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 24-JAN-2024, entry version 183. 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}; 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; 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; 139. DR IntAct; O94842; 71. DR MINT; O94842; -. DR STRING; 9606.ENSP00000477868; -. DR GlyCosmos; O94842; 6 sites, 2 glycans. DR GlyGen; O94842; 12 sites, 2 O-linked glycans (12 sites). DR iPTMnet; O94842; -. DR PhosphoSitePlus; O94842; -. DR SwissPalm; O94842; -. DR BioMuta; TOX4; -. DR EPD; O94842; -. DR jPOST; O94842; -. DR MassIVE; O94842; -. DR MaxQB; O94842; -. DR PaxDb; 9606-ENSP00000477868; -. DR PeptideAtlas; O94842; -. DR ProteomicsDB; 4828; -. DR ProteomicsDB; 50477; -. [O94842-1] DR Pumba; O94842; -. DR Antibodypedia; 7517; 144 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 AGR; HGNC:20161; -. 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; AVDSEDW; -. DR OrthoDB; 4252846at2759; -. DR PhylomeDB; O94842; -. DR TreeFam; TF106481; -. DR PathwayCommons; O94842; -. DR SignaLink; O94842; -. DR BioGRID-ORCS; 9878; 79 hits in 1188 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 209 other cell types or tissues. DR ExpressionAtlas; O94842; baseline and differential. 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 CDD; cd21995; HMG-box_TOX-like; 1. DR Gene3D; 1.10.30.10; High mobility group box domain; 1. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR PANTHER; PTHR45781; AGAP000281-PA; 1. DR PANTHER; PTHR45781:SF2; TOX HIGH MOBILITY GROUP BOX FAMILY MEMBER 4; 1. DR Pfam; PF00505; HMG_box; 1. DR PRINTS; PR00886; HIGHMOBLTY12. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF47095; HMG-box; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. DR Genevisible; O94842; HS. 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 //