ID   LAP2A_MOUSE             Reviewed;         693 AA.
AC   Q61033; B2RUB9; Q61028;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Lamina-associated polypeptide 2, isoforms alpha/zeta;
DE   AltName: Full=Thymopoietin isoforms alpha/zeta;
DE            Short=TP alpha/zeta;
GN   Name=Tmpo; Synonyms=Lap2;
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] (ISOFORMS ALPHA; BETA; GAMMA; DELTA; EPSILON AND
RP   ZETA).
RC   STRAIN=C57BL/6 X DBA/2; TISSUE=Thymus;
RX   PubMed=8743987; DOI=10.1101/gr.6.5.361;
RA   Berger R., Theodor L., Shoham J., Gokkel E., Brok-Simoni F., Avraham K.B.,
RA   Copeland N.G., Jenkins N.A., Rechavi G., Simon A.J.;
RT   "The characterization and localization of the mouse thymopoietin/lamina-
RT   associated polypeptide 2 gene and its alternatively spliced products.";
RL   Genome Res. 6:361-370(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; THR-159
RP   AND SER-422, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67 AND THR-74, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-67; THR-74; SER-82;
RP   THR-153; SER-155; SER-158; THR-159; SER-165; SER-167; SER-420 AND SER-422,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 (ISOFORM ZETA), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [10]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-85; ARG-87 AND ARG-329, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 459-693, IDENTIFICATION BY MASS
RP   SPECTROMETRY, DOMAIN, INTERACTION WITH LMNA, AND SUBUNIT.
RX   PubMed=17562312; DOI=10.1016/j.str.2007.04.007;
RA   Bradley C.M., Jones S., Huang Y., Suzuki Y., Kvaratskhelia M.,
RA   Hickman A.B., Craigie R., Dyda F.;
RT   "Structural basis for dimerization of LAP2alpha, a component of the nuclear
RT   lamina.";
RL   Structure 15:643-653(2007).
CC   -!- FUNCTION: May be involved in the structural organization of the nucleus
CC       and in the post-mitotic nuclear assembly. Plays an important role,
CC       together with LMNA, in the nuclear anchorage of RB1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. Interacts with LMNA, BANF1 and RB1 and with
CC       chromosomes. Associates directly or indirectly with lamins at specific
CC       cell-cycle stages (By similarity). Interacts with CMTM6 (By
CC       similarity). {ECO:0000250, ECO:0000250|UniProtKB:P42166}.
CC   -!- INTERACTION:
CC       Q61033-1; Q61033-1: Tmpo; NbExp=3; IntAct=EBI-15641551, EBI-15641551;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC       Note=Expressed diffusely throughout the nucleus. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=Alpha;
CC         IsoId=Q61033-1; Sequence=Displayed;
CC       Name=Zeta;
CC         IsoId=Q61033-2; Sequence=VSP_010128, VSP_010129;
CC       Name=Beta;
CC         IsoId=Q61029-1; Sequence=External;
CC       Name=Delta;
CC         IsoId=Q61029-2; Sequence=External;
CC       Name=Epsilon;
CC         IsoId=Q61029-3; Sequence=External;
CC       Name=Gamma;
CC         IsoId=Q61029-4; Sequence=External;
CC   -!- DOMAIN: The N-terminal part contains two structurally independent, non-
CC       interacting domains: LEM-like (also called LAP2-N or LEM-D) and LEM
CC       (also called LAP2-C or LEM-B). LEM-like binds DNA while LEM interacts
CC       with BANF1 (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal domain forms a four-stranded coiled coil.
CC       {ECO:0000269|PubMed:17562312}.
CC   -!- PTM: Phosphorylated in a mitose-specific manner. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LEM family. {ECO:0000305}.
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DR   EMBL; U39073; AAC52573.1; -; mRNA.
DR   EMBL; U39078; AAC52578.1; -; mRNA.
DR   EMBL; CH466539; EDL21530.1; -; Genomic_DNA.
DR   EMBL; BC141062; AAI41063.1; -; mRNA.
DR   CCDS; CCDS24122.1; -. [Q61033-1]
DR   RefSeq; NP_035735.2; NM_011605.3. [Q61033-1]
DR   PDB; 2V0X; X-ray; 2.20 A; A/B=459-693.
DR   PDBsum; 2V0X; -.
DR   AlphaFoldDB; Q61033; -.
DR   SMR; Q61033; -.
DR   BioGRID; 204234; 15.
DR   DIP; DIP-29323N; -.
DR   IntAct; Q61033; 4.
DR   MINT; Q61033; -.
DR   STRING; 10090.ENSMUSP00000020123; -.
DR   GlyGen; Q61033; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q61033; -.
DR   SwissPalm; Q61033; -.
DR   EPD; Q61033; -.
DR   jPOST; Q61033; -.
DR   MaxQB; Q61033; -.
DR   PaxDb; 10090-ENSMUSP00000020123; -.
DR   PeptideAtlas; Q61033; -.
DR   ProteomicsDB; 264965; -. [Q61033-1]
DR   ProteomicsDB; 264966; -. [Q61033-2]
DR   Pumba; Q61033; -.
DR   Antibodypedia; 2387; 456 antibodies from 37 providers.
DR   DNASU; 21917; -.
DR   Ensembl; ENSMUST00000020123.7; ENSMUSP00000020123.6; ENSMUSG00000019961.18. [Q61033-1]
DR   GeneID; 21917; -.
DR   UCSC; uc007gtu.2; mouse. [Q61033-2]
DR   UCSC; uc007gtv.2; mouse. [Q61033-1]
DR   AGR; MGI:106920; -.
DR   CTD; 7112; -.
DR   MGI; MGI:106920; Tmpo.
DR   VEuPathDB; HostDB:ENSMUSG00000019961; -.
DR   eggNOG; ENOG502QWCI; Eukaryota.
DR   GeneTree; ENSGT00940000154098; -.
DR   HOGENOM; CLU_397364_0_0_1; -.
DR   InParanoid; Q61033; -.
DR   OrthoDB; 5403043at2759; -.
DR   TreeFam; TF328426; -.
DR   BioGRID-ORCS; 21917; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Tmpo; mouse.
DR   EvolutionaryTrace; Q61033; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q61033; Protein.
DR   Bgee; ENSMUSG00000019961; Expressed in ectoderm and 279 other cell types or tissues.
DR   ExpressionAtlas; Q61033; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR   CDD; cd12940; LEM_LAP2_LEMD1; 1.
DR   CDD; cd12935; LEM_like; 1.
DR   Gene3D; 1.10.287.3160; -; 1.
DR   Gene3D; 1.10.720.40; -; 2.
DR   InterPro; IPR021623; LAP2alpha_C.
DR   InterPro; IPR013146; LEM-like_dom.
DR   InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR   InterPro; IPR003887; LEM_dom.
DR   PANTHER; PTHR12019:SF24; LAMINA-ASSOCIATED POLYPEPTIDE 2, ISOFORM ALPHA; 1.
DR   PANTHER; PTHR12019; LAMINA-ASSOCIATED POLYPEPTIDE THYMOPOIETIN; 1.
DR   Pfam; PF11560; LAP2alpha; 1.
DR   Pfam; PF03020; LEM; 1.
DR   Pfam; PF08198; Thymopoietin; 1.
DR   SMART; SM00540; LEM; 1.
DR   SMART; SM01261; Thymopoietin; 1.
DR   SUPFAM; SSF63451; LEM domain; 2.
DR   PROSITE; PS50954; LEM; 1.
DR   PROSITE; PS50955; LEM_LIKE; 1.
DR   Genevisible; Q61033; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Chromosome; Coiled coil;
KW   DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..693
FT                   /note="Lamina-associated polypeptide 2, isoforms
FT                   alpha/zeta"
FT                   /id="PRO_0000206145"
FT   DOMAIN          5..48
FT                   /note="LEM-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00313,
FT                   ECO:0000255|PROSITE-ProRule:PRU00314"
FT   DOMAIN          108..152
FT                   /note="LEM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT   REGION          48..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..107
FT                   /note="Linker"
FT   REGION          148..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          557..656
FT   MOTIF           190..196
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        92..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42166"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         74
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42166"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         85
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         87
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         153
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         155
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         159
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         163
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P42166"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42166"
FT   MOD_RES         329
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42166"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42166"
FT   MOD_RES         368
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42166"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         655
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42166"
FT   VAR_SEQ         188..225
FT                   /note="GKKKEHKKVKSARDCVPFSELASTPSGAFFQGISFPEI -> DSKIELKLEK
FT                   REPLKGRAKTPVTLKQRRTEHNQVFVVL (in isoform Zeta)"
FT                   /evidence="ECO:0000303|PubMed:8743987"
FT                   /id="VSP_010128"
FT   VAR_SEQ         226..693
FT                   /note="Missing (in isoform Zeta)"
FT                   /evidence="ECO:0000303|PubMed:8743987"
FT                   /id="VSP_010129"
FT   CONFLICT        72..73
FT                   /note="EP -> DA (in Ref. 1; AAC52573/AAC52578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262..265
FT                   /note="KGQT -> RGRP (in Ref. 1; AAC52578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280..281
FT                   /note="SS -> LC (in Ref. 1; AAC52578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322..324
FT                   /note="DIV -> EHS (in Ref. 1; AAC52578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393..394
FT                   /note="GT -> RS (in Ref. 1; AAC52578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        606
FT                   /note="D -> I (in Ref. 1; AAC52578)"
FT                   /evidence="ECO:0000305"
FT   HELIX           495..504
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   HELIX           505..507
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   STRAND          508..510
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   TURN            516..518
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   HELIX           524..530
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   HELIX           537..541
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   HELIX           558..604
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   HELIX           610..654
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   STRAND          655..657
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   HELIX           661..669
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   STRAND          674..678
FT                   /evidence="ECO:0007829|PDB:2V0X"
FT   MOD_RES         Q61033-2:206
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   693 AA;  75168 MW;  00604F3B66FF63F3 CRC64;
     MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLAAGANSK
     GPPDFSSDEE REPTPVLGSG ASVGRGRGAV GRKATKKTDK PRLEDKDDLD VTELSNEELL
     DQLVRYGVNP GPIVGTTRKL YEKKLLKLRE QGTESRSSTP LPTVSSSAEN TRQNGSNDSD
     RYSDNDEGKK KEHKKVKSAR DCVPFSELAS TPSGAFFQGI SFPEISTRPP LGRTELQAAK
     KVQTTKRDPP RETCTDTALP GKGQTHKLAP GRSLFIPSES SYDRCVEKSS SPSSQREFAA
     RLVSAAASPS LIRETTTTYS KDIVENICRG GKSRAQPLRA EEPGVSDQSV FSSEREVLQE
     SERSQVISPP LAQAIRDYVN SLLVQGGVGS LPGTSDSVPT LDVENICKRL SQSSYQDSES
     LSPPRKVPRL SEKPARGGDS GSCVAFQNTP GSEHRSSFAK SVVSHSLTTL GVEVSKPPPQ
     HDKIEASEPS FPLHESILKV VEEEWQQIDR QLPSVACRYP VSSIEAARIL SVPKVDDEIL
     GFISEATPRA ATQASSTESC DKHLDLALCR SYEAAASALQ IAAHTAFVAK SLQADISQAA
     QIINSDPSDA QQALRILNRT YDAASYLCDA AFDEVRMSAC AMGSSTMGRR YLWLKDCKIS
     PASKNKLTVA PFKGGTLFGG EVHKVIKKRG NKQ
//