RHG31_MOUSE
ID RHG31_MOUSE Reviewed; 1425 AA.
AC A6X8Z5; Q3TL91; Q3U1T7; Q3UDE7; Q3UUH4; Q6ZPW0; Q9WV94;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Rho GTPase-activating protein 31;
DE AltName: Full=Cdc42 GTPase-activating protein;
GN Name=Arhgap31; Synonyms=Cdgap, Kiaa1204;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Hypothalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-820, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9786927; DOI=10.1074/jbc.273.44.29172;
RA Lamarche-Vane N., Hall A.;
RT "CdGAP, a novel proline-rich GTPase-activating protein for Cdc42 and Rac.";
RL J. Biol. Chem. 273:29172-29177(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1425.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP INTERACTION WITH ITSN1, AND SUBCELLULAR LOCATION.
RX PubMed=11744688; DOI=10.1074/jbc.m105516200;
RA Jenna S., Hussain N.K., Danek E.I., Triki I., Wasiak S., McPherson P.S.,
RA Lamarche-Vane N.;
RT "The activity of the GTPase-activating protein CdGAP is regulated by the
RT endocytic protein intersectin.";
RL J. Biol. Chem. 277:6366-6373(2002).
RN [6]
RP IDENTIFICATION, AND PHOSPHORYLATION AT THR-776.
RX PubMed=16024771; DOI=10.1128/mcb.25.15.6314-6329.2005;
RA Tcherkezian J., Danek E.I., Jenna S., Triki I., Lamarche-Vane N.;
RT "Extracellular signal-regulated kinase 1 interacts with and phosphorylates
RT CdGAP at an important regulatory site.";
RL Mol. Cell. Biol. 25:6314-6329(2005).
RN [7]
RP FUNCTION, INTERACTION WITH PARVA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-56 AND ASN-169.
RX PubMed=16860736; DOI=10.1016/j.cub.2006.05.057;
RA LaLonde D.P., Grubinger M., Lamarche-Vane N., Turner C.E.;
RT "CdGAP associates with actopaxin to regulate integrin-dependent changes in
RT cell morphology and motility.";
RL Curr. Biol. 16:1375-1385(2006).
RN [8]
RP PHOSPHORYLATION AT THR-776, AND INDUCTION BY SERUM.
RX PubMed=17158447; DOI=10.1074/jbc.m610073200;
RA Danek E.I., Tcherkezian J., Triki I., Meriane M., Lamarche-Vane N.;
RT "Glycogen synthase kinase-3 phosphorylates CdGAP at a consensus ERK 1
RT regulatory site.";
RL J. Biol. Chem. 282:3624-3631(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; THR-283; SER-343;
RP SER-346; SER-384; SER-464; THR-666; SER-685; SER-690; SER-765; THR-769;
RP SER-961; SER-1092; SER-1093 AND SER-1163, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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: Functions as a GTPase-activating protein (GAP) for RAC1 and
CC CDC42. Required for cell spreading, polarized lamellipodia formation
CC and cell migration. {ECO:0000269|PubMed:16860736,
CC ECO:0000269|PubMed:9786927}.
CC -!- SUBUNIT: Interacts with ITSN1, which inhibits GAP activity. Interacts
CC with PARVA. Interacts with GTP-loaded RHOU (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC A6X8Z5; Q9Z0R4: Itsn1; NbExp=3; IntAct=EBI-4325995, EBI-645386;
CC A6X8Z5; Q7L0Q8: RHOU; Xeno; NbExp=2; IntAct=EBI-4325995, EBI-1638043;
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell junction,
CC focal adhesion.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in heart and lung.
CC {ECO:0000269|PubMed:9786927}.
CC -!- INDUCTION: By serum (at protein level). {ECO:0000269|PubMed:17158447}.
CC -!- PTM: Phosphorylated on Thr-776 by GSK3; which reduces GAP activity.
CC {ECO:0000269|PubMed:16024771, ECO:0000269|PubMed:17158447}.
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DR EMBL; AK138417; BAE23651.1; -; mRNA.
DR EMBL; AK149975; BAE29205.1; -; mRNA.
DR EMBL; AK150109; BAE29314.1; -; mRNA.
DR EMBL; AK155729; BAE33406.1; -; mRNA.
DR EMBL; AK166583; BAE38872.1; -; mRNA.
DR EMBL; AK166622; BAE38901.1; -; mRNA.
DR EMBL; AC154425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF151363; AAD38043.1; -; mRNA.
DR EMBL; AK129309; BAC98119.1; -; mRNA.
DR CCDS; CCDS28172.1; -.
DR RefSeq; NP_064656.2; NM_020260.2.
DR AlphaFoldDB; A6X8Z5; -.
DR SMR; A6X8Z5; -.
DR BioGRID; 198630; 2.
DR ELM; A6X8Z5; -.
DR IntAct; A6X8Z5; 2.
DR STRING; 10090.ENSMUSP00000023487; -.
DR iPTMnet; A6X8Z5; -.
DR PhosphoSitePlus; A6X8Z5; -.
DR EPD; A6X8Z5; -.
DR jPOST; A6X8Z5; -.
DR PaxDb; A6X8Z5; -.
DR PeptideAtlas; A6X8Z5; -.
DR PRIDE; A6X8Z5; -.
DR ProteomicsDB; 253281; -.
DR Antibodypedia; 49897; 37 antibodies from 15 providers.
DR DNASU; 12549; -.
DR Ensembl; ENSMUST00000023487; ENSMUSP00000023487; ENSMUSG00000022799.
DR GeneID; 12549; -.
DR KEGG; mmu:12549; -.
DR UCSC; uc007zfg.1; mouse.
DR CTD; 57514; -.
DR MGI; MGI:1333857; Arhgap31.
DR VEuPathDB; HostDB:ENSMUSG00000022799; -.
DR eggNOG; KOG1449; Eukaryota.
DR GeneTree; ENSGT00940000159458; -.
DR HOGENOM; CLU_006917_0_0_1; -.
DR InParanoid; A6X8Z5; -.
DR OMA; RTNPYID; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; A6X8Z5; -.
DR TreeFam; TF351451; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR BioGRID-ORCS; 12549; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Arhgap31; mouse.
DR PRO; PR:A6X8Z5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; A6X8Z5; protein.
DR Bgee; ENSMUSG00000022799; Expressed in right lung lobe and 217 other tissues.
DR ExpressionAtlas; A6X8Z5; baseline and differential.
DR Genevisible; A6X8Z5; MM.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell projection; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1425
FT /note="Rho GTPase-activating protein 31"
FT /id="PRO_0000320115"
FT DOMAIN 21..216
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 258..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 769
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 776
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000269|PubMed:16024771,
FT ECO:0000269|PubMed:17158447"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 56
FT /note="R->A: 70% reduction of GAP activity; when associated
FT with V-169."
FT /evidence="ECO:0000269|PubMed:16860736"
FT MUTAGEN 169
FT /note="N->V: 70% reduction of GAP activity; when associated
FT with A-56."
FT /evidence="ECO:0000269|PubMed:16860736"
FT CONFLICT 292
FT /note="R -> K (in Ref. 2; BAE33406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1153
FT /note="V -> F (in Ref. 2; BAE38872/BAE38901)"
FT /evidence="ECO:0000305"
FT CONFLICT 1365
FT /note="S -> C (in Ref. 2; BAE38872/BAE38901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1425 AA; 155276 MW; 00A39A0664D1A558 CRC64;
MKNKGAKQKL KRKGAASAFG CDLTEYLESS GQDVPYVLKS CAEFIETHGI VDGIYRLSGI
TSNIQRLRQE FGSDQCPDLT REVYLQDIHC VGSLCKLYFR ELPNPLLTYE LYEKFTEAVS
HRPEEGQLAR IQNVILELPP PHYRTLEYLI RHLAHIASFS SKTNMHARNL ALVWAPNLLR
SKKIEATICN GDAAFLAVRV QQVVIEFILN HADQIFNGGA PGALQQDESR TITKSLTLPA
LSLPMKLVSL EEAQARSLAT NHPARKERRE NSLPEIVPPP FHTVLELPDN KRKLSSKSKK
WKSIFNLGRS GSDSKSKLSR NGSVFVRGQR LSVEKATIRP AKSMDSLCSV PVEGKENKGN
FSRTVTTGGF FIPATKMHAS STGSSCDLSK EGEWGQEGMP AGAEGGCEVG GQIRPLPEQL
KVFRPIGDPE SEQSAPKLLG MFYTSSDSPG KSVFTSSLFQ MEPSPRHQRK ALNISEPFAV
SVPLRVSAVI STNSTPCRTP PKELQSLSSL EEFSFQGSES GGWPEEEKPL GAESFPGSVT
KKAATEDTKP EPEVPGRAEC SQSPPLDPGT QVEKKTLHVS LGSQVSKEAE KRPKAEKVME
ESQGASQPKP STPQESLGAG TEPLILHEMD EEDLAQALIW PEIQQELKII ESEEEFSSLP
PAAQKTSPIP ESSPAPFPFP EAPGSLPSSS APREVWTRDA ANQSIQEAAI LTDREKLEPV
CSLLESESQQ ELSPDPASLA PLEMLLFEKV SSPARIEIGG PRNLSPPLTP APPPPTPLEE
EPEVLLSKEG PDREDAARDS RTDVYTEQPT PKESPGIPTP CQREEAIASP NEKQNARHAV
PENKGPGLPS PTKEVDIIPQ EEGGAPHSAQ EPSDCDEDDT VTDPAQHGLE MVEPWEEPQW
VTSPLHSPTL KEVQESQTQG SQGHRLERRL CHRPSLRQSH SLDSKTTGNS HWTLEAPFSS
SCANLETERN YEPLQPPAAR TKIAGLEEKA LKAFREFSGL KGLEVLPSQK GPSGIQPKPV
ETNFMGLAEG KEQEPQLELS NRQMKHSDVP GPDSSKESSP RAQDSTLPGE HPLQLQLKNT
ECGPSKGKHR PSSLNLDSAT PIADLFRLEN GAPFSSPGIE LSELGDTKVT WMSSSHCKAA
PWNSQDTQDL DIVAHTLTGR RNSAPVSVSA VRTSFMVKMC QAKAVPVIPP KIQYTQIPQP
LPSQSTGEGG AQPLERSQEE PGSTPEIPQK STKDDSPSSL GSPEEEQPKQ ETGASASRRQ
ASITSCMYEG SSCSPEPSAS TLASTQDAVV QCRKRTSETE PSGDNLLSSK LERASGGPKA
FHRSRPGRPQ SLILFPIMDH LPSSPTVIDS KVLLSPIRSP TQTVSPGLLC GELAENTWIT
PEGVTLRNKM TIPKNGQRLE TSTSCFYQPQ RRSVILDGRS GRQIE
