TLE3_MOUSE
ID TLE3_MOUSE Reviewed; 772 AA.
AC Q08122; Q6PHP0; Q923A4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Transducin-like enhancer protein 3;
DE AltName: Full=ESG;
DE AltName: Full=Grg-3;
GN Name=Tle3; Synonyms=Esg;
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), AND TISSUE SPECIFICITY.
RC STRAIN=CD-1;
RX PubMed=8365415; DOI=10.1111/j.1432-1033.1993.tb18151.x;
RA Miyasaka H., Choudhury B.K., Hou E.W., Li S.S.-L.;
RT "Molecular cloning and expression of mouse and human cDNA encoding AES and
RT ESG proteins with strong similarity to Drosophila enhancer of split groucho
RT protein.";
RL Eur. J. Biochem. 216:343-352(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORM 3).
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 MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 324-772 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-772 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=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 [5]
RP INTERACTION WITH LEF1; TCF7; TCF7L1 AND TCF7L2.
RX PubMed=11266540; DOI=10.1093/nar/29.7.1410;
RA Brantjes H., Roose J., van De Wetering M., Clevers H.;
RT "All Tcf HMG box transcription factors interact with Groucho-related co-
RT repressors.";
RL Nucleic Acids Res. 29:1410-1419(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP INTERACTION WITH TBX18.
RX PubMed=17584735; DOI=10.1074/jbc.m703724200;
RA Farin H.F., Bussen M., Schmidt M.K., Singh M.K., Schuster-Gossler K.,
RA Kispert A.;
RT "Transcriptional repression by the T-box proteins Tbx18 and Tbx15 depends
RT on Groucho corepressors.";
RL J. Biol. Chem. 282:25748-25759(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP REVIEW.
RX PubMed=18254933; DOI=10.1186/gb-2008-9-1-205;
RA Jennings B.H., Ish-Horowicz D.;
RT "The Groucho/TLE/Grg family of transcriptional co-repressors.";
RL Genome Biol. 9:R205.1-R205.7(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-259; SER-263;
RP SER-267; SER-286; THR-328 AND THR-334, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=23990468; DOI=10.1074/jbc.m113.461848;
RA Kogawa M., Hisatake K., Atkins G.J., Findlay D.M., Enoki Y., Sato T.,
RA Gray P.C., Kanesaki-Yatsuka Y., Anderson P.H., Wada S., Kato N., Fukuda A.,
RA Katayama S., Tsujimoto M., Yoda T., Suda T., Okazaki Y., Matsumoto M.;
RT "The paired-box homeodomain transcription factor Pax6 binds to the upstream
RT region of the TRAP gene promoter and suppresses receptor activator of NF-
RT kappaB ligand (RANKL)-induced osteoclast differentiation.";
RL J. Biol. Chem. 288:31299-31312(2013).
CC -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC transcription factors. Inhibits the transcriptional activation mediated
CC by CTNNB1 and TCF family members in Wnt signaling. The effects of full-
CC length TLE family members may be modulated by association with
CC dominant-negative AES (By similarity). May play an important role
CC during spermatogenesis. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer and heterooligomer with other family members.
CC Binds FOXA2 (By similarity). Interacts with XIAP/BIRC4 (By similarity).
CC Binds LEF1, TCF7, TCF7L1 and TCF7L2/TCF4. Interacts with TBX18 (via
CC engrailed homology 1 repressor motif), leading to decreased of TBX18
CC transcriptional activity. {ECO:0000250, ECO:0000269|PubMed:11266540,
CC ECO:0000269|PubMed:17584735}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3;
CC IsoId=Q08122-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q08122-1; Sequence=VSP_038441;
CC Name=2;
CC IsoId=Q08122-2; Sequence=VSP_007025;
CC Name=4;
CC IsoId=Q08122-4; Sequence=VSP_038442;
CC -!- TISSUE SPECIFICITY: Expressed only in testis (PubMed:8365415).
CC Expressed in bone marrow-derived macrophages (PubMed:23990468).
CC {ECO:0000269|PubMed:23990468, ECO:0000269|PubMed:8365415}.
CC -!- INDUCTION: Repressed during TNFSF11/RANKL-induced osteoclast
CC differentiation. {ECO:0000269|PubMed:23990468}.
CC -!- DOMAIN: WD repeat Groucho/TLE family members are characterized by 5
CC regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a
CC central CcN domain, containing a nuclear localization signal, and a
CC serine/proline-rich SP domain. The most highly conserved are the N-
CC terminal Q domain and the C-terminal WD-repeat domain.
CC {ECO:0000305|PubMed:18254933}.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. This ubiquitination does not affect
CC its stability, nuclear localization, or capacity to tetramerize but
CC inhibits its interaction with TCF7L2/TCF4.
CC {ECO:0000250|UniProtKB:Q04726}.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
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DR EMBL; X73360; CAA51770.1; -; mRNA.
DR EMBL; AC126672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006672; AAH06672.1; -; mRNA.
DR EMBL; BC056465; AAH56465.1; -; mRNA.
DR EMBL; AK031322; BAC27347.1; -; mRNA.
DR CCDS; CCDS52825.1; -. [Q08122-3]
DR CCDS; CCDS52826.1; -. [Q08122-4]
DR PIR; S35681; S35681.
DR RefSeq; NP_001077396.1; NM_001083927.1. [Q08122-4]
DR RefSeq; NP_033415.2; NM_009389.2. [Q08122-3]
DR RefSeq; XP_006511091.1; XM_006511028.3. [Q08122-2]
DR AlphaFoldDB; Q08122; -.
DR SMR; Q08122; -.
DR BioGRID; 204218; 3.
DR CORUM; Q08122; -.
DR STRING; 10090.ENSMUSP00000124131; -.
DR iPTMnet; Q08122; -.
DR PhosphoSitePlus; Q08122; -.
DR EPD; Q08122; -.
DR jPOST; Q08122; -.
DR MaxQB; Q08122; -.
DR PaxDb; Q08122; -.
DR PRIDE; Q08122; -.
DR ProteomicsDB; 260661; -. [Q08122-3]
DR ProteomicsDB; 260662; -. [Q08122-1]
DR ProteomicsDB; 260663; -. [Q08122-2]
DR ProteomicsDB; 260664; -. [Q08122-4]
DR Antibodypedia; 7320; 101 antibodies from 27 providers.
DR DNASU; 21887; -.
DR Ensembl; ENSMUST00000160882; ENSMUSP00000124131; ENSMUSG00000032280. [Q08122-4]
DR Ensembl; ENSMUST00000162583; ENSMUSP00000124977; ENSMUSG00000032280. [Q08122-2]
DR Ensembl; ENSMUST00000162973; ENSMUSP00000124173; ENSMUSG00000032280. [Q08122-3]
DR GeneID; 21887; -.
DR KEGG; mmu:21887; -.
DR UCSC; uc009pzo.1; mouse. [Q08122-4]
DR UCSC; uc009pzp.1; mouse. [Q08122-3]
DR CTD; 7090; -.
DR MGI; MGI:104634; Tle3.
DR VEuPathDB; HostDB:ENSMUSG00000032280; -.
DR eggNOG; KOG0639; Eukaryota.
DR GeneTree; ENSGT01030000234519; -.
DR InParanoid; Q08122; -.
DR OrthoDB; 546143at2759; -.
DR TreeFam; TF314167; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-MMU-4641265; Repression of WNT target genes.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 21887; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Tle3; mouse.
DR PRO; PR:Q08122; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q08122; protein.
DR Bgee; ENSMUSG00000032280; Expressed in undifferentiated genital tubercle and 294 other tissues.
DR ExpressionAtlas; Q08122; baseline and differential.
DR Genevisible; Q08122; MM.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR005617; Groucho/TLE_N.
DR InterPro; IPR009146; Groucho_enhance.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10814; PTHR10814; 1.
DR Pfam; PF03920; TLE_N; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR01850; GROUCHOFAMLY.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Developmental protein; Differentiation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Spermatogenesis; Transcription; Transcription regulation; Ubl conjugation;
KW WD repeat; Wnt signaling pathway.
FT CHAIN 1..772
FT /note="Transducin-like enhancer protein 3"
FT /id="PRO_0000051281"
FT REPEAT 484..522
FT /note="WD 1"
FT REPEAT 530..569
FT /note="WD 2"
FT REPEAT 574..613
FT /note="WD 3"
FT REPEAT 616..655
FT /note="WD 4"
FT REPEAT 657..696
FT /note="WD 5"
FT REPEAT 698..737
FT /note="WD 6"
FT REPEAT 739..771
FT /note="WD 7"
FT REGION 1..131
FT /note="Q domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 130..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..199
FT /note="GP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 184..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..268
FT /note="CcN domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 269..452
FT /note="SP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT MOTIF 225..228
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 141..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 275
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q04727"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 319
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 321
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04726"
FT VAR_SEQ 2..8
FT /note="YPQGRHP -> CPCGLQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8365415"
FT /id="VSP_038441"
FT VAR_SEQ 124
FT /note="G -> GVRGLPNLPLT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038442"
FT VAR_SEQ 351..353
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007025"
FT CONFLICT 545
FT /note="R -> G (in Ref. 1; CAA51770)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="W -> R (in Ref. 4; BAC27347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 83447 MW; 39735F2718A8D27A CRC64;
MYPQGRHPAP HQPGQPGFKF TVAESCDRIK DEFQFLQAQY HSLKVEYDKL ANEKTEMQRH
YVMYYEMSYG LNIEMHKQTE IAKRLNTILA QIMPFLSQEH QQQVAQAVER AKQVTMTELN
AIIGQQQLQA QHLSHATHGP PVQLPPHPSG LQPPGIPPVT GSSSGLLALG ALGSQAHLAV
KDEKNHHELD HRERESSTNN SVSPSESLRA SEKHRGSADY SMEAKKRKAE EKDSLSRYDS
DGDKSDDLVV DVSNEDPATP RVSPAHSPPE NGLDKARGLK KDAPTSPASV ASSSSTPSSK
TKDLGHNDKS STPGLKSNTP TPRNDAPTPG TSTTPGLRSM PGKPPGMDPI GIMASALRTP
ITLTSSYPAP FAMMSHHEMN GSLTSPSAYA GLHNIPSQMS AAAAAAAAAY GRSPMVSFGA
VGFDPHPPMR ATGLPSSLAS IPGGKPAYSF HVSADGQMQP VPFPHDALAG PGIPRHARQI
NTLSHGEVVC AVTISNPTRH VYTGGKGCVK IWDISQPGSK SPISQLDCLN RDNYIRSCKL
LPDGRTLIVG GEASTLTIWD LASPTPRIKA ELTSSAPACY ALAISPDAKV CFSCCSDGNI
AVWDLHNQTL VRQFQGHTDG ASCIDISHDG TKLWTGGLDN TVRSWDLREG RQLQQHDFTS
QIFSLGYCPT GEWLAVGMES SNVEVLHHTK PDKYQLHLHE SCVLSLKFAY CGKWFVSTGK
DNLLNAWRTP YGASIFQSKE SSSVLSCDIS ADDKYIVTGS GDKKATVYEV IY
