TOR1_SCHPO
ID TOR1_SCHPO Reviewed; 2335 AA.
AC O14356;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Serine/threonine-protein kinase tor1 {ECO:0000305|PubMed:11096119};
DE EC=2.7.11.1 {ECO:0000305|PubMed:12805221};
DE AltName: Full=Phosphatidylinositol kinase homolog tor1;
DE AltName: Full=Target of rapamycin kinase 1;
GN Name=tor1 {ECO:0000303|PubMed:11096119};
GN ORFNames=SPBC30D10.10c {ECO:0000312|PomBase:SPBC30D10.10c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=11409178; DOI=10.1007/s002940100198;
RA Kawai M., Nakashima A., Ueno M., Ushimaru T., Aiba K., Doi H., Uritani M.;
RT "Fission yeast tor1 functions in response to various stresses including
RT nitrogen starvation, high osmolarity, and high temperature.";
RL Curr. Genet. 39:166-174(2001).
RN [3]
RP IDENTIFICATION, FUNCTION, AND INDUCTION.
RX PubMed=11096119; DOI=10.1074/jbc.m010446200;
RA Weisman R., Choder M.;
RT "The fission yeast TOR homolog, tor1+, is required for the response to
RT starvation and other stresses via a conserved serine.";
RL J. Biol. Chem. 276:7027-7032(2001).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12805221; DOI=10.1093/emboj/cdg298;
RA Matsuo T., Kubo Y., Watanabe Y., Yamamoto M.;
RT "Schizosaccharomyces pombe AGC family kinase Gad8p forms a conserved
RT signaling module with TOR and PDK1-like kinases.";
RL EMBO J. 22:3073-3083(2003).
RN [5]
RP FUNCTION.
RX PubMed=15466417; DOI=10.1534/genetics.104.034983;
RA Weisman R., Roitburg I., Nahari T., Kupiec M.;
RT "Regulation of leucine uptake by tor1+ in Schizosaccharomyces pombe is
RT sensitive to rapamycin.";
RL Genetics 169:539-550(2005).
RN [6]
RP INTERACTION WITH POP3 AND STE20.
RX PubMed=17046992; DOI=10.1242/jcs.03241;
RA Alvarez B., Moreno S.;
RT "Fission yeast Tor2 promotes cell growth and represses cell
RT differentiation.";
RL J. Cell Sci. 119:4475-4485(2006).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [8]
RP IDENTIFICATION IN THE TORC2 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18076573; DOI=10.1111/j.1365-2443.2007.01141.x;
RA Hayashi T., Hatanaka M., Nagao K., Nakaseko Y., Kanoh J., Kokubu A.,
RA Ebe M., Yanagida M.;
RT "Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and
RT organization of two highly phosphorylated TOR complexes by specific and
RT common subunits.";
RL Genes Cells 12:1357-1370(2007).
RN [9]
RP FUNCTION.
RX PubMed=17179073; DOI=10.1534/genetics.106.064170;
RA Weisman R., Roitburg I., Schonbrun M., Harari R., Kupiec M.;
RT "Opposite effects of tor1 and tor2 on nitrogen starvation responses in
RT fission yeast.";
RL Genetics 175:1153-1162(2007).
RN [10]
RP INTERACTION WITH POP3; SIN1 AND STE20.
RX PubMed=17261596; DOI=10.1128/mcb.01039-06;
RA Matsuo T., Otsubo Y., Urano J., Tamanoi F., Yamamoto M.;
RT "Loss of the TOR kinase Tor2 mimics nitrogen starvation and activates the
RT sexual development pathway in fission yeast.";
RL Mol. Cell. Biol. 27:3154-3164(2007).
RN [11]
RP PHOSPHORYLATION AT THR-1972, AND MUTAGENESIS OF THR-1972.
RX PubMed=24247430; DOI=10.1083/jcb.201305103;
RA Halova L., Du W., Kirkham S., Smith D.L., Petersen J.;
RT "Phosphorylation of the TOR ATP binding domain by AGC kinase constitutes a
RT novel mode of TOR inhibition.";
RL J. Cell Biol. 203:595-604(2013).
CC -!- FUNCTION: Phosphatidylinositol 3-kinase homolog, component of TORC2,
CC which regulates multiple cellular processes to control cell growth in
CC response to environmental signals. TORC2 is required for cell survival
CC under various stress conditions. TORC2 positively controls G1 cell-
CC cycle arrest, sexual development and amino acid uptake. Positively
CC regulates amino acid uptake through the control of expression of amino
CC acid permeases (PubMed:11409178, PubMed:11096119, PubMed:15466417,
CC PubMed:17179073). Responsible for the phosphorylation of AGC kinase
CC gad8 at 'Ser-527' and 'Ser-546', activating gad8 kinase activity and
CC promoting sexual development (PubMed:12805221).
CC {ECO:0000269|PubMed:11096119, ECO:0000269|PubMed:11409178,
CC ECO:0000269|PubMed:12805221, ECO:0000269|PubMed:15466417,
CC ECO:0000269|PubMed:17179073}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305|PubMed:12805221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305|PubMed:12805221};
CC -!- SUBUNIT: The target of rapamycin complex 2 (TORC2) is composed of at
CC least bit61, pop3/wat1, sin1, ste20 and tor1.
CC {ECO:0000269|PubMed:17046992, ECO:0000269|PubMed:17261596,
CC ECO:0000269|PubMed:18076573}.
CC -!- INTERACTION:
CC O14356; Q9P3W5: tel2; NbExp=3; IntAct=EBI-2014420, EBI-2014377;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: By nitrogen and/or carbon starvation, cold, osmotic and
CC oxidative stress. {ECO:0000269|PubMed:11096119}.
CC -!- PTM: Phosphorylation at Thr-1972 in the ATP-binding region by AKT1
CC strongly reduces kinase activity. {ECO:0000269|PubMed:24247430}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase 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; CU329671; CAB10805.1; -; Genomic_DNA.
DR PIR; T40186; T40186.
DR RefSeq; NP_596275.1; NM_001022196.2.
DR AlphaFoldDB; O14356; -.
DR SMR; O14356; -.
DR BioGRID; 277001; 181.
DR IntAct; O14356; 7.
DR STRING; 4896.SPBC30D10.10c.1; -.
DR iPTMnet; O14356; -.
DR MaxQB; O14356; -.
DR PaxDb; O14356; -.
DR PRIDE; O14356; -.
DR EnsemblFungi; SPBC30D10.10c.1; SPBC30D10.10c.1:pep; SPBC30D10.10c.
DR GeneID; 2540473; -.
DR KEGG; spo:SPBC30D10.10c; -.
DR PomBase; SPBC30D10.10c; tor1.
DR VEuPathDB; FungiDB:SPBC30D10.10c; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; O14356; -.
DR OMA; FSGRVVH; -.
DR PhylomeDB; O14356; -.
DR BRENDA; 2.7.1.137; 5613.
DR PRO; PR:O14356; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IMP:PomBase.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0035562; P:negative regulation of chromatin binding; EXP:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:1900237; P:positive regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR GO; GO:0038203; P:TORC2 signaling; IMP:PomBase.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.20.120.150; -; 1.
DR Gene3D; 1.25.10.10; -; 3.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024585; DUF3385_TOR.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139:SF9; PTHR11139:SF9; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF47212; SSF47212; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cytoplasm; Kinase; Meiosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2335
FT /note="Serine/threonine-protein kinase tor1"
FT /id="PRO_0000088812"
FT REPEAT 1..31
FT /note="HEAT 1"
FT REPEAT 164..201
FT /note="HEAT 2"
FT REPEAT 331..371
FT /note="HEAT 3"
FT REPEAT 410..449
FT /note="HEAT 4"
FT REPEAT 474..512
FT /note="HEAT 5"
FT REPEAT 522..560
FT /note="HEAT 6"
FT REPEAT 562..596
FT /note="HEAT 7"
FT REPEAT 642..679
FT /note="HEAT 8"
FT REPEAT 684..722
FT /note="HEAT 9"
FT REPEAT 728..766
FT /note="HEAT 10"
FT REPEAT 843..880
FT /note="HEAT 11"
FT REPEAT 904..923
FT /note="HEAT 12"
FT REPEAT 924..961
FT /note="HEAT 13"
FT REPEAT 964..1003
FT /note="HEAT 14"
FT REPEAT 1005..1042
FT /note="HEAT 15"
FT DOMAIN 1226..1781
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 1955..2269
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2303..2335
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1961..1967
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2134..2142
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2154..2179
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOD_RES 1972
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:24247430"
FT MUTAGEN 1972
FT /note="T->A: Increased mTOR kinase activity and stress
FT resistance."
FT /evidence="ECO:0000269|PubMed:24247430"
SQ SEQUENCE 2335 AA; 266184 MW; 5DCF1CF4ABE8E9A4 CRC64;
MEYFSDLKNK NESIQLAAAD QLKEFVHSST KELSGESLAR FNNDINRRIF ELIHSHDSHE
RFGGILAIGK LIEFESEGDV TNLSRYANYL RMTLPSTDWH SMELSAKVLG HLAASGGTLA
AEFVEFEVQR AFEWLQGDRQ EQKRMAAILI IKALAQNSPT LVYLYISEIF QNLWTGLRDP
KPLIRETAAD ALGASLDVVC QREAKVQLQC FNEVLLQAEH GLRQSSVEYL HGSLLAYKEL
FEKSGSFIRE HYTEFCDLAL RLREHRDNSI RRCIVFLLPT LSEYNPKKFQ QRYLDSFMVY
LLSHIRKDKE KSLAFEAIGR IAMAVNEAMI PYLQNILKVI RDTLTAKVRE KTQYEKPVFE
CIGMLAAAVK LELLEDSRSL LGLIFSCELS VHLRQALVKM AENIPPLLAP IQERLLNMVS
QILTGKNFEI RTNDTYTPSF TNIYSAREPD QRSKSTESII LALETLGTFN FTGYSLISFI
QESVLSYLEN DNSEIRIAAA RTCCQVFARD PICRKTNPLA VESVAEVLEK LLTLGIADSD
PKIRETVLSL LDERFDRHLA HPDNIRCLFI ALNDEVFSIR EIAIIIIGRL ALYNPAHVMP
SLRKTIIQLL SDMEYSGNSR QKEESAQLLK LLVSKARTLI KPYIQSIIHV ILPKAADTSP
GVSSAIISAL GELASVEGED MPVDVRGSFM KLILVNLQDQ SSTLKRLASL KCLRKLCGRS
GYVIQPYLDY PPLLGALIGI LQSEQPTPIR REVLRTLGVL GALDPYTYLT TEEVSDDLQS
SHNNAHGVPQ ISAAQYPSLE NYAMVAVVTL IGILKDSSLS MHHSSVVQAV MHICSQMGSK
STVFLPQVVP TFLQVMQSLS ASSAEFYFQQ LTTLTSIIGP NIRDYVSDIF NLSKVFWEST
TSLLLVILEL IDAIAIALQD EFKFYLPQIL SCMLKAFSLD NTSSRSVSYK VLQSFVIFGS
NIEEYMHLVL PVIIRSFERD TIPLGFRKSA LKCIAQLFQS VNFSDHASRI IHPLVRMLGK
SNGDLRAVIM DTLCAIVSQL GYDYSIFIPM VNKVLVSHKI SHPAYELLVS RLLKGEPLPK
DVVVKEFKPR PSTKPFSTQD EVLTKLPVDQ ASLKAAWESS QKLTRDDWQD WIRRISIELL
KESPSSALRS CSTLAGIYHP LARDLFNVSF LSCWDELTES NKKNLVKSIE LAMNAPNISV
EILQTLLNLA EYMEREDHTL PIPIKVISAH ASKCNVYAKA LHYTELQFVQ ETKEEVSIST
IESLITINNH LQQSDAAVGM LQYTKEHKQF SLKETWYEKL HRWDDALAAY EHREREGDSS
FEINIGKLRC YYALGDWDHL SELAQKAWVT SEQEHREAIA PLAAAAAWGL GQWNLISEYV
SAMDRDPQDK EFFSAISAVH LGQYNKAYGH IERHRDILVN DLSSIIGESY NRAYGIMVKS
QMLSELEEII DYKKNMQYEN NLDSLKKTWR KRLEGCQKNV DVWHNTLRFR ALVLSPQDSP
EMWIKLADLC RRSDRLKLSN QCLTYLMGRD PSNAYPLDSL KLLNPHVVYT YLKYLWATDQ
KNIAVSELEE FTSYLSSKHG YKMGDSSKLV DILASSSVSS EERSFLARCF HKLGKWKKSL
QDSVNQESVR DILNCYFYAT LFDKSWYKAW HSWALANFEV VGYYEQTEHG VTQDMYEQYI
VPAIKGFFHS SVLNQKNSLQ DILRLLNLWF KFGEHSDVAA AIVEGFSNVP MDTWLEVIPQ
LIARIHTSSS SVRASVHQLL SDIGRVHPQA LVYSLTVSSK STNPQQKHSA KSIMDSMLSH
SDTLVRQALL VSQELIRVAI LWHELWYEGL EEASQAYFSD HDISLMIDIV KPLHETLEKG
PSTLSEISFA QTFGYDLRKA RSYWQKFLQD GDPTELNQSW DLYYQVFRRI QKQLPRIKHL
ELQYVSPKLL DACDLELAVP GTYGHNKPVI RISHFHHTFE VISSKQRPRR LTIHGSDGKD
YQYVLKGHED LRQDERVMQL FGLCNTLLTT DSETFKRRLN IERYTVIPLS PNSGLLGWVP
HSDTLHFLIK EFRSKRNILL NLEHRMMLQM APDCDSLTLL QKLEVFEYVM ANTDGYDLYH
VLWLKSRSSE AWLDRRTSYT QSLAVMSMVG YILGLGDRHP SNLMMDRYSG KIIHIDFGDC
FEVAMHREKF PEKIPFRLTR MLINAMEVSG IQGTYKITCE LVMRVLRSNT ESLMAVLEAF
VYDPLINWRL MTKSSFGAST TLRPTSSSVE EKGRSYTHRA RHADYAALSE TNGVNAEGLN
ERSIQVLKRV SNKLTGKDFD LKEQLPVKAQ VEKLIQQATA PENLCRCYVG WCSFW
