GBRB2_MOUSE
ID GBRB2_MOUSE Reviewed; 512 AA.
AC P63137; A6H6R7; D1LYT3; P15432;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-2;
DE AltName: Full=GABA(A) receptor subunit beta-2;
DE Flags: Precursor;
GN Name=Gabrb2; Synonyms=Gabrb-2;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX PubMed=7893750; DOI=10.1016/0167-4781(95)00009-6;
RA Kamatchi G.L., Kofuji P., Wang J.B., Fernando J.C., Liu Z., Mathura J.R.,
RA Burt D.R.;
RT "GABAA receptor beta 1, beta 2, and beta 3 subunits: comparisons in DBA/2J
RT and C57BL/6J mice.";
RL Biochim. Biophys. Acta 1261:134-142(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=19763268; DOI=10.1371/journal.pone.0006977;
RA Zhao C., Xu Z., Wang F., Chen J., Ng S.K., Wong P.W., Yu Z., Pun F.W.,
RA Ren L., Lo W.S., Tsang S.Y., Xue H.;
RT "Alternative-splicing in the exon-10 region of GABA(A) receptor beta(2)
RT subunit gene: relationships between novel isoforms and psychotic
RT disorders.";
RL PLoS ONE 4:E6977-E6977(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-441, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
RP INTERACTION WITH KCTD8; KCTD12; KCTD12B AND KCTD16, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20400944; DOI=10.1038/nature08964;
RA Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA Bettler B.;
RT "Native GABA(B) receptors are heteromultimers with a family of auxiliary
RT subunits.";
RL Nature 465:231-235(2010).
RN [9]
RP FUNCTION, GLYCOSYLATION, AND DOMAIN EXTRACELLULAR.
RX PubMed=27129275; DOI=10.1074/jbc.m116.714790;
RA Brown L.E., Nicholson M.W., Arama J.E., Mercer A., Thomson A.M.,
RA Jovanovic J.N.;
RT "Gamma-aminobutyric acid type A (GABAA) receptor subunits play a direct
RT structural role in synaptic contact formation via their N-terminal
RT extracellular domains.";
RL J. Biol. Chem. 291:13926-13942(2016).
CC -!- FUNCTION: Ligand-gated chloride channel which is a component of the
CC heteropentameric receptor for GABA, the major inhibitory
CC neurotransmitter in the brain (PubMed:20400944). Plays an important
CC role in the formation of functional inhibitory GABAergic synapses in
CC addition to mediating synaptic inhibition as a GABA-gated ion channel
CC (PubMed:27129275). The gamma2 subunit is necessary but not sufficient
CC for a rapid formation of active synaptic contacts and the synaptogenic
CC effect of this subunit is influenced by the type of alpha and beta
CC subunits present in the receptor pentamer (PubMed:27129275). The
CC alpha1/beta2/gamma2 receptor and the alpha2/beta2/gamma2 receptor
CC exhibit synaptogenic activity (PubMed:27129275). Functions also as
CC histamine receptor and mediates cellular responses to histamine (By
CC similarity). {ECO:0000250|UniProtKB:P63138,
CC ECO:0000269|PubMed:20400944, ECO:0000269|PubMed:27129275}.
CC -!- ACTIVITY REGULATION: Allosterically activated by benzodiazepines and
CC the anesthetic etomidate (By similarity). Inhibited by the antagonist
CC bicuculline (By similarity). {ECO:0000250|UniProtKB:P0C2W5,
CC ECO:0000250|UniProtKB:P47870}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains (By similarity). Interacts with UBQLN1 (By
CC similarity). Interacts with KCTD8, KCTD12 and KCTD16; this interaction
CC determines the pharmacology and kinetics of the receptor response, the
CC KCTD proteins markedly accelerating the GABA-B response, although to
CC different extents (PubMed:20400944). May interact with KIF21B (By
CC similarity). Identified in a complex of 720 kDa composed of LHFPL4,
CC NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (By similarity).
CC {ECO:0000250|UniProtKB:P63138, ECO:0000269|PubMed:20400944}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:20400944}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20400944}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P63138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=P63137-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P63137-2; Sequence=VSP_038829;
CC -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC formation. {ECO:0000269|PubMed:27129275}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:27129275}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRB2 sub-
CC subfamily. {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; U14419; AAA79974.1; -; mRNA.
DR EMBL; GU086167; ACY69098.1; -; mRNA.
DR EMBL; AK090279; BAC41155.1; -; mRNA.
DR EMBL; AL627444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466609; EDL32344.1; -; Genomic_DNA.
DR EMBL; BC145973; AAI45974.1; -; mRNA.
DR EMBL; BC145975; AAI45976.1; -; mRNA.
DR CCDS; CCDS24555.1; -. [P63137-2]
DR CCDS; CCDS88146.1; -. [P63137-1]
DR PIR; S53531; S53531.
DR RefSeq; NP_001334243.1; NM_001347314.1. [P63137-1]
DR RefSeq; NP_032096.1; NM_008070.3. [P63137-2]
DR RefSeq; XP_011247028.1; XM_011248726.1.
DR RefSeq; XP_017169750.1; XM_017314261.1.
DR AlphaFoldDB; P63137; -.
DR SMR; P63137; -.
DR BioGRID; 199803; 3.
DR ComplexPortal; CPX-2979; GABA-A receptor, alpha-1/beta-2/gamma-2.
DR ComplexPortal; CPX-2987; GABA-A receptor, alpha-6/beta-2/delta.
DR ComplexPortal; CPX-2988; GABA-A receptor, alpha-4/beta-2/delta.
DR IntAct; P63137; 1.
DR MINT; P63137; -.
DR STRING; 10090.ENSMUSP00000007797; -.
DR ChEMBL; CHEMBL4296059; -.
DR GlyConnect; 2325; 6 N-Linked glycans (1 site).
DR GlyGen; P63137; 3 sites, 6 N-linked glycans (1 site).
DR iPTMnet; P63137; -.
DR PhosphoSitePlus; P63137; -.
DR SwissPalm; P63137; -.
DR MaxQB; P63137; -.
DR PeptideAtlas; P63137; -.
DR PRIDE; P63137; -.
DR ProteomicsDB; 267774; -. [P63137-1]
DR ProteomicsDB; 267775; -. [P63137-2]
DR Antibodypedia; 4534; 335 antibodies from 34 providers.
DR DNASU; 14401; -.
DR Ensembl; ENSMUST00000007797; ENSMUSP00000007797; ENSMUSG00000007653. [P63137-2]
DR Ensembl; ENSMUST00000192403; ENSMUSP00000141868; ENSMUSG00000007653. [P63137-1]
DR GeneID; 14401; -.
DR KEGG; mmu:14401; -.
DR UCSC; uc007imi.1; mouse. [P63137-2]
DR UCSC; uc011xte.1; mouse. [P63137-1]
DR CTD; 2561; -.
DR MGI; MGI:95620; Gabrb2.
DR VEuPathDB; HostDB:ENSMUSG00000007653; -.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000154245; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; P63137; -.
DR OMA; INKMDPH; -.
DR OrthoDB; 480926at2759; -.
DR PhylomeDB; P63137; -.
DR TreeFam; TF315453; -.
DR Reactome; R-MMU-977443; GABA receptor activation.
DR BioGRID-ORCS; 14401; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Gabrb2; mouse.
DR PRO; PR:P63137; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P63137; protein.
DR Bgee; ENSMUSG00000007653; Expressed in lateral geniculate body and 135 other tissues.
DR Genevisible; P63137; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1902710; C:GABA receptor complex; ISO:MGI.
DR GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0016917; F:GABA receptor activity; ISO:MGI.
DR GO; GO:0004890; F:GABA-A receptor activity; ISS:UniProtKB.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISO:MGI.
DR GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; ISO:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0090102; P:cochlea development; IMP:DFLAT.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:MGI.
DR GO; GO:1904862; P:inhibitory synapse assembly; IDA:UniProtKB.
DR GO; GO:0060119; P:inner ear receptor cell development; IMP:DFLAT.
DR GO; GO:0060384; P:innervation; IMP:DFLAT.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:DFLAT.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:DFLAT.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; IMP:DFLAT.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:DFLAT.
DR GO; GO:0007605; P:sensory perception of sound; IMP:DFLAT.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:MGI.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR002289; GABAAb_rcpt.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR01160; GABAARBETA.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Chloride; Chloride channel;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..512
FT /note="Gamma-aminobutyric acid receptor subunit beta-2"
FT /id="PRO_0000000460"
FT TOPO_DOM 26..244
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..266
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..292
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 327..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 490..511
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 441
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..174
FT /evidence="ECO:0000250"
FT VAR_SEQ 360..397
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7893750"
FT /id="VSP_038829"
SQ SEQUENCE 512 AA; 59197 MW; 41AC9154A438E4FF CRC64;
MWRVRKRGYF GIWSFPLIIA AVCAQSVNDP SNMSLVKETV DRLLKGYDIR LRPDFGGPPV
AVGMNIDIAS IDMVSEVNMD YTLTMYFQQA WRDKRLSYNV IPLNLTLDNR VADQLWVPDT
YFLNDKKSFV HGVTVKNRMI RLHPDGTVLY GLRITTTAAC MMDLRRYPLD EQNCTLEIES
YGYTTDDIEF YWRGDDNAVT GVTKIELPQF SIVDYKLITK KVVFSTGSYP RLSLSFKLKR
NIGYFILQTY MPSILITILS WVSFWINYDA SAARVALGIT TVLTMTTINT HLRETLPKIP
YVKAIDMYLM GCFVFVFMAL LEYALVNYIF FGRGPQRQKK AAEKAANANN EKMRLDVNKM
FYKDIKQNGT QYRSLWDPTG DLSPTRRTTN YDFSLYTMDP HENILLSTLE IKNEMATSEA
VMGLGDPRST MLAYDASSIQ YRKAGLPRHS FGRNALERHV AQKKSRLRRR ASQLKITIPD
LTDVNAIDRW SRIFFPVVFS FFNIVYWLYY VN
