NKTR_MOUSE
ID NKTR_MOUSE Reviewed; 1453 AA.
AC P30415; F8VPR8; Q3UNH0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=NK-tumor recognition protein {ECO:0000305};
DE Short=NK-TR protein {ECO:0000305};
DE AltName: Full=Natural-killer cells cyclophilin-related protein;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase NKTR {ECO:0000250|UniProtKB:P30414};
DE Short=PPIase {ECO:0000250|UniProtKB:P30414};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:P30414};
GN Name=Nktr {ECO:0000312|MGI:MGI:97346};
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].
RX PubMed=8421688; DOI=10.1073/pnas.90.2.542;
RA Anderson S.K., Gallinger S., Roder J., Frey J., Young H.A., Ortaldo J.R.;
RT "A cyclophilin-related protein involved in the function of natural killer
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:542-546(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
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 [4]
RP SEQUENCE REVISION TO C-TERMINUS.
RC STRAIN=BALB/cJ; TISSUE=Blood;
RA Anderson S.K.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 470-476; 537-544; 709-716 AND 1445-1451, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611; SER-900 AND SER-1148,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding. Component of a putative tumor-recognition complex involved in
CC the function of NK cells. {ECO:0000250|UniProtKB:P30414}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000250|UniProtKB:P30414};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000250|UniProtKB:P30414}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30414}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37500.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L04289; AAA37500.2; ALT_INIT; mRNA.
DR EMBL; AK144214; BAE25777.1; -; mRNA.
DR EMBL; AC159810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23636.1; -.
DR RefSeq; NP_035048.3; NM_010918.2.
DR AlphaFoldDB; P30415; -.
DR SMR; P30415; -.
DR BioGRID; 201775; 3.
DR DIP; DIP-59972N; -.
DR IntAct; P30415; 2.
DR MINT; P30415; -.
DR STRING; 10090.ENSMUSP00000035112; -.
DR iPTMnet; P30415; -.
DR PhosphoSitePlus; P30415; -.
DR EPD; P30415; -.
DR jPOST; P30415; -.
DR MaxQB; P30415; -.
DR PaxDb; P30415; -.
DR PeptideAtlas; P30415; -.
DR PRIDE; P30415; -.
DR ProteomicsDB; 252900; -.
DR Antibodypedia; 12363; 105 antibodies from 22 providers.
DR DNASU; 18087; -.
DR Ensembl; ENSMUST00000035112; ENSMUSP00000035112; ENSMUSG00000032525.
DR GeneID; 18087; -.
DR KEGG; mmu:18087; -.
DR UCSC; uc009sdr.1; mouse.
DR CTD; 4820; -.
DR MGI; MGI:97346; Nktr.
DR VEuPathDB; HostDB:ENSMUSG00000032525; -.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000158548; -.
DR InParanoid; P30415; -.
DR OMA; THTDRYI; -.
DR OrthoDB; 1403619at2759; -.
DR TreeFam; TF318563; -.
DR BioGRID-ORCS; 18087; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Nktr; mouse.
DR PRO; PR:P30415; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P30415; protein.
DR Bgee; ENSMUSG00000032525; Expressed in ascending aorta and 251 other tissues.
DR ExpressionAtlas; P30415; baseline and differential.
DR Genevisible; P30415; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016018; F:cyclosporin A binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Isomerase; Isopeptide bond;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Rotamase;
KW Ubl conjugation.
FT CHAIN 1..1453
FT /note="NK-tumor recognition protein"
FT /id="PRO_0000064218"
FT DOMAIN 10..175
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 187..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1453
FT /note="Arg/Ser tandem repeat-rich"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..458
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..776
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1004
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1326
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT MOD_RES 880
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT CROSSLNK 576
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT CROSSLNK 637
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT CROSSLNK 664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT CROSSLNK 1208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT CROSSLNK 1249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P30414"
FT CONFLICT 112
FT /note="A -> V (in Ref. 2; BAE25777)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="K -> Q (in Ref. 2; BAE25777)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="E -> G (in Ref. 2; BAE25777)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="R -> K (in Ref. 2; BAE25777)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="S -> T (in Ref. 1; AAA37500)"
FT /evidence="ECO:0000305"
FT CONFLICT 856..859
FT /note="RTPK -> ENSE (in Ref. 1; AAA37500)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="K -> R (in Ref. 2; BAE25777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1453 AA; 163449 MW; AA536CDA355CF272 CRC64;
MGAQDRPQCH FDIEINREPV GRIMFQLFSD ICPKTCKNFL CLCSGEKGLG KTTGKKLCYK
GSTFHRVVKN FMIQGGDFSE GNGKGGESIY GGYFKDENFI LKHDRAFLLS MANRGKHTNG
SQFFITTKPA PHLDGVHVVF GLVISGFEVI EQIENLKTDA ASRPYADVRV IDCGVLATKL
TKDVFEKKRK KPTCSEGSDS SSRSSSSSES SSESEVERET IRRRRHKRRP KVRHAKKRRK
EMSSSEEPRR KRTVSPEGYS ERSDVNEKRS VDSNTKREKP VVRPEEIPPV PENRFLLRRD
MPAITVEPEQ NIPDVAPVVS DQKPSVSKSG RKIKGRGTIR YHTPPRSRSH SESKDDDSSE
TPPHWKEEMQ RLRAYRPPSG EKWSKGDKLS DPCSSRWDER SLSQRSRSWS YNGYYSDLST
ARHSDGHHKK HRKEKKFKHK KKAKKQKHCR RHRQTKKRRI VMPDLEPSRS PTHRMKSSCV
RERRSRASSS SSHHSSKRDW SKSDQDDGSA STHSSRDSYR SKSHSRSDSR GSSRSRAVSK
SSSRSLNRSK SRSSSRSGPR RTSISPKKPA QLSENKPVKT EPLRPSVPQN GNVLVQPVAA
ENIPVIPLSD SPPPSRWKPG QKPWKPSYER IQEMKAKTTH LLPVQSTYSL TNIKATVSSS
SYHKREKPSE SDGSAYSKYS DRSSGSSGRS GSKSSRSRSS SRSYTRSRSR SLPTSRSLSR
SPSSRSHSPN KYSDGSQHSR SSSYTSVSSD DGRRAMFRSN RKKSVTSHKR HRSNSEKTLH
SKYVRGREKS SRHRKYSESR SSLDYSSDSD QSHVQVYSAP EKEKQGKVEA LNDKQGKGRE
EGKPKPEWEC PRSKKRTPKD HSRDDSVSKG KNCAGSKWDS ESNSEQDVTK SRKSDPRRGS
EKEEGEASSD SESEVGQSHI KAKPPAKPPT STFLPGSDGA WKSRRPQSSA SESESSCSNL
GNIRGEPQKQ KHSKDDLKGD HTKRAREKSK AKKDKKHKAP KRKQAFHWQP PLEFGDDEEE
EMNGKQVTQD PKEKRHVSEK CEAVKDGIPN VEKTCDEGSS PSKPKKGTLE QDPLAEGGHD
PSSCPAPLKV EDNTASSPPS AQHLEEHGPG GGEDVLQTDD NMEICTPDRT SPAKGEVVSP
LANHRLDSPE VNIIPEQDEC MAHPRAGGEQ ESSMSESKTL GESGVKQDSS TSVTSPVETS
GKKEGAEKSQ MNLTDKWKPL QGVGNLSVST ATTSSALDVK ALSTVPEVKP QGLRIEIKSK
NKVRPGSLFD EVRKTARLNR RPRNQESSSD DQTPSRDGDS QSRSPHRSRS KSETKSRHRT
RSVSYSHSRS RSRSSTSSYR SRSYSRSRSR DWYSRGRTRS RSSSYGSFHS HRTSSRSRSR
SSSYDLHSRS RSYTYDSYYS RSRSRSRSQR SDSYHRGRSY NRRSRSGRSY GSDSESDRSY
SHHRSPSESS RYS
