENSP00000307766.4; NM_000865.3; NP_000856.1.
DR UCSC; uc003pli.4; human.
DR CTD; 3354; -.
DR DisGeNET; 3354; -.
DR GeneCards; HTR1E; -.
DR HGNC; HGNC:5291; HTR1E.
DR HPA; ENSG00000168830; Tissue enhanced (brain, ovary).
DR MIM; 182132; gene.
DR neXtProt; NX_P28566; -.
DR OpenTargets; ENSG00000168830; -.
DR PharmGKB; PA29552; -.
DR VEuPathDB; HostDB:ENSG00000168830; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P28566; -.
DR OMA; IHTSIRI; -.
DR OrthoDB; 703991at2759; -.
DR PhylomeDB; P28566; -.
DR TreeFam; TF316350; -.
DR PathwayCommons; P28566; -.
DR Reactome; R-HSA-390666; Serotonin receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P28566; -.
DR SIGNOR; P28566; -.
DR BioGRID-ORCS; 3354; 12 hits in 1067 CRISPR screens.
DR ChiTaRS; HTR1E; human.
DR GeneWiki; 5-HT1E_receptor; -.
DR GenomeRNAi; 3354; -.
DR Pharos; P28566; Tchem.
DR PRO; PR:P28566; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P28566; protein.
DR Bgee; ENSG00000168830; Expressed in prefrontal cortex and 52 other tissues.
DR Genevisible; P28566; HS.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IDA:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR InterPro; IPR027425; 5HT1E_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF33; PTHR24247:SF33; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01101; 5HTRECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..365
FT /note="5-hydroxytryptamine receptor 1E"
FT /id="PRO_0000068933"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 23..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 48..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 60..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 83..96
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 97..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 160..179
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 180..202
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 203..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 292..314
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 315..324
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 325..347
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 348..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 119..121
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 340..344
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 107
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 175
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 208
FT /note="A -> T (in dbSNP:rs3828741)"
FT /id="VAR_022061"
FT VARIANT 262
FT /note="S -> F (in dbSNP:rs6303)"
FT /evidence="ECO:0000269|PubMed:10391209"
FT /id="VAR_014165"
FT HELIX 21..49
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 56..74
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 94..125
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 136..154
FT /evidence="ECO:0007829|PDB:7E33"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 192..211
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 284..315
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 323..345
FT /evidence="ECO:0007829|PDB:7E33"
FT HELIX 349..357
FT /evidence="ECO:0007829|PDB:7E33"
SQ SEQUENCE 365 AA; 41682 MW; 4C31DD783A3F7483 CRC64;
MNITNCTTEA SMAIRPKTIT EKMLICMTLV VITTLTTLLN LAVIMAIGTT KKLHQPANYL
ICSLAVTDLL VAVLVMPLSI IYIVMDRWKL GYFLCEVWLS VDMTCCTCSI LHLCVIALDR
YWAITNAIEY ARKRTAKRAA LMILTVWTIS IFISMPPLFW RSHRRLSPPP SQCTIQHDHV
IYTIYSTLGA FYIPLTLILI LYYRIYHAAK SLYQKRGSSR HLSNRSTDSQ NSFASCKLTQ
TFCVSDFSTS DPTTEFEKFH ASIRIPPFDN DLDHPGERQQ ISSTRERKAA RILGLILGAF
ILSWLPFFIK ELIVGLSIYT VSSEVADFLT WLGYVNSLIN PLLYTSFNED FKLAFKKLIR
CREHT
