ID FZD7_HUMAN Reviewed; 574 AA. AC O75084; O94816; Q53S59; Q96B74; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2004, sequence version 2. DT 13-FEB-2019, entry version 172. DE RecName: Full=Frizzled-7; DE Short=Fz-7; DE Short=hFz7; DE AltName: Full=FzE3; DE Flags: Precursor; GN Name=FZD7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND COUPLING TO BETA-CATENIN PATHWAY. RC TISSUE=Esophageal carcinoma; RX PubMed=9707618; DOI=10.1073/pnas.95.17.10164; RA Tanaka S., Akiyoshi T., Mori M., Wands J.R., Sugimachi K.; RT "A novel frizzled gene identified in human esophageal carcinoma RT mediates APC/beta-catenin signals."; RL Proc. Natl. Acad. Sci. U.S.A. 95:10164-10169(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetal lung; RX PubMed=9813155; DOI=10.1006/bbrc.1998.9607; RA Sagara N., Toda G., Hirai M., Terada M., Katoh M.; RT "Molecular cloning, differential expression, and chromosomal RT localization of human frizzled-1, frizzled-2, and frizzled-7."; RL Biochem. Biophys. Res. Commun. 252:117-122(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH MYOC. RX PubMed=19188438; DOI=10.1128/MCB.01274-08; RA Kwon H.S., Lee H.S., Ji Y., Rubin J.S., Tomarev S.I.; RT "Myocilin is a modulator of Wnt signaling."; RL Mol. Cell. Biol. 29:2139-2154(2009). RN [7] RP VARIANT SER-24. RX PubMed=17224074; DOI=10.1186/bcr1637; RA Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., RA Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., RA Kristensen V., Perou C.M., Boerresen-Dale A.-L.; RT "Somatic sequence alterations in twenty-one genes selected by RT expression profile analysis of breast carcinomas."; RL Breast Cancer Res. 9:R5-R5(2007). RN [8] RP INTERACTION WITH GPC3. RX PubMed=24496449; DOI=10.1242/jcs.140871; RA Capurro M., Martin T., Shi W., Filmus J.; RT "Glypican-3 binds to Frizzled and plays a direct role in the RT stimulation of canonical Wnt signaling."; RL J. Cell Sci. 127:1565-1575(2014). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 569-574, SITE, INTERACTION RP WITH SYNTENIN, MUTAGENESIS OF LYS-569, AND SUBCELLULAR LOCATION. RX PubMed=27386966; DOI=10.1038/ncomms12101; RA Egea-Jimenez A.L., Gallardo R., Garcia-Pino A., Ivarsson Y., RA Wawrzyniak A.M., Kashyap R., Loris R., Schymkowitz J., Rousseau F., RA Zimmermann P.; RT "Frizzled 7 and PIP2 binding by syntenin PDZ2 domain supports Frizzled RT 7 trafficking and signalling."; RL Nat. Commun. 7:12101-12101(2016). CC -!- FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors CC are coupled to the beta-catenin canonical signaling pathway, which CC leads to the activation of disheveled proteins, inhibition of GSK- CC 3 kinase, nuclear accumulation of beta-catenin and activation of CC Wnt target genes. A second signaling pathway involving PKC and CC calcium fluxes has been seen for some family members, but it is CC not yet clear if it represents a distinct pathway or if it can be CC integrated in the canonical pathway, as PKC seems to be required CC for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem CC to involve interactions with G-proteins. May be involved in CC transduction and intercellular transmission of polarity CC information during tissue morphogenesis and/or in differentiated CC tissues. CC -!- SUBUNIT: Interacts with MAGI3 and DVL1 (By similarity). Interacts CC with MYOC. Binds to SDCBP; this interaction is increased by CC inositol trisphosphate (IP3) (PubMed:27386966). Interacts with CC glypican GPC3 (PubMed:24496449). {ECO:0000250, CC ECO:0000269|PubMed:19188438, ECO:0000269|PubMed:24496449, CC ECO:0000269|PubMed:27386966}. CC -!- INTERACTION: CC P04156:PRNP; NbExp=3; IntAct=EBI-746917, EBI-977302; CC O00560:SDCBP; NbExp=4; IntAct=EBI-746917, EBI-727004; CC Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-746917, EBI-741480; CC P56703:WNT3; NbExp=3; IntAct=EBI-746917, EBI-3644922; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27386966}; CC Multi-pass membrane protein {ECO:0000269|PubMed:27386966}. CC Endosome membrane {ECO:0000269|PubMed:27386966}; Multi-pass CC membrane protein {ECO:0000269|PubMed:27386966}. Note=Associated to CC the plasma membrane in the presence of FZD7 and CC phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in CC recycling endosomes in other conditions. CC {ECO:0000269|PubMed:27386966}. CC -!- TISSUE SPECIFICITY: High expression in adult skeletal muscle and CC fetal kidney, followed by fetal lung, adult heart, brain, and CC placenta. Specifically expressed in squamous cell esophageal CC carcinomas. CC -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of CC Dvl (Disheveled) family members and is involved in the activation CC of the Wnt/beta-catenin signaling pathway. {ECO:0000250}. CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands. CC {ECO:0000250}. CC -!- PTM: Ubiquitinated by ZNRF3, leading to its degradation by the CC proteasome. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AB010881; BAA32424.1; -; mRNA. DR EMBL; AB017365; BAA34668.1; -; mRNA. DR EMBL; AC069148; AAX93250.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70298.1; -; Genomic_DNA. DR EMBL; BC015915; AAH15915.1; -; mRNA. DR CCDS; CCDS2351.1; -. DR PIR; JE0339; JE0339. DR RefSeq; NP_003498.1; NM_003507.1. DR UniGene; Hs.173859; -. DR PDB; 4Z33; X-ray; 2.45 A; C/D=569-574. DR PDB; 5T44; X-ray; 1.99 A; A/B=31-168. DR PDB; 5URV; X-ray; 2.20 A; A/B=30-168. DR PDB; 5WBS; X-ray; 2.88 A; A/B/C/D/E/F/G/H=30-174. DR PDBsum; 4Z33; -. DR PDBsum; 5T44; -. DR PDBsum; 5URV; -. DR PDBsum; 5WBS; -. DR ProteinModelPortal; O75084; -. DR SMR; O75084; -. DR BioGrid; 113920; 18. DR IntAct; O75084; 32. DR MINT; O75084; -. DR STRING; 9606.ENSP00000286201; -. DR ChEMBL; CHEMBL3559688; -. DR iPTMnet; O75084; -. DR PhosphoSitePlus; O75084; -. DR BioMuta; FZD7; -. DR EPD; O75084; -. DR jPOST; O75084; -. DR MaxQB; O75084; -. DR PaxDb; O75084; -. DR PeptideAtlas; O75084; -. DR PRIDE; O75084; -. DR ProteomicsDB; 49751; -. DR DNASU; 8324; -. DR Ensembl; ENST00000286201; ENSP00000286201; ENSG00000155760. DR GeneID; 8324; -. DR KEGG; hsa:8324; -. DR UCSC; uc002uyw.2; human. DR CTD; 8324; -. DR DisGeNET; 8324; -. DR EuPathDB; HostDB:ENSG00000155760.2; -. DR GeneCards; FZD7; -. DR HGNC; HGNC:4045; FZD7. DR HPA; HPA069165; -. DR MIM; 603410; gene. DR neXtProt; NX_O75084; -. DR OpenTargets; ENSG00000155760; -. DR PharmGKB; PA28462; -. DR eggNOG; KOG3577; Eukaryota. DR eggNOG; ENOG410XRC8; LUCA. DR GeneTree; ENSGT00940000158239; -. DR HOGENOM; HOG000233237; -. DR HOVERGEN; HBG006977; -. DR InParanoid; O75084; -. DR KO; K02432; -. DR OMA; SFPFSCP; -. DR OrthoDB; 330751at2759; -. DR PhylomeDB; O75084; -. DR TreeFam; TF317907; -. DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors). DR Reactome; R-HSA-4086400; PCP/CE pathway. DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins. DR SignaLink; O75084; -. DR SIGNOR; O75084; -. DR ChiTaRS; FZD7; human. DR GeneWiki; FZD7; -. DR GenomeRNAi; 8324; -. DR PRO; PR:O75084; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000155760; Expressed in 212 organ(s), highest expression level in thoracic mammary gland. DR Genevisible; O75084; HS. DR GO; GO:0016021; C:integral component of membrane; TAS:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB. DR GO; GO:0005109; F:frizzled binding; IPI:UniProtKB. DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW. DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB. DR GO; GO:0042813; F:Wnt-activated receptor activity; IDA:WormBase. DR GO; GO:0017147; F:Wnt-protein binding; IPI:BHF-UCL. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB. DR GO; GO:0060231; P:mesenchymal to epithelial transition; IMP:BHF-UCL. DR GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IGI:BHF-UCL. DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:BHF-UCL. DR GO; GO:0042666; P:negative regulation of ectodermal cell fate specification; IMP:BHF-UCL. DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB. DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IBA:GO_Central. DR GO; GO:0038031; P:non-canonical Wnt signaling pathway via JNK cascade; IMP:BHF-UCL. DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IMP:BHF-UCL. DR GO; GO:0046330; P:positive regulation of JNK cascade; IC:BHF-UCL. DR GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL. DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:BHF-UCL. DR GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IEA:Ensembl. DR GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl. DR GO; GO:0019827; P:stem cell population maintenance; IMP:BHF-UCL. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl. DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl. DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome. DR Gene3D; 1.10.2000.10; -; 1. DR InterPro; IPR015526; Frizzled/SFRP. DR InterPro; IPR000539; Frizzled/Smoothened_TM. DR InterPro; IPR020067; Frizzled_dom. DR InterPro; IPR036790; Frizzled_dom_sf. DR InterPro; IPR026552; FZD7. DR InterPro; IPR017981; GPCR_2-like. DR PANTHER; PTHR11309; PTHR11309; 1. DR PANTHER; PTHR11309:SF31; PTHR11309:SF31; 1. DR Pfam; PF01534; Frizzled; 1. DR Pfam; PF01392; Fz; 1. DR PRINTS; PR00489; FRIZZLED. DR SMART; SM00063; FRI; 1. DR SMART; SM01330; Frizzled; 1. DR SUPFAM; SSF63501; SSF63501; 1. DR PROSITE; PS50038; FZ; 1. DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Developmental protein; KW Disulfide bond; Endosome; G-protein coupled receptor; Glycoprotein; KW Membrane; Polymorphism; Receptor; Reference proteome; Signal; KW Transducer; Transmembrane; Transmembrane helix; Ubl conjugation; KW Wnt signaling pathway. FT SIGNAL 1 32 {ECO:0000255}. FT CHAIN 33 574 Frizzled-7. FT /FTId=PRO_0000012996. FT TOPO_DOM 33 256 Extracellular. {ECO:0000255}. FT TRANSMEM 257 277 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 278 288 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 289 309 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 310 336 Extracellular. {ECO:0000255}. FT TRANSMEM 337 357 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 358 379 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 380 400 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 401 423 Extracellular. {ECO:0000255}. FT TRANSMEM 424 444 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 445 470 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 471 491 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 492 528 Extracellular. {ECO:0000255}. FT TRANSMEM 529 549 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 550 574 Cytoplasmic. {ECO:0000255}. FT DOMAIN 44 163 FZ. {ECO:0000255|PROSITE- FT ProRule:PRU00090}. FT MOTIF 552 557 Lys-Thr-X-X-X-Trp motif, mediates FT interaction with the PDZ domain of Dvl FT family members. {ECO:0000250}. FT MOTIF 572 574 PDZ-binding. FT SITE 569 569 Essential for SDCBP-mediated plasma FT membrane phosphatidylinositol-4,5- FT bisphosphate recognition. FT {ECO:0000269|PubMed:27386966}. FT CARBOHYD 63 63 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 164 164 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 49 110 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT DISULFID 57 103 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT DISULFID 94 131 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT DISULFID 120 160 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT DISULFID 124 148 {ECO:0000255|PROSITE-ProRule:PRU00090}. FT VARIANT 24 24 G -> D (in dbSNP:rs35111363). FT /FTId=VAR_049292. FT VARIANT 24 24 G -> S (in dbSNP:rs755615030). FT {ECO:0000269|PubMed:17224074}. FT /FTId=VAR_033024. FT VARIANT 196 196 G -> E (in dbSNP:rs34908164). FT /FTId=VAR_033941. FT VARIANT 487 487 A -> V (in dbSNP:rs35600847). FT /FTId=VAR_033942. FT MUTAGEN 569 569 K->A: Impaired SDCBP-mediated interaction FT with phosphatidylinositol-4,5- FT bisphosphate. FT {ECO:0000269|PubMed:27386966}. FT CONFLICT 8 8 A -> V (in Ref. 1; BAA32424). FT {ECO:0000305}. FT CONFLICT 15 15 L -> F (in Ref. 1; BAA32424). FT {ECO:0000305}. FT CONFLICT 201 201 R -> K (in Ref. 1; BAA32424). FT {ECO:0000305}. FT CONFLICT 308 308 L -> F (in Ref. 1; BAA32424). FT {ECO:0000305}. FT CONFLICT 408 408 S -> N (in Ref. 1; BAA32424). FT {ECO:0000305}. FT CONFLICT 415 415 L -> F (in Ref. 1; BAA32424). FT {ECO:0000305}. FT CONFLICT 433 433 L -> F (in Ref. 1; BAA32424). FT {ECO:0000305}. FT CONFLICT 447 447 L -> F (in Ref. 1; BAA32424). FT {ECO:0000305}. FT CONFLICT 534 534 Y -> C (in Ref. 1; BAA32424). FT {ECO:0000305}. FT STRAND 49 51 {ECO:0000244|PDB:5T44}. FT HELIX 55 57 {ECO:0000244|PDB:5T44}. FT STRAND 58 61 {ECO:0000244|PDB:5T44}. FT STRAND 64 68 {ECO:0000244|PDB:5T44}. FT HELIX 76 83 {ECO:0000244|PDB:5T44}. FT HELIX 84 86 {ECO:0000244|PDB:5T44}. FT HELIX 87 91 {ECO:0000244|PDB:5T44}. FT HELIX 98 106 {ECO:0000244|PDB:5T44}. FT STRAND 112 115 {ECO:0000244|PDB:5T44}. FT HELIX 121 136 {ECO:0000244|PDB:5T44}. FT TURN 137 139 {ECO:0000244|PDB:5T44}. FT HELIX 144 146 {ECO:0000244|PDB:5T44}. FT HELIX 148 150 {ECO:0000244|PDB:5T44}. FT STRAND 156 158 {ECO:0000244|PDB:5T44}. FT STRAND 572 574 {ECO:0000244|PDB:4Z33}. SQ SEQUENCE 574 AA; 63620 MW; 801934246B426DF5 CRC64; MRDPGAAAPL SSLGLCALVL ALLGALSAGA GAQPYHGEKG ISVPDHGFCQ PISIPLCTDI AYNQTILPNL LGHTNQEDAG LEVHQFYPLV KVQCSPELRF FLCSMYAPVC TVLDQAIPPC RSLCERARQG CEALMNKFGF QWPERLRCEN FPVHGAGEIC VGQNTSDGSG GPGGGPTAYP TAPYLPDLPF TALPPGASDG RGRPAFPFSC PRQLKVPPYL GYRFLGERDC GAPCEPGRAN GLMYFKEEER RFARLWVGVW SVLCCASTLF TVLTYLVDMR RFSYPERPII FLSGCYFMVA VAHVAGFLLE DRAVCVERFS DDGYRTVAQG TKKEGCTILF MVLYFFGMAS SIWWVILSLT WFLAAGMKWG HEAIEANSQY FHLAAWAVPA VKTITILAMG QVDGDLLSGV CYVGLSSVDA LRGFVLAPLF VYLFIGTSFL LAGFVSLFRI RTIMKHDGTK TEKLEKLMVR IGVFSVLYTV PATIVLACYF YEQAFREHWE RTWLLQTCKS YAVPCPPGHF PPMSPDFTVF MIKYLMTMIV GITTGFWIWS GKTLQSWRRF YHRLSHSSKG ETAV //