TOX_MOUSE
ID TOX_MOUSE Reviewed; 526 AA.
AC Q66JW3; Q8BKH9; Q8BYQ5; Q8R4H0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Thymocyte selection-associated high mobility group box protein TOX {ECO:0000303|PubMed:11850626};
DE AltName: Full=Thymus high mobility group box protein TOX {ECO:0000303|PubMed:11850626};
GN Name=Tox {ECO:0000303|PubMed:11850626, ECO:0000312|MGI:MGI:2181659};
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 1), FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X 129S2; TISSUE=Thymus;
RX PubMed=11850626; DOI=10.1038/ni767;
RA Wilkinson B., Chen J.-Y., Han P., Rufner K.M., Goularte O.D., Kaye J.;
RT "TOX: an HMG box protein implicated in the regulation of thymocyte
RT selection.";
RL Nat. Immunol. 3:272-280(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic eye, Hypothalamus, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic limb;
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 FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15078895; DOI=10.1084/jem.20040051;
RA Aliahmad P., O'Flaherty E., Han P., Goularte O.D., Wilkinson B., Satake M.,
RA Molkentin J.D., Kaye J.;
RT "TOX provides a link between calcineurin activation and CD8 lineage
RT commitment.";
RL J. Exp. Med. 199:1089-1099(2004).
RN [5]
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=18195075; DOI=10.1084/jem.20071944;
RA Aliahmad P., Kaye J.;
RT "Development of all CD4 T lineages requires nuclear factor TOX.";
RL J. Exp. Med. 205:245-256(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20818394; DOI=10.1038/ni.1930;
RA Aliahmad P., de la Torre B., Kaye J.;
RT "Shared dependence on the DNA-binding factor TOX for the development of
RT lymphoid tissue-inducer cell and NK cell lineages.";
RL Nat. Immunol. 11:945-952(2010).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=25527292; DOI=10.15252/embj.201490061;
RA Artegiani B., de Jesus Domingues A.M., Bragado Alonso S., Brandl E.,
RA Massalini S., Dahl A., Calegari F.;
RT "Tox: a multifunctional transcription factor and novel regulator of
RT mammalian corticogenesis.";
RL EMBO J. 34:896-910(2015).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25915732; DOI=10.1038/ni.3168;
RA Seehus C.R., Aliahmad P., de la Torre B., Iliev I.D., Spurka L.,
RA Funari V.A., Kaye J.;
RT "The development of innate lymphoid cells requires TOX-dependent generation
RT of a common innate lymphoid cell progenitor.";
RL Nat. Immunol. 16:599-608(2015).
RN [9]
RP FUNCTION, INDUCTION (MICROBIAL INFECTION), AND INTERACTION WITH HBO1
RP COMPLEX; DNMT1; LEO1; PAF1; SAP130 AND SIN3A.
RX PubMed=31207603; DOI=10.1038/s41586-019-1325-x;
RA Khan O., Giles J.R., McDonald S., Manne S., Ngiow S.F., Patel K.P.,
RA Werner M.T., Huang A.C., Alexander K.A., Wu J.E., Attanasio J., Yan P.,
RA George S.M., Bengsch B., Staupe R.P., Donahue G., Xu W., Amaravadi R.K.,
RA Xu X., Karakousis G.C., Mitchell T.C., Schuchter L.M., Kaye J.,
RA Berger S.L., Wherry E.J.;
RT "TOX transcriptionally and epigenetically programs CD8+ T cell
RT exhaustion.";
RL Nature 571:211-218(2019).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=31207604; DOI=10.1038/s41586-019-1324-y;
RA Scott A.C., Duendar F., Zumbo P., Chandran S.S., Klebanoff C.A.,
RA Shakiba M., Trivedi P., Menocal L., Appleby H., Camara S., Zamarin D.,
RA Walther T., Snyder A., Femia M.R., Comen E.A., Wen H.Y., Hellmann M.D.,
RA Anandasabapathy N., Liu Y., Altorki N.K., Lauer P., Levy O., Glickman M.S.,
RA Kaye J., Betel D., Philip M., Schietinger A.;
RT "TOX is a critical regulator of tumour-specific T cell differentiation.";
RL Nature 571:270-274(2019).
RN [11]
RP STRUCTURE BY NMR OF 251-339.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the HMG-box domain of thymus high mobility group box
RT protein TOX from mouse.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Transcriptional regulator with a major role in neural stem
CC cell commitment and corticogenesis as well as in lymphoid cell
CC development and lymphoid tissue organogenesis (PubMed:25527292,
CC PubMed:20818394, PubMed:11850626, PubMed:18195075, PubMed:15078895,
CC PubMed:25915732). Binds to GC-rich DNA sequences in the proximity of
CC transcription start sites and may alter chromatin structure, modifying
CC access of transcription factors to DNA (PubMed:25527292,
CC PubMed:31207603, PubMed:31207604). During cortical development,
CC controls the neural stem cell pool by inhibiting the switch from
CC proliferative to differentiating progenitors. Beyond progenitor cells,
CC promotes neurite outgrowth in newborn neurons migrating to reach the
CC cortical plate. May activate or repress critical genes for neural stem
CC cell fate such as SOX2, EOMES and ROBO2 (PubMed:25527292). Plays an
CC essential role in the development of lymphoid tissue-inducer (LTi)
CC cells, a subset necessary for the formation of secondary lymphoid
CC organs: peripheral lymph nodes and Peyer's patches (PubMed:20818394).
CC Acts as a developmental checkpoint and regulates thymocyte positive
CC selection toward T cell lineage commitment (PubMed:11850626,
CC PubMed:18195075). Required for the development of various T cell
CC subsets, including CD4-positive helper T cells, CD8-positive cytotoxic
CC T cells, regulatory T cells and CD1D-dependent natural killer T (NKT)
CC cells (PubMed:18195075, PubMed:15078895). Required for the
CC differentiation of common lymphoid progenitors (CMP) to innate lymphoid
CC cells (ILC). May regulate the NOTCH-mediated gene program, promoting
CC differentiation of the ILC lineage (PubMed:25915732). Required at the
CC progenitor phase of NK cell development in the bone marrow to specify
CC NK cell lineage commitment (PubMed:20818394). Upon chronic antigen
CC stimulation, diverts T cell development by promoting the generation of
CC exhaustive T cells, while suppressing effector and memory T cell
CC programming. May regulate the expression of genes encoding inhibitory
CC receptors such as PDCD1 and induce the exhaustion program, to prevent
CC the overstimulation of T cells and activation-induced cell death
CC (PubMed:31207603, PubMed:31207604). {ECO:0000269|PubMed:11850626,
CC ECO:0000269|PubMed:15078895, ECO:0000269|PubMed:18195075,
CC ECO:0000269|PubMed:20818394, ECO:0000269|PubMed:25527292,
CC ECO:0000269|PubMed:25915732, ECO:0000269|PubMed:31207603,
CC ECO:0000269|PubMed:31207604}.
CC -!- SUBUNIT: Interacts with HBO1 complex composed at least of KAT7/HBO1,
CC ING4, MEAF6, and JADE2; this complex is involved in histone
CC acetylation. Interacts with DNMT1, LEO1, PAF1, SAP130 and SIN3A; these
CC interactors regulate chromatin remodeling. Interacts with an array of
CC proteins involved in RNA processing and translation and DNA
CC replication. {ECO:0000269|PubMed:31207603}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:11850626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66JW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66JW3-2; Sequence=VSP_019598, VSP_019599;
CC -!- TISSUE SPECIFICITY: Expressed in neurons of the subventricular zone (at
CC protein level) (PubMed:25527292). Expressed in distinct subpopulations
CC of thymocytes undergoing positive selection: double CD4-positive CD8-
CC positive (DP) cells, CD4-positive CD8-low transitional cells and in
CC single CD4-positive and CD8-positive cells (at protein level)
CC (PubMed:11850626, PubMed:15078895). Expressed in ILC progenitors and
CC mature ILC subsets: ILC1, ILC2 and ILC3 (at protein level)
CC (PubMed:25915732). Expressed in lymphoid tissue-inducer cells and bone
CC marrow NK cell subsets (PubMed:20818394). Abundant in thymus, liver and
CC brain. Also detected in small intestine, spleen, stomach and testis
CC (PubMed:11850626). Highly expressed in tumor-infiltrating CD8-positive
CC T cells (at protein level) (PubMed:31207604).
CC {ECO:0000269|PubMed:11850626, ECO:0000269|PubMed:15078895,
CC ECO:0000269|PubMed:20818394, ECO:0000269|PubMed:25527292,
CC ECO:0000269|PubMed:25915732, ECO:0000269|PubMed:31207604}.
CC -!- DEVELOPMENTAL STAGE: In the developing brain, expressed at embryonic
CC day 9.5 dpc in neuroepithelium, displaying a rostral-high/ caudal-low
CC and lateral-high/medial-low expression pattern. Abundant at 15.5 dpc in
CC progenitors of the ventricular zone and differentiated neurons in the
CC cortical plate. The lateral-medial gradient spread further in all cells
CC of the ventricular zone of the lateral cortex by 18.5 dpc (at protein
CC level). {ECO:0000269|PubMed:25527292}.
CC -!- INDUCTION: Transiently up-regulated during key developmental transition
CC of immune cell subsets, likely marking a developmental checkpoint. Up-
CC regulated during beta and positive selection of developing thymocytes,
CC upon activation of pre-T cell receptor or T cell receptor in a
CC calcineurin-dependent manner (PubMed:11850626, PubMed:15078895). Low
CC expression is detected in precursor bone marrow NK cells, then is up-
CC regulated in immature and mature bone marrow NK cells and later down-
CC regulated in splenic mature NK cells (PubMed:20818394).
CC {ECO:0000269|PubMed:11850626, ECO:0000269|PubMed:15078895,
CC ECO:0000269|PubMed:20818394}.
CC -!- INDUCTION: (Microbial infection) Up-regulated in LCMV-specific CD8-
CC positive T cells. Expressed at high levels in exhausted T cells during
CC chronic infection. {ECO:0000269|PubMed:31207603}.
CC -!- DOMAIN: The HMG box is critical for TOX-dependent CD4-positive T cell
CC lineage commitment. {ECO:0000269|PubMed:18195075}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice lack lymph nodes. The development of
CC Peyer's patches is compromised, detectable only in some mutants.
CC Peyer's patches are much smaller in size less abundant when compared to
CC wild-type littermates. T cell lymphopenia is a hallmark phenotype of
CC TOX-deficient mice. {ECO:0000269|PubMed:18195075,
CC ECO:0000269|PubMed:20818394}.
CC -!- SIMILARITY: Belongs to the high motility group (HMG) box superfamily.
CC {ECO:0000305}.
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DR EMBL; AF472514; AAL78656.1; -; mRNA.
DR EMBL; AK029694; BAC26568.1; -; mRNA.
DR EMBL; AK038671; BAC30091.1; -; mRNA.
DR EMBL; AK051947; BAC34818.1; -; mRNA.
DR EMBL; BC080732; AAH80732.1; -; mRNA.
DR CCDS; CCDS17953.1; -. [Q66JW3-1]
DR RefSeq; NP_663757.3; NM_145711.4. [Q66JW3-1]
DR RefSeq; XP_006538007.1; XM_006537944.3.
DR RefSeq; XP_006538008.1; XM_006537945.2.
DR PDB; 2CO9; NMR; -; A=251-339.
DR PDBsum; 2CO9; -.
DR AlphaFoldDB; Q66JW3; -.
DR BMRB; Q66JW3; -.
DR SMR; Q66JW3; -.
DR BioGRID; 232958; 1.
DR STRING; 10090.ENSMUSP00000037966; -.
DR iPTMnet; Q66JW3; -.
DR PhosphoSitePlus; Q66JW3; -.
DR EPD; Q66JW3; -.
DR MaxQB; Q66JW3; -.
DR PaxDb; Q66JW3; -.
DR PeptideAtlas; Q66JW3; -.
DR PRIDE; Q66JW3; -.
DR ProteomicsDB; 258955; -. [Q66JW3-1]
DR ProteomicsDB; 258956; -. [Q66JW3-2]
DR Antibodypedia; 11831; 166 antibodies from 30 providers.
DR DNASU; 252838; -.
DR Ensembl; ENSMUST00000039987; ENSMUSP00000037966; ENSMUSG00000041272. [Q66JW3-1]
DR GeneID; 252838; -.
DR KEGG; mmu:252838; -.
DR UCSC; uc008rxs.2; mouse. [Q66JW3-1]
DR UCSC; uc008rxt.1; mouse. [Q66JW3-2]
DR CTD; 9760; -.
DR MGI; MGI:2181659; Tox.
DR VEuPathDB; HostDB:ENSMUSG00000041272; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000159497; -.
DR HOGENOM; CLU_030650_2_0_1; -.
DR InParanoid; Q66JW3; -.
DR OMA; PMQQSIG; -.
DR OrthoDB; 818359at2759; -.
DR PhylomeDB; Q66JW3; -.
DR TreeFam; TF106481; -.
DR BioGRID-ORCS; 252838; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Tox; mouse.
DR EvolutionaryTrace; Q66JW3; -.
DR PRO; PR:Q66JW3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q66JW3; protein.
DR Bgee; ENSMUSG00000041272; Expressed in rib and 261 other tissues.
DR Genevisible; Q66JW3; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0043373; P:CD4-positive, alpha-beta T cell lineage commitment; IMP:UniProtKB.
DR GO; GO:0002362; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment; IMP:UniProtKB.
DR GO; GO:0043375; P:CD8-positive, alpha-beta T cell lineage commitment; IMP:UniProtKB.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0002521; P:leukocyte differentiation; IBA:GO_Central.
DR GO; GO:0048535; P:lymph node development; IMP:MGI.
DR GO; GO:0030098; P:lymphocyte differentiation; IMP:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; ISO:MGI.
DR GO; GO:0002364; P:NK T cell lineage commitment; IMP:UniProtKB.
DR GO; GO:0048541; P:Peyer's patch development; IMP:MGI.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; IMP:UniProtKB.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IMP:MGI.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:1902232; P:regulation of positive thymic T cell selection; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; DNA-binding;
KW Neurogenesis; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..526
FT /note="Thymocyte selection-associated high mobility group
FT box protein TOX"
FT /id="PRO_0000244570"
FT DNA_BIND 261..329
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 194..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 237..256
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 194..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 232
FT /note="I -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019598"
FT VAR_SEQ 233..526
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019599"
FT CONFLICT 27
FT /note="L -> Q (in Ref. 2; BAC30091)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="E -> D (in Ref. 3; AAH80732)"
FT /evidence="ECO:0000305"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:2CO9"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:2CO9"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:2CO9"
FT HELIX 304..332
FT /evidence="ECO:0007829|PDB:2CO9"
SQ SEQUENCE 526 AA; 57203 MW; F6E7EE5EFCC6CC03 CRC64;
MDVRFYPPPA QPAAAPAAPC LGPSPCLDPY YCNKFDGENM YMSMTEPSQD YVPASQSYPG
PSLESEDFNI PPITPPSLPD HSLVHLNEVE SGYHSLCHPM NHNGLLPFHP QTMDLPEITV
SNMLGQDGAL LSNSISVMQE IGNAEGAQYS SHPQMAAMRP RGQPTDIRQQ ASMMQPGQLT
TINQSQLSAQ LGLNMGGTNV AHNSPSPPGS KSATPSPSSS VHEDECEDAS KINGGEKRPA
SDMGKKPKTP KKKKKKDPNE PQKPVSAYAL FFRDTQAAIK GQNPNATFGE VSKIVASMWD
GLGEEQKQVY KKKTEAAKKE YLKQLAAYRA SLVSKSYTDP VDVKTSQPPQ LVNSKPSVFH
GPSQAHSALY LSSHYHQQPG MTPQLTAMHP SLPRNIAPKP NNQMPVTVSI ANMAVSPPPP
LQISPPLHQH LSMQQHQSLA MQQPLGSQLP MQVQTALHSP TMQQGFTLQP DYQTIINPTS
TAAQVVTQAM EYVRSGCRNP PPQPVDWSTD YCSSGGMQRD KALYLT
