TOX4_HUMAN
ID TOX4_HUMAN Reviewed; 621 AA.
AC O94842; B4DPY8; B4DSM0; E7EV69;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=TOX high mobility group box family member 4 {ECO:0000305};
DE AltName: Full=Epidermal Langerhans cell protein LCP1;
GN Name=TOX4 {ECO:0000312|HGNC:HGNC:20161}; Synonyms=C14orf92, KIAA0737;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH PPP1R10/PNUTS.
RX PubMed=20516061; DOI=10.1074/jbc.m110.109801;
RA Lee J.H., You J., Dobrota E., Skalnik D.G.;
RT "Identification and characterization of a novel human PP1 phosphatase
RT complex.";
RL J. Biol. Chem. 285:24466-24476(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-313 AND SER-315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-182; SER-533;
RP SER-550; SER-552; SER-560; SER-562 AND SER-567, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-481, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [13]
RP INDUCTION BY DIABETES, AND TISSUE SPECIFICITY.
RX PubMed=34914893; DOI=10.1016/j.cmet.2021.11.013;
RA Wang L., Yu J., Zhou Q., Wang X., Mukhanova M., Du W., Sun L.,
RA Pajvani U.B., Accili D.;
RT "TOX4, an insulin receptor-independent regulator of hepatic glucose
RT production, is activated in diabetic liver.";
RL Cell Metab. 34:158-170.e5(2022).
CC -!- FUNCTION: Transcription factor that modulates cell fate reprogramming
CC from the somatic state to the pluripotent and neuronal fate (By
CC similarity). Component of the PTW/PP1 phosphatase complex, which plays
CC a role in the control of chromatin structure and cell cycle progression
CC during the transition from mitosis into interphase (PubMed:20516061).
CC In liver, controls the expression of hormone-regulated gluconeogenic
CC genes such as G6PC1 and PCK1. This regulation is independent of the
CC insulin receptor activation (By similarity).
CC {ECO:0000250|UniProtKB:Q8BU11, ECO:0000269|PubMed:20516061}.
CC -!- ACTIVITY REGULATION: In liver, recruited to target gene promoters
CC following treatment with dexamethasone and cAMP. Binding is decreased
CC in presence of insulin. {ECO:0000250|UniProtKB:Q8BU11}.
CC -!- SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of
CC PPP1R10/PNUTS, TOX4, WDR82 and PPP1CA or PPP1CB or PPP1CC. Interacts
CC with PPP1R10/PNUTS (PubMed:20516061). Interacts with FOXO1 and CREB1
CC (increased by cAMP); FOXO1 and CREB1 are required for full induction of
CC TOX4-dependent activity and the interactions are inhibited by insulin
CC (By similarity). {ECO:0000250|UniProtKB:Q8BU11,
CC ECO:0000269|PubMed:20516061}.
CC -!- INTERACTION:
CC O94842; P54253: ATXN1; NbExp=7; IntAct=EBI-948613, EBI-930964;
CC O94842; A0A0S2Z5G4: BANP; NbExp=3; IntAct=EBI-948613, EBI-16429704;
CC O94842; B4DE54: BANP; NbExp=3; IntAct=EBI-948613, EBI-16429313;
CC O94842; Q8N9N5: BANP; NbExp=3; IntAct=EBI-948613, EBI-744695;
CC O94842; Q8N9N5-2: BANP; NbExp=6; IntAct=EBI-948613, EBI-11524452;
CC O94842; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-948613, EBI-16429296;
CC O94842; Q53EP0-3: FNDC3B; NbExp=6; IntAct=EBI-948613, EBI-10242151;
CC O94842; Q8WXD5: GEMIN6; NbExp=3; IntAct=EBI-948613, EBI-752301;
CC O94842; Q01449: MYL7; NbExp=3; IntAct=EBI-948613, EBI-10222416;
CC O94842; Q2TAL8: QRICH1; NbExp=5; IntAct=EBI-948613, EBI-2798044;
CC O94842; O95947: TBX6; NbExp=7; IntAct=EBI-948613, EBI-2824328;
CC O94842; Q96E35: ZMYND19; NbExp=6; IntAct=EBI-948613, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:20516061}.
CC Note=Associated with chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O94842-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94842-2; Sequence=VSP_053873;
CC Name=3;
CC IsoId=O94842-3; Sequence=VSP_055512;
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
CC {ECO:0000269|PubMed:34914893}.
CC -!- INDUCTION: Expression is highly induced in diabetic liver.
CC {ECO:0000269|PubMed:34914893}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34457.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018280; BAA34457.2; ALT_INIT; mRNA.
DR EMBL; AK298555; BAG60750.1; -; mRNA.
DR EMBL; AK299807; BAG61682.1; -; mRNA.
DR EMBL; BC013689; AAH13689.1; -; mRNA.
DR CCDS; CCDS32043.1; -. [O94842-1]
DR RefSeq; NP_001290452.1; NM_001303523.1. [O94842-2]
DR RefSeq; NP_055643.1; NM_014828.3. [O94842-1]
DR AlphaFoldDB; O94842; -.
DR SMR; O94842; -.
DR BioGRID; 115209; 116.
DR IntAct; O94842; 68.
DR MINT; O94842; -.
DR STRING; 9606.ENSP00000477868; -.
DR GlyGen; O94842; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; O94842; -.
DR PhosphoSitePlus; O94842; -.
DR BioMuta; TOX4; -.
DR EPD; O94842; -.
DR jPOST; O94842; -.
DR MassIVE; O94842; -.
DR MaxQB; O94842; -.
DR PaxDb; O94842; -.
DR PeptideAtlas; O94842; -.
DR PRIDE; O94842; -.
DR ProteomicsDB; 4828; -.
DR ProteomicsDB; 50477; -. [O94842-1]
DR Antibodypedia; 7517; 133 antibodies from 18 providers.
DR DNASU; 9878; -.
DR Ensembl; ENST00000448790.7; ENSP00000393080.3; ENSG00000092203.15. [O94842-1]
DR Ensembl; ENST00000613569.4; ENSP00000477868.1; ENSG00000092203.15. [O94842-1]
DR GeneID; 9878; -.
DR KEGG; hsa:9878; -.
DR MANE-Select; ENST00000448790.7; ENSP00000393080.3; NM_014828.4; NP_055643.1.
DR UCSC; uc058zcl.1; human. [O94842-1]
DR CTD; 9878; -.
DR DisGeNET; 9878; -.
DR GeneCards; TOX4; -.
DR HGNC; HGNC:20161; TOX4.
DR HPA; ENSG00000092203; Low tissue specificity.
DR MIM; 614032; gene.
DR neXtProt; NX_O94842; -.
DR OpenTargets; ENSG00000092203; -.
DR PharmGKB; PA162406753; -.
DR VEuPathDB; HostDB:ENSG00000092203; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000154888; -.
DR HOGENOM; CLU_030650_0_0_1; -.
DR InParanoid; O94842; -.
DR OMA; WCSIKNQ; -.
DR OrthoDB; 1465513at2759; -.
DR PhylomeDB; O94842; -.
DR TreeFam; TF106481; -.
DR PathwayCommons; O94842; -.
DR SignaLink; O94842; -.
DR BioGRID-ORCS; 9878; 75 hits in 1109 CRISPR screens.
DR ChiTaRS; TOX4; human.
DR GeneWiki; TOX4; -.
DR GenomeRNAi; 9878; -.
DR Pharos; O94842; Tbio.
DR PRO; PR:O94842; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O94842; protein.
DR Bgee; ENSG00000092203; Expressed in colonic epithelium and 207 other tissues.
DR ExpressionAtlas; O94842; baseline and differential.
DR Genevisible; O94842; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
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 InterPro; IPR037985; TOX4.
DR PANTHER; PTHR45781:SF2; PTHR45781:SF2; 1.
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 Alternative splicing; DNA-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..621
FT /note="TOX high mobility group box family member 4"
FT /id="PRO_0000048568"
FT DNA_BIND 223..291
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 153..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 213..218
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 168..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU11"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 481
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..24
FT /note="MEFPGGNDNYLTITGPSHPFLSGA -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053873"
FT VAR_SEQ 82..107
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055512"
FT CONFLICT 271
FT /note="V -> I (in Ref. 2; BAG61682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 66195 MW; D5EEAE6FA4756CB1 CRC64;
MEFPGGNDNY LTITGPSHPF LSGAETFHTP SLGDEEFEIP PISLDSDPSL AVSDVVGHFD
DLADPSSSQD GSFSAQYGVQ TLDMPVGMTH GLMEQGGGLL SGGLTMDLDH SIGTQYSANP
PVTIDVPMTD MTSGLMGHSQ LTTIDQSELS SQLGLSLGGG TILPPAQSPE DRLSTTPSPT
SSLHEDGVED FRRQLPSQKT VVVEAGKKQK APKKRKKKDP NEPQKPVSAY ALFFRDTQAA
IKGQNPNATF GEVSKIVASM WDSLGEEQKQ VYKRKTEAAK KEYLKALAAY KDNQECQATV
ETVELDPAPP SQTPSPPPMA TVDPASPAPA SIEPPALSPS IVVNSTLSSY VANQASSGAG
GQPNITKLII TKQMLPSSIT MSQGGMVTVI PATVVTSRGL QLGQTSTATI QPSQQAQIVT
RSVLQAAAAA AAAASMQLPP PRLQPPPLQQ MPQPPTQQQV TILQQPPPLQ AMQQPPPQKV
RINLQQQPPP LQIKSVPLPT LKMQTTLVPP TVESSPERPM NNSPEAHTVE APSPETICEM
ITDVVPEVES PSQMDVELVS GSPVALSPQP RCVRSGCENP PIVSKDWDNE YCSNECVVKH
CRDVFLAWVA SRNSNTVVFV K
