GOPC_MOUSE
ID GOPC_MOUSE Reviewed; 463 AA.
AC Q8BH60; Q8BSV4; Q920R1; Q9ET11;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Golgi-associated PDZ and coiled-coil motif-containing protein {ECO:0000312|MGI:MGI:2149946};
DE AltName: Full=CFTR-associated ligand {ECO:0000250|UniProtKB:Q9HD26};
DE AltName: Full=PDZ protein interacting specifically with TC10 {ECO:0000250|UniProtKB:Q9HD26};
DE Short=PIST {ECO:0000250|UniProtKB:Q9HD26};
GN Name=Gopc {ECO:0000312|MGI:MGI:2149946};
GN Synonyms=Cal {ECO:0000250|UniProtKB:Q9HD26};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), OLIGOMERIZATION, AND INTERACTION
RP WITH RHOQ.
RC TISSUE=Embryo;
RX PubMed=11162552; DOI=10.1006/bbrc.2000.4160;
RA Neudauer C.L., Joberty G., Macara I.G.;
RT "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family
RT GTPase TC10.";
RL Biochem. Biophys. Res. Commun. 280:541-547(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DOMAIN, OLIGOMERIZATION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FZD5 AND FZD8.
RC TISSUE=Kidney;
RX PubMed=11520064; DOI=10.1006/bbrc.2001.5430;
RA Yao R., Maeda T., Takada S., Noda T.;
RT "Identification of a PDZ domain containing Golgi protein, GOPC, as an
RT interaction partner of frizzled.";
RL Biochem. Biophys. Res. Commun. 286:771-778(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=11384996; DOI=10.1074/jbc.m104137200;
RA Charest A., Lane K., McMahon K., Housman D.E.;
RT "Association of a novel PDZ domain-containing peripheral Golgi protein with
RT the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF)
RT attachment protein receptor) protein syntaxin 6.";
RL J. Biol. Chem. 276:29456-29465(2001).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP DOMAIN, AND INTERACTION WITH GRID2 AND BECN1.
RX PubMed=12372286; DOI=10.1016/s0896-6273(02)00861-9;
RA Yue Z., Horton A., Bravin M., DeJager P.L., Selimi F., Heintz N.;
RT "A novel protein complex linking the delta 2 glutamate receptor and
RT autophagy: implications for neurodegeneration in lurcher mice.";
RL Neuron 35:921-933(2002).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12149515; DOI=10.1073/pnas.162027899;
RA Yao R., Ito C., Natsume Y., Sugitani Y., Yamanaka H., Kuretake S.,
RA Yanagida K., Sato A., Toshimori K., Noda T.;
RT "Lack of acrosome formation in mice lacking a Golgi protein, GOPC.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11211-11216(2002).
RN [8]
RP INTERACTION WITH CLCN3 AND CFTR, AND DOMAIN.
RX PubMed=12471024; DOI=10.1074/jbc.m211050200;
RA Gentzsch M., Cui L., Mengos A., Chang X.-B., Chen J.-H., Riordan J.R.;
RT "The PDZ-binding chloride channel ClC-3B localizes to the Golgi and
RT associates with cystic fibrosis transmembrane conductance regulator-
RT interacting PDZ proteins.";
RL J. Biol. Chem. 278:6440-6449(2003).
RN [9]
RP INTERACTION WITH CSPG5, AND SUBCELLULAR LOCATION.
RX PubMed=12885772; DOI=10.1074/jbc.m305577200;
RA Hassel B., Schreff M., Stuebe E.-M., Blaich U., Schumacher S.;
RT "CALEB/NGC interacts with the Golgi-associated protein PIST.";
RL J. Biol. Chem. 278:40136-40143(2003).
RN [10]
RP INTERACTION WITH CACNG2.
RX PubMed=15136571; DOI=10.1074/jbc.m402214200;
RA Ives J.H., Fung S., Tiwari P., Payne H.L., Thompson C.L.;
RT "Microtubule-associated protein light chain 2 is a stargazin-AMPA receptor
RT complex-interacting protein in vivo.";
RL J. Biol. Chem. 279:31002-31009(2004).
RN [11]
RP INTERACTION WITH ASIC3, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=15317815; DOI=10.1074/jbc.m405874200;
RA Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.;
RT "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have
RT opposite effects on H+- gated current.";
RL J. Biol. Chem. 279:46962-46968(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402 AND SER-405, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role in intracellular protein trafficking and
CC degradation (PubMed:12149515). May regulate CFTR chloride currents and
CC acid-induced ASIC3 currents by modulating cell surface expression of
CC both channels (PubMed:15317815). May also regulate the intracellular
CC trafficking of the ADR1B receptor (By similarity). May play a role in
CC autophagy (PubMed:12372286). Together with MARCHF2 mediates the
CC ubiquitination and lysosomal degradation of CFTR (By similarity).
CC Overexpression results in CFTR intracellular retention and degradation
CC in the lysosomes (By similarity). {ECO:0000250|UniProtKB:Q9HD26,
CC ECO:0000269|PubMed:12149515, ECO:0000269|PubMed:12372286,
CC ECO:0000269|PubMed:15317815}.
CC -!- SUBUNIT: Homooligomer (PubMed:11162552). Interacts with FZD5
CC (PubMed:11520064). Interacts with FZD8 (PubMed:11520064). Interacts
CC with GRID2 and BECN1 (PubMed:12372286). Interacts with CSPG5
CC (PubMed:12885772). Interacts with CLCN3 (PubMed:12471024). Interacts
CC with STX6 (By similarity). Interacts with CFTR (PubMed:12471024).
CC Interacts with ASIC3 (PubMed:15317815). Interacts with GOLGA3 (By
CC similarity). Interacts with NLGN1 (By similarity). Interacts with RHOQ
CC (PubMed:11162552). Interacts with MARCHF2; the interaction leads to
CC CFTR ubiquitination and degradation (By similarity). May interact with
CC CACNG2 (PubMed:15136571). {ECO:0000250|UniProtKB:Q9HD26,
CC ECO:0000269|PubMed:11162552, ECO:0000269|PubMed:11520064,
CC ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:12471024,
CC ECO:0000269|PubMed:12885772, ECO:0000269|PubMed:15136571,
CC ECO:0000269|PubMed:15317815}.
CC -!- INTERACTION:
CC Q8BH60; O88597: Becn1; NbExp=5; IntAct=EBI-296357, EBI-643716;
CC Q8BH60; Q9EQD0: Fzd5; NbExp=3; IntAct=EBI-296357, EBI-7938232;
CC Q8BH60; Q61091: Fzd8; NbExp=3; IntAct=EBI-296357, EBI-6171689;
CC Q8BH60; Q61625: Grid2; NbExp=5; IntAct=EBI-296357, EBI-2794106;
CC Q8BH60; O95196: CSPG5; Xeno; NbExp=3; IntAct=EBI-296357, EBI-296349;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral
CC membrane protein. Golgi apparatus, trans-Golgi network membrane;
CC Peripheral membrane protein. Synapse. Postsynaptic density. Cell
CC projection, dendrite. Note=Enriched in synaptosomal and postsynaptic
CC densities (PSD) fractions. Expressed in cell bodies and dendrites of
CC Purkinje cells. Localized at the trans-Golgi network (TGN) of
CC spermatids and the medulla of round spermatides.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=NPIST, Beta;
CC IsoId=Q8BH60-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q8BH60-2; Sequence=VSP_016065;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC Expressed in dorsal root glanglion (DRG), spinal cord and brain.
CC Isoform 1 is preferentially expressed in whole brain (at protein level)
CC and cerebellum. Expressed in spermatocytes and spermatides but not in
CC Sertoli cells and spermatogonia. {ECO:0000269|PubMed:11384996,
CC ECO:0000269|PubMed:12149515, ECO:0000269|PubMed:12372286,
CC ECO:0000269|PubMed:15317815}.
CC -!- DEVELOPMENTAL STAGE: In the cerebellum, expression increases post-
CC natally, following maturation of this tissue (at protein level).
CC {ECO:0000269|PubMed:12372286}.
CC -!- DOMAIN: The coiled-coil region probably mediates targeting to the
CC Golgi, oligomerization and interaction with RHOQ. May also mediates
CC association to membranes and interactions with GOLGA3 and STX6 (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The PDZ domain mediates interaction with ADRB1 (By similarity).
CC Mediates also interactions with FZD5, FZD8, ASIC3, GRID2, CFTR, CLCN3.
CC {ECO:0000250, ECO:0000269|PubMed:11520064, ECO:0000269|PubMed:12372286,
CC ECO:0000269|PubMed:12471024}.
CC -!- DISRUPTION PHENOTYPE: Male mice are infertile with globozoospermia.
CC Spermatozoa display a default in acrosome formation and are unable to
CC activate oocytes. {ECO:0000269|PubMed:12149515}.
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DR EMBL; AF287893; AAG00571.1; -; mRNA.
DR EMBL; AB052838; BAB69946.1; -; mRNA.
DR EMBL; AK030427; BAC26958.1; -; mRNA.
DR EMBL; AK030637; BAC27058.1; -; mRNA.
DR EMBL; AK032613; BAC27951.1; -; mRNA.
DR EMBL; BC051171; AAH51171.1; -; mRNA.
DR CCDS; CCDS35898.1; -. [Q8BH60-2]
DR RefSeq; NP_001186201.1; NM_001199272.1. [Q8BH60-1]
DR RefSeq; NP_444417.2; NM_053187.3. [Q8BH60-2]
DR AlphaFoldDB; Q8BH60; -.
DR BMRB; Q8BH60; -.
DR SMR; Q8BH60; -.
DR BioGRID; 220478; 13.
DR IntAct; Q8BH60; 11.
DR MINT; Q8BH60; -.
DR STRING; 10090.ENSMUSP00000101115; -.
DR iPTMnet; Q8BH60; -.
DR PhosphoSitePlus; Q8BH60; -.
DR CPTAC; non-CPTAC-3814; -.
DR EPD; Q8BH60; -.
DR MaxQB; Q8BH60; -.
DR PaxDb; Q8BH60; -.
DR PRIDE; Q8BH60; -.
DR ProteomicsDB; 271130; -. [Q8BH60-1]
DR ProteomicsDB; 271131; -. [Q8BH60-2]
DR Ensembl; ENSMUST00000020008; ENSMUSP00000020008; ENSMUSG00000019861. [Q8BH60-2]
DR GeneID; 94221; -.
DR KEGG; mmu:94221; -.
DR UCSC; uc007fbf.2; mouse. [Q8BH60-2]
DR UCSC; uc007fbg.2; mouse. [Q8BH60-1]
DR CTD; 57120; -.
DR MGI; MGI:2149946; Gopc.
DR VEuPathDB; HostDB:ENSMUSG00000019861; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000156535; -.
DR HOGENOM; CLU_045744_0_0_1; -.
DR InParanoid; Q8BH60; -.
DR OMA; QCNLRQE; -.
DR OrthoDB; 1038418at2759; -.
DR PhylomeDB; Q8BH60; -.
DR Reactome; R-MMU-5627083; RHO GTPases regulate CFTR trafficking.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR BioGRID-ORCS; 94221; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Gopc; mouse.
DR PRO; PR:Q8BH60; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BH60; protein.
DR Bgee; ENSMUSG00000019861; Expressed in trigeminal ganglion and 239 other tissues.
DR ExpressionAtlas; Q8BH60; baseline and differential.
DR Genevisible; Q8BH60; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
DR GO; GO:0005109; F:frizzled binding; IPI:BHF-UCL.
DR GO; GO:0030695; F:GTPase regulator activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0019905; F:syntaxin binding; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; TAS:UniProtKB.
DR GO; GO:0043004; P:cytoplasmic sequestering of CFTR protein; ISO:MGI.
DR GO; GO:0010360; P:negative regulation of anion channel activity; ISO:MGI.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IMP:MGI.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR038879; GOPC.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR16528; PTHR16528; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HD26"
FT CHAIN 2..463
FT /note="Golgi-associated PDZ and coiled-coil motif-
FT containing protein"
FT /id="PRO_0000087543"
FT DOMAIN 289..372
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT COILED 85..201
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD26"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 151..158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11162552,
FT ECO:0000303|PubMed:11520064, ECO:0000303|PubMed:15489334"
FT /id="VSP_016065"
SQ SEQUENCE 463 AA; 50662 MW; 47BB5760BFFB6303 CRC64;
MSAGGPCPAG AGGGPGGSSC PVGVSPGGVS MFRWLEVLEK EFDKAFVDVD LLLGEIDPDQ
ADITYEGRQK MTSLSSCFAQ LCHKAQTVSQ INHKLEAQLV DLRSELTETQ AEKVVLEKEV
HEQLLQLHST QLQLHAKTGQ SVDSGAIKAK LSVHSVEDLE RELEANKTEK VKEARLEAEV
KLLRKENEAL RRHIAVLQAE VYGARLAAKY LDKELAGRVQ QIQLLGRDMK GPAHDKLWNQ
LEAEIHLHRH KTVIRACRGR NDLKRPMQAP PGHDQDSLKK SQGVGPIRKV LLLKEDHEGL
GISITGGKEH GVPILISEIH PGQPADRCGG LHVGDAILAV NGVNLRDTKH KEAVTILSQQ
RGEIEFEVVY VAPEVDSDDE NVEYEDESGH RYRLYLDELE GSGNSGASCK DSSGEMKMLQ
GYNKKAVRDA HENGDVGAAG ESPLDDTAAR AAHLHSLHQK KAY
