NUA_ARATH
ID NUA_ARATH Reviewed; 2093 AA.
AC A4GSN8; F4IDK8; F4IDK9; O64521; O64522; O64524; O64525; Q8H7F1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Nuclear-pore anchor {ECO:0000303|PubMed:17513499, ECO:0000303|PubMed:21189294};
DE AltName: Full=Protein TRANSLOCATED PROMOTER REGION {ECO:0000303|PubMed:17535820};
DE Short=AtTPR;
GN Name=NUA {ECO:0000303|PubMed:17513499, ECO:0000303|PubMed:21189294};
GN Synonyms=TPR {ECO:0000303|PubMed:17535820};
GN OrderedLocusNames=At1g79280 {ECO:0000312|Araport:AT1G79280};
GN ORFNames=YUP8H12R.11, YUP8H12R.12, YUP8H12R.8,
GN YUP8H12R.9 {ECO:0000312|EMBL:AAC17058.1, ECO:0000312|EMBL:AAC17060.1,
GN ECO:0000312|EMBL:AAC17073.1, ECO:0000312|EMBL:AAC17074.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ESD4,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17513499; DOI=10.1105/tpc.106.049239;
RA Xu X.M., Rose A., Muthuswamy S., Jeong S.Y., Venkatakrishnan S., Zhao Q.,
RA Meier I.;
RT "NUCLEAR PORE ANCHOR, the Arabidopsis homolog of Tpr/Mlp1/Mlp2/megator, is
RT involved in mRNA export and SUMO homeostasis and affects diverse aspects of
RT plant development.";
RL Plant Cell 19:1537-1548(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1411-1558.
RA Stracke R., Palme K.;
RT "Signal Peptide Selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17535820; DOI=10.1104/pp.107.100735;
RA Jacob Y., Mongkolsiriwatana C., Veley K.M., Kim S.Y., Michaels S.D.;
RT "The nuclear pore protein AtTPR is required for RNA homeostasis, flowering
RT time, and auxin signaling.";
RL Plant Physiol. 144:1383-1390(2007).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19704557; DOI=10.4161/psb.2.6.4836;
RA Xu X.M., Rose A., Meier I.;
RT "NUA Activities at the Plant Nuclear Pore.";
RL Plant Signal. Behav. 2:553-555(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP FUNCTION.
RX PubMed=19704774; DOI=10.4161/psb.3.1.4903;
RA Jacob Y., Michaels S.D.;
RT "Peering through the pore: The role of AtTPR in nuclear transport and
RT development.";
RL Plant Signal. Behav. 3:62-64(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2022, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND NOMENCLATURE.
RX PubMed=21189294; DOI=10.1105/tpc.110.079947;
RA Tamura K., Fukao Y., Iwamoto M., Haraguchi T., Hara-Nishimura I.;
RT "Identification and characterization of nuclear pore complex components in
RT Arabidopsis thaliana.";
RL Plant Cell 22:4084-4097(2010).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20872268; DOI=10.1007/s00425-010-1278-7;
RA Muthuswamy S., Meier I.;
RT "Genetic and environmental changes in SUMO homeostasis lead to nuclear mRNA
RT retention in plants.";
RL Planta 233:201-208(2011).
RN [12]
RP FUNCTION, INTERACTION WITH MAD1, AND DISRUPTION PHENOTYPE.
RX PubMed=22457071; DOI=10.1007/s11103-012-9903-4;
RA Ding D., Muthuswamy S., Meier I.;
RT "Functional interaction between the Arabidopsis orthologs of spindle
RT assembly checkpoint proteins MAD1 and MAD2 and the nucleoporin NUA.";
RL Plant Mol. Biol. 79:203-216(2012).
CC -!- FUNCTION: Component of the nuclear pore complex. Acts as a docking site
CC for activities required for desumoylation and mRNA export. Required for
CC the proper expression or localization of a subset of miRNAs. Plays a
CC role in meristematic cell division by interacting with spindle assembly
CC checkpoint proteins. {ECO:0000269|PubMed:17513499,
CC ECO:0000269|PubMed:17535820, ECO:0000269|PubMed:19704557,
CC ECO:0000269|PubMed:19704774, ECO:0000303|PubMed:20872268}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). The NPC has an eight-
CC fold symmetrical structure comprising a central transport channel and
CC two rings, the cytoplasmic and nuclear rings, to which eight filaments
CC are attached. The cytoplasmic filaments have loose ends, while the
CC nuclear filaments are joined in a distal ring, forming a nuclear
CC basket. NPCs are highly dynamic in configuration and composition, and
CC can be devided in 3 subcomplexes, the NUP62 subcomplex, the NUP107-160
CC subcomplex and the NUP93 subcomplex, containing approximately 30
CC different nucleoporin proteins. Interacts with MAD1 and (via N-
CC terminus) with ESD4. {ECO:0000269|PubMed:17513499,
CC ECO:0000269|PubMed:22457071, ECO:0000305|PubMed:21189294}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:17513499,
CC ECO:0000269|PubMed:19704557, ECO:0000269|PubMed:21189294}. Nucleus
CC membrane {ECO:0000269|PubMed:19704557}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19704557}; Nucleoplasmic side
CC {ECO:0000269|PubMed:19704557}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:19704557}. Note=Located at the inner surface of the
CC nuclear envelope during interphase and in the vicinity of the spindle
CC during prometaphase. {ECO:0000269|PubMed:17513499,
CC ECO:0000269|PubMed:19704557}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A4GSN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A4GSN8-2; Sequence=VSP_057128;
CC Name=3;
CC IsoId=A4GSN8-3; Sequence=VSP_057127;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in the shoot apical
CC region. {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:17535820}.
CC -!- INDUCTION: Not induced by vernalization. {ECO:0000269|PubMed:17535820}.
CC -!- DOMAIN: The N-terminal domain is involved in RNA and SUMO homeostasis
CC while the C-terminal part is required for nuclear pore association.
CC -!- DISRUPTION PHENOTYPE: Early flowering under both long and short days
CC and pleiotropic alterations in shoot development and auxin signaling.
CC Stunted primary root development in the absence of sucrose.
CC Accumulation of nuclear poly(A)+ RNA and high-molecular weight SUMO
CC conjugates. {ECO:0000269|PubMed:17513499, ECO:0000269|PubMed:17535820,
CC ECO:0000303|PubMed:20872268}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17058.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC17060.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC17073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC17074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF426860; ABO21684.1; -; mRNA.
DR EMBL; AC002986; AAC17058.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC002986; AAC17060.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC002986; AAC17073.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC002986; AAC17074.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36226.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36227.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36228.1; -; Genomic_DNA.
DR EMBL; AF083705; AAN60264.1; -; mRNA.
DR PIR; T01025; T01025.
DR PIR; T01026; T01026.
DR PIR; T01028; T01028.
DR PIR; T01029; T01029.
DR RefSeq; NP_001185435.1; NM_001198506.1. [A4GSN8-3]
DR RefSeq; NP_001185436.1; NM_001198507.1. [A4GSN8-2]
DR RefSeq; NP_178048.2; NM_106578.3. [A4GSN8-1]
DR AlphaFoldDB; A4GSN8; -.
DR SMR; A4GSN8; -.
DR BioGRID; 29487; 8.
DR IntAct; A4GSN8; 1.
DR STRING; 3702.AT1G79280.2; -.
DR iPTMnet; A4GSN8; -.
DR PaxDb; A4GSN8; -.
DR PRIDE; A4GSN8; -.
DR ProteomicsDB; 248663; -. [A4GSN8-1]
DR EnsemblPlants; AT1G79280.1; AT1G79280.1; AT1G79280. [A4GSN8-1]
DR EnsemblPlants; AT1G79280.2; AT1G79280.2; AT1G79280. [A4GSN8-2]
DR EnsemblPlants; AT1G79280.3; AT1G79280.3; AT1G79280. [A4GSN8-3]
DR GeneID; 844268; -.
DR Gramene; AT1G79280.1; AT1G79280.1; AT1G79280. [A4GSN8-1]
DR Gramene; AT1G79280.2; AT1G79280.2; AT1G79280. [A4GSN8-2]
DR Gramene; AT1G79280.3; AT1G79280.3; AT1G79280. [A4GSN8-3]
DR KEGG; ath:AT1G79280; -.
DR Araport; AT1G79280; -.
DR TAIR; locus:2207390; AT1G79280.
DR eggNOG; KOG4674; Eukaryota.
DR HOGENOM; CLU_001545_0_0_1; -.
DR InParanoid; A4GSN8; -.
DR OMA; KYDRVDP; -.
DR OrthoDB; 20957at2759; -.
DR PhylomeDB; A4GSN8; -.
DR PRO; PR:A4GSN8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A4GSN8; baseline and differential.
DR Genevisible; A4GSN8; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IMP:TAIR.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:TAIR.
DR GO; GO:0006606; P:protein import into nucleus; IEA:InterPro.
DR GO; GO:0048443; P:stamen development; IMP:TAIR.
DR InterPro; IPR012929; TPR/MLP1.
DR Pfam; PF07926; TPR_MLP1_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport.
FT CHAIN 1..2093
FT /note="Nuclear-pore anchor"
FT /id="PRO_0000395976"
FT REGION 1175..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..2093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 57..362
FT /evidence="ECO:0000255"
FT COILED 439..529
FT /evidence="ECO:0000255"
FT COILED 570..627
FT /evidence="ECO:0000255"
FT COILED 688..1172
FT /evidence="ECO:0000255"
FT COILED 1208..1252
FT /evidence="ECO:0000255"
FT COILED 1293..1585
FT /evidence="ECO:0000255"
FT COILED 1818..1849
FT /evidence="ECO:0000255"
FT COMPBIAS 1178..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1834
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1842..1901
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1903..1917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1920..1935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1982..2011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 787..792
FT /note="SVLKQE -> VYHHPLK (in isoform 3)"
FT /id="VSP_057127"
FT VAR_SEQ 942
FT /note="E -> EAALVIILDVVHKIQAGFRIGSA (in isoform 2)"
FT /id="VSP_057128"
SQ SEQUENCE 2093 AA; 237040 MW; DC03ED0639506402 CRC64;
MPLFMPDEEL ARLSSDAASV VAERADEYIR KIYAELDSVR AKADAASITA EQTCSLLEQK
YLSLSQDFSS LESQNAKLQS DFDDRLAELA QSQAQKHQLH LQSIEKDGEV ERMSTEMSEL
HKSKRQLMEL LEQKDAEISE KNSTIKSYLD KIVKLTDTSS EKEARLAEAT AELARSQAMC
SRLSQEKELT ERHAKWLDEE LTAKVDSYAE LRRRHSDLES EMSAKLVDVE KNYIECSSSL
NWHKERLREL ETKIGSLQED LSSCKDAATT TEEQYTAELF TANKLVDLYK ESSEEWSRKA
GELEGVIKAL EARLSQVESS YKERLDKEVS TKQLLEKENG DLKQKLEKCE AEIEKTRKTD
ELNLIPFSNF TRRVDNSGTS NMIEESQAVI SKVPAGVSGT ALAASLLRDG WSLAKIYEKY
QEAVDAMRHE QLGRKEAEMI LQRVLSELEE KAGFIQEERG EYERVVEAYC LVNQKLQDSV
SEQSNMEKFI MELKADLRRR ERENTLLQKD ISDLQKQVTI LLKECRDVQL RCGAARDDDE
DDYPLLSDVE MEMESEADKI ISEHLLKFKD INGLVEQNVK LRNLVRSLSE QIESRETELK
ETFEVDLKNK TDEASAKVAT VLKRAEEQGQ MIESLHTSVA MYKRLYEEEQ KLHSSDSRSS
DLSPAVVPGR KNFLHLLEDS EEATKRAQEK AFERIRILEE DFAKARSEVI AIRSERDKLA
MEANFAREKL EGIMKESERK REEMNSVLAR NIEFSQLIID HQRKLRESSE SLHAAEEISR
KLSMEVSVLK QEKELLSNAE KRASDEVSAL SQRVYRLQAT LDTVQSTEEV REETRAAERR
KQEEHIKQLQ REWAEAKKEL QEERSNARDF TSDRNQTLNN AVMQVEEMGK ELANALKAVS
VAESRASVAE ARLSDLEKKI RSSDPKTLDM DSGGIVSLSD KEMSIELRTA KEEIEKLRGE
VESSKSHMLQ YKSIAQVNET ALKQMESAHE NFRLEAEKRQ RSLEAELVSL RERVSELEND
CIQKSEQLAT AAAGKEDALL SASAEIASLR EENLVKKSQI EAMNIQMSTL KNDLETEHEK
WRVAQRNYER QVILLSETIQ ELTKTSQALA ALQEEASELR KLADARGIEN SELNAKWSEE
KLMLEQQKNL AEKKYHELNE QNKLLHSRLE AKHLNSAEKN SRSGTISSGS TDSDHLEDSG
LQRVVHYLRR TKEIAETEIS LMRQEKLRLQ SQLESALKMA ESARGSLTAE RASTRASLLT
DDGIKSLQLQ VSEMNLLRES NMQLREENKH NFEKCQEMRE VAQKARMESE NFENLLKTKQ
TELDLCMKEM EKLRMETDLH KKRVDELRET YRNIDIADYN RLKDEVRQLE EKLKAKDAHA
EDCKKVLLEK QNKISLLEKE LTNCKKDLSE REKRLDDAQQ AQATMQSEFN KQKQELEKNK
KIHYTLNMTK RKYEKEKDEL SKQNQSLAKQ LEEAKEEAGK RTTTDAVVEQ SVKEREEKEK
RIQILDKYVH QLKDEVRKKT EDLKKKDEEL TKERSERKSV EKEVGDSLTK IKKEKTKVDE
ELAKLERYQT ALTHLSEELE KLKHADGNLP EGTSAVQVLS GSILNDQAAA YVSAVEYFER
VARSIASNSQ VSTKPTDMVT EPSSGIPAAE PSTMTRVPSS TPLIKSPVAT TQQLPKVASD
NKEKRLISQK PSTEFRRPSG RRIVRPQLVK PEESPKVDVD MPEAEGTGDE GKQPAAHEPE
SQVTTSVRPV QTLVRKRQAD SLVSEPQQDS LTQGETSSEI APPASKKAKG SESHPDTSEG
ENLAKEPAID ELMDATTTTD GDNEETEAEN AEEKTEEYVE AQQDNEADEP VEESPTETET
IPTEEESRDQ TEEENQEPLT DMESDKEEGE LDLDTLEDLE EGTDVASMMR SPEKEEVQPE
TLATPTQSPS RMETAMEEAE TTIETPVEDD KTDEGGDAAE EAADIPNNAN DQQEAPETDI
KPETSAATTS PVSTAPTTSS TLASAITSSG APETEDPKRA PSPGGGSSTI VTLADRAQMK
RRERIANIVV SRAPNPATRG ARGRTVNLRG GGRLLPRGGR APRGGRGQSP SPP
