NFAT5_MOUSE
ID NFAT5_MOUSE Reviewed; 1534 AA.
AC Q9WV30; E9Q0P3; E9Q6U2; G5E8N9; Q91WY0; Q9JLA1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Nuclear factor of activated T-cells 5;
DE Short=NF-AT5;
DE AltName: Full=Rel domain-containing transcription factor NFAT5;
DE AltName: Full=T-cell transcription factor NFAT5;
GN Name=Nfat5;
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 4).
RA Lu J., Xu H., Olson E.N.;
RT "Identification of NFAT5, a new rel-like transcription factor.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-1534 (ISOFORM 3), ALTERNATIVE SPLICING,
RP FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND INDUCTION.
RC TISSUE=Brain;
RX PubMed=11934689; DOI=10.1152/ajprenal.00123.2001;
RA Maouyo D., Kim J.Y., Lee S.D., Wu Y., Woo S.K., Kwon H.M.;
RT "Mouse TonEBP-NFAT5: expression in early development and alternative
RT splicing.";
RL Am. J. Physiol. 282:F802-F809(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-1534 (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=11233530; DOI=10.1101/sqb.1999.64.517;
RA Lopez-Rodriguez C., Aramburu J., Rakeman A.S., Copeland N.G., Gilbert D.J.,
RA Thomas S., Disteche C., Jenkins N.A., Rao A.;
RT "NFAT5: the NF-AT family of transcription factors expands in a new
RT direction.";
RL Cold Spring Harb. Symp. Quant. Biol. 64:517-526(1999).
RN [6]
RP SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=10377394; DOI=10.1073/pnas.96.13.7214;
RA Lopez-Rodriguez C., Aramburu J., Rakeman A.S., Rao A.;
RT "NFAT5, a constitutively nuclear NFAT protein that does not cooperate with
RT Fos and Jun.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7214-7219(1999).
RN [7]
RP FUNCTION IN RENAL HOMEOSTASIS, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=14983020; DOI=10.1073/pnas.0308703100;
RA Lopez-Rodriguez C., Antos C.L., Shelton J.M., Richardson J.A., Lin F.,
RA Novobrantseva T.I., Bronson R.T., Igarashi P., Rao A., Olson E.N.;
RT "Loss of NFAT5 results in renal atrophy and lack of tonicity-responsive
RT gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2392-2397(2004).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY OSMOTIC STRESS.
RX PubMed=23233732; DOI=10.1194/jlr.m033365;
RA Ueno M., Shen W.J., Patel S., Greenberg A.S., Azhar S., Kraemer F.B.;
RT "Fat-specific protein 27 modulates nuclear factor of activated T cells 5
RT and the cellular response to stress.";
RL J. Lipid Res. 54:734-743(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Transcription factor involved in the transcriptional
CC regulation of osmoprotective and inflammatory genes. Regulates
CC hypertonicity-induced cellular accumulation of osmolytes.
CC {ECO:0000269|PubMed:11934689, ECO:0000269|PubMed:14983020}.
CC -!- SUBUNIT: Homodimer when bound to DNA, completely encircles its DNA
CC target. Does not bind with Fos and Jun transcription factors. Interacts
CC with CIDEC; this interaction is direct and retains NFAT5 in the
CC cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10377394,
CC ECO:0000269|PubMed:11934689}. Cytoplasm {ECO:0000269|PubMed:11934689}.
CC Note=Nuclear distribution increases under hypertonic conditions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=C;
CC IsoId=Q9WV30-1; Sequence=Displayed;
CC Name=2; Synonyms=D;
CC IsoId=Q9WV30-2; Sequence=VSP_058790;
CC Name=3; Synonyms=B;
CC IsoId=Q9WV30-3; Sequence=VSP_058790, VSP_058791, VSP_058789;
CC Name=4;
CC IsoId=Q9WV30-4; Sequence=VSP_058792, VSP_058793;
CC -!- TISSUE SPECIFICITY: Detected in white and brown adipose tissue, muscle,
CC heart, liver and kidney. Expressed in lymphocytes (at protein level).
CC {ECO:0000269|PubMed:14983020, ECO:0000269|PubMed:23233732}.
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc, expressed in brain and developing
CC lens. At 12.5 dpc, the expression is extended to liver. By 17.5 dpc,
CC expressed abundantly in brain, spinal cord, heart end liver and
CC moderately in salivary gland, lung, kidney, gut and bladder (at protein
CC level). {ECO:0000269|PubMed:11934689}.
CC -!- INDUCTION: Up-regulated upon hypertonic conditions, this up-regulation
CC in not observed in ES cells. {ECO:0000269|PubMed:11934689,
CC ECO:0000269|PubMed:23233732}.
CC -!- PTM: Phosphorylated at Thr-135 by CDK5 in response to osmotic stress;
CC this phosphorylation mediates its rapid nuclear localization.
CC -!- DISRUPTION PHENOTYPE: Embryonic and perinatal lethality with incomplete
CC penetrance. At 17.5 dpc, 50% of the expected Mendelian rate with only
CC 3.4% of the expected number living past 21 days after birth. The few
CC survivors to adulthood fail to thrive and their weight is half compared
CC to the wild-type. At 3 weeks old, kidney hypoplasia and an altered
CC medullary morphology are observed with an increased apoptosis in the
CC kidney inner medulla. Under osmotic stress, the transcriptional
CC regulation of osmoprotective genes is altered in the kidney medulla.
CC {ECO:0000269|PubMed:14983020}.
CC -!- MISCELLANEOUS: [Isoform 1]: May have longer half-life and is more
CC efficient in stimulation of transcription than isoform 3.
CC -!- MISCELLANEOUS: [Isoform 3]: The transcript encoding this isoform
CC contains an alternative coding exon 4 which contains 2 stop codons and
CC could target the transcript to nonsense-mediated mRNA decay after the
CC pioneer round of translation, as suggested by decreased NFAT5 protein
CC levels when the number of exon 4-containing transcripts increases. The
CC insertion of exon 4 is stimulated in the presence of DDX5 and DDX17.
CC {ECO:0000269|PubMed:10377394}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31405.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK97603.1; Type=Erroneous translation; Evidence={ECO:0000305};
CC Sequence=EDL11405.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF162853; AAD44343.1; -; mRNA.
DR EMBL; AC125207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11404.1; -; Genomic_DNA.
DR EMBL; CH466525; EDL11405.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF369980; AAK97603.1; ALT_SEQ; mRNA.
DR EMBL; AF200687; AAF31405.1; ALT_INIT; mRNA.
DR CCDS; CCDS22648.2; -. [Q9WV30-2]
DR CCDS; CCDS72168.1; -. [Q9WV30-4]
DR RefSeq; NP_001273189.1; NM_001286260.1. [Q9WV30-4]
DR RefSeq; NP_061293.2; NM_018823.2. [Q9WV30-2]
DR RefSeq; NP_598718.2; NM_133957.3.
DR RefSeq; XP_006531255.1; XM_006531192.3. [Q9WV30-1]
DR RefSeq; XP_017168393.1; XM_017312904.1.
DR AlphaFoldDB; Q9WV30; -.
DR SMR; Q9WV30; -.
DR BioGRID; 207661; 4.
DR IntAct; Q9WV30; 2.
DR MINT; Q9WV30; -.
DR STRING; 10090.ENSMUSP00000127784; -.
DR iPTMnet; Q9WV30; -.
DR PhosphoSitePlus; Q9WV30; -.
DR EPD; Q9WV30; -.
DR jPOST; Q9WV30; -.
DR MaxQB; Q9WV30; -.
DR PaxDb; Q9WV30; -.
DR PRIDE; Q9WV30; -.
DR ProteomicsDB; 293539; -. [Q9WV30-1]
DR ProteomicsDB; 293540; -. [Q9WV30-2]
DR ProteomicsDB; 293541; -. [Q9WV30-3]
DR ProteomicsDB; 293542; -. [Q9WV30-4]
DR Antibodypedia; 29866; 317 antibodies from 30 providers.
DR DNASU; 54446; -.
DR Ensembl; ENSMUST00000075922; ENSMUSP00000075311; ENSMUSG00000003847. [Q9WV30-4]
DR Ensembl; ENSMUST00000125721; ENSMUSP00000116094; ENSMUSG00000003847. [Q9WV30-1]
DR Ensembl; ENSMUST00000133026; ENSMUSP00000116631; ENSMUSG00000003847. [Q9WV30-3]
DR Ensembl; ENSMUST00000151114; ENSMUSP00000119370; ENSMUSG00000003847. [Q9WV30-2]
DR Ensembl; ENSMUST00000169453; ENSMUSP00000127784; ENSMUSG00000003847. [Q9WV30-2]
DR GeneID; 54446; -.
DR KEGG; mmu:54446; -.
DR UCSC; uc009nhl.2; mouse. [Q9WV30-2]
DR UCSC; uc009nhm.3; mouse. [Q9WV30-4]
DR UCSC; uc009nhp.1; mouse. [Q9WV30-1]
DR CTD; 10725; -.
DR MGI; MGI:1859333; Nfat5.
DR VEuPathDB; HostDB:ENSMUSG00000003847; -.
DR eggNOG; ENOG502QSVE; Eukaryota.
DR GeneTree; ENSGT00940000155213; -.
DR HOGENOM; CLU_004396_0_0_1; -.
DR InParanoid; Q9WV30; -.
DR OMA; LMETPGN; -.
DR OrthoDB; 95502at2759; -.
DR TreeFam; TF326480; -.
DR BioGRID-ORCS; 54446; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Nfat5; mouse.
DR PRO; PR:Q9WV30; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9WV30; protein.
DR Bgee; ENSMUSG00000003847; Expressed in humerus cartilage element and 250 other tissues.
DR ExpressionAtlas; Q9WV30; baseline and differential.
DR Genevisible; Q9WV30; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IBA:GO_Central.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; TAS:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR008366; NFAT.
DR InterPro; IPR015646; NFAT5.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR12533; PTHR12533; 1.
DR PANTHER; PTHR12533:SF10; PTHR12533:SF10; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR01789; NUCFACTORATC.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cytoplasm; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1534
FT /note="Nuclear factor of activated T-cells 5"
FT /id="PRO_0000205184"
FT DOMAIN 264..443
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT DNA_BIND 293..300
FT /evidence="ECO:0000250"
FT REGION 34..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1478..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT MOD_RES 135
FT /note="Phosphothreonine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT CROSSLNK 602
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94916"
FT VAR_SEQ 24
FT /note="R -> RDSLKLHPSQTFHRAGLLE (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:11233530,
FT ECO:0000305|PubMed:11934689"
FT /id="VSP_058790"
FT VAR_SEQ 67..81
FT /note="DASSAPSSSSMGGAC -> GFASEAGSVCIKNDL (in isoform 3)"
FT /evidence="ECO:0000305|PubMed:11934689"
FT /id="VSP_058791"
FT VAR_SEQ 82..1534
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305|PubMed:11934689"
FT /id="VSP_058789"
FT VAR_SEQ 1213..1225
FT /note="VALGSLPPNPMPQ -> ESLHSHITPDACK (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_058792"
FT VAR_SEQ 1226..1534
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_058793"
FT CONFLICT 108
FT /note="C -> G (in Ref. 4; AAK97603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1534 AA; 165800 MW; 996904A84D3A7AFE CRC64;
MPSDFISLLS ADLDLESPKS LYSRESVYDL LPKELQLPPP RETSVASMSQ TSGGEAGSPP
PAVVAADASS APSSSSMGGA CSSFTTSSSP TIYSTSVTDS KAMQVESCSS AVGVSNRGVS
EKQLTGNTVQ QHPSTPKRHT VLYISPPPED LLDNSRMSCQ DEGCGLESEQ SCSMWMEDSP
SNFSNMSTSS YNDNTEVPRK SRKRNPKQRP GVKRRDCEES NMDIFDADSA KAPHYVLSQL
TTDNKGNSKA GNGTLDSQKG TGVKKSPMLC GQYPVKSEGK ELKIVVQPET QHRARYLTEG
SRGSVKDRTQ QGFPTVKLEG HNEPVVLQVF VGNDSGRVKP HGFYQACRVT GRNTTPCKEV
DIEGTTVIEV GLDPSNNMTL AVDCVGILKL RNADVEARIG IAGSKKKSTR ARLVFRVNIT
RKDGSTLTLQ TPSSPILCTQ PAGVPEILKK SLHSCSVKGE EEVFLIGKNF LKGTKVIFQE
NVSDENSWKS EAEIDMELFH QNHLIVKVPP YHDQHITLPV SVGIYVVTNA GRSHDVQPFT
YTPDPAAGAL NVNVKKEISS PARPCSFEEA MKAMKTTGCN VDKVTILPNA LITPLISSSM
IKTEDVTPME VTSEKRSSPI FQTTKSIGST QQTLETISNI AGGAPFSSPS SSSHLTPESE
NQQQLQPKAY NPETLTTIQT QDISQPGTFP AVSAASQLPS SDALLQQATQ FQTREAQSRD
TIQSDTVVNL SQLTEASQQQ QSPLQEQAQT LQQQIPSNIF PSPSSVSQLQ STIQQLQAGS
FTGSAAGGRS GSVDLVQQVL EAQQQLSSVL FSTPDGNENV QEQLNADIFQ VSQIQNSVSP
GMFSSAESAV HTRPDNLLPG RADSVHQQTE NTLSNQQQQQ QQQQQVMESS AAMVMEMQQS
ICQAAAQIQS ELFPSAASAS GSLQQSPVYQ QPSHMMSALP TNEDMQMQCE LFSSPPAASG
NETSTTTTPQ VATPGSTMFQ TPSSGDGEET GAQAKQIQNS VFQTMVQMQR SGDSQPQVNL
FSSTKNIMSV QNNGTQQQGN SLFQQGSEMM SLQSGNFLQQ SSHSQAQLFH PQNPIADAQN
LSQETQGSIF HSPNPIVHSQ TSTASSEQLQ PSMFHSQNTI AVLQGSSVPQ DQQSPNIFLS
QSSINNLQTN TVAQEEQISF FAAQNSISPL QSTSNTEQQA AFQQQPPISH IQTPILSQEQ
AQPSQQGLFQ PQVALGSLPP NPMPQNQQGP IFQTQRPIVG MQSNSPSQEQ QQQQQQQQQQ
QQQQQQQQQS ILFSNQNAMA TMASQKQPPP NMMFSPNQNP MASQEQQNQS IFHQQSNMAP
MNQEQQPMQF QNQPTVSSLQ NPGPTQSESP QTSLFHSSPQ IQLVQGSPSS QDQQVTLFLS
PASMSALQTS INQPDMQQSP LYSPQNNIPG IQGSTSSPQP QATLFHNTTG GTINQIQNSP
GSSQQTSGMF LFGIQNNCSQ LLTSGPATLP DQLMAINQQG QPQNEGQSSV TTLLSQQMPE
TSPLASSVNS SQNMEKIDLL VSLQSQGNNL TGSF
