TBL1R_MOUSE
ID TBL1R_MOUSE Reviewed; 514 AA.
AC Q8BHJ5; Q3UWL6; Q8CBG4; Q8VEG3; Q9EQD4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=F-box-like/WD repeat-containing protein TBL1XR1;
DE AltName: Full=Nuclear receptor corepressor/HDAC3 complex subunit TBLR1;
DE AltName: Full=TBL1-related protein 1;
DE AltName: Full=Transducin beta-like 1X-related protein 1;
GN Name=Tbl1xr1; Synonyms=Ira1, Tblr1;
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].
RC STRAIN=BALB/cJ;
RX PubMed=11063877; DOI=10.1016/s0301-472x(00)00539-7;
RA Zhang X., Dormady S.P., Basch R.S.;
RT "Identification of four human cDNAs that are differentially expressed by
RT early hematopoietic progenitors.";
RL Exp. Hematol. 28:1286-1296(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Egg, 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] OF 314-514.
RC TISSUE=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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, 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).
RN [6] {ECO:0007744|PDB:5NAF}
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 134-514 IN COMPLEX WITH MECP2,
RP AND MUTAGENESIS OF GLU-171; CYS-214; ASP-313; GLU-351; ASP-369; PRO-444 AND
RP TYR-446.
RX PubMed=28348241; DOI=10.1073/pnas.1700731114;
RA Kruusvee V., Lyst M.J., Taylor C., Tarnauskaite Z., Bird A.P., Cook A.G.;
RT "Structure of the MeCP2-TBLR1 complex reveals a molecular basis for Rett
RT syndrome and related disorders.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E3243-E3250(2017).
CC -!- FUNCTION: F-box-like protein involved in the recruitment of the
CC ubiquitin/19S proteasome complex to nuclear receptor-regulated
CC transcription units. Plays an essential role in transcription
CC activation mediated by nuclear receptors. Probably acts as integral
CC component of the N-Cor corepressor complex that mediates the
CC recruitment of the 19S proteasome complex, leading to the subsequent
CC proteasomal degradation of N-Cor complex, thereby allowing cofactor
CC exchange, and transcription activation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the N-Cor repressor complex, at least composed of
CC NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Probable
CC component of some E3 ubiquitin ligase complex. Interacts with histones
CC H2B and H4 (By similarity). Interacts with MECP2; bridges interaction
CC between MECP2 and NCOR1 (PubMed:28348241).
CC {ECO:0000250|UniProtKB:Q9BZK7, ECO:0000269|PubMed:28348241}.
CC -!- INTERACTION:
CC Q8BHJ5; P51608: MECP2; Xeno; NbExp=4; IntAct=EBI-1216384, EBI-1189067;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The F-box-like domain is related to the F-box domain, and
CC apparently displays the same function as component of ubiquitin E3
CC ligase complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat EBI family. {ECO:0000305}.
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DR EMBL; AF268195; AAG44738.1; -; mRNA.
DR EMBL; AK029595; BAC26526.1; -; mRNA.
DR EMBL; AK033347; BAC28241.1; -; mRNA.
DR EMBL; AK036064; BAC29294.1; -; mRNA.
DR EMBL; AK136255; BAE22898.1; -; mRNA.
DR EMBL; BC018512; AAH18512.1; -; mRNA.
DR CCDS; CCDS17266.1; -.
DR RefSeq; NP_109657.2; NM_030732.3.
DR RefSeq; XP_006535642.1; XM_006535579.3.
DR RefSeq; XP_006535643.1; XM_006535580.3.
DR RefSeq; XP_011248020.1; XM_011249718.2.
DR RefSeq; XP_011248021.1; XM_011249719.2.
DR RefSeq; XP_011248023.1; XM_011249721.2.
DR RefSeq; XP_017175306.1; XM_017319817.1.
DR PDB; 5NAF; X-ray; 2.49 A; A/B/C/D=134-514.
DR PDBsum; 5NAF; -.
DR AlphaFoldDB; Q8BHJ5; -.
DR SMR; Q8BHJ5; -.
DR BioGRID; 219863; 6.
DR DIP; DIP-38606N; -.
DR IntAct; Q8BHJ5; 7.
DR MINT; Q8BHJ5; -.
DR STRING; 10090.ENSMUSP00000067164; -.
DR iPTMnet; Q8BHJ5; -.
DR PhosphoSitePlus; Q8BHJ5; -.
DR EPD; Q8BHJ5; -.
DR MaxQB; Q8BHJ5; -.
DR PaxDb; Q8BHJ5; -.
DR PeptideAtlas; Q8BHJ5; -.
DR PRIDE; Q8BHJ5; -.
DR ProteomicsDB; 263011; -.
DR Antibodypedia; 9317; 368 antibodies from 33 providers.
DR DNASU; 81004; -.
DR Ensembl; ENSMUST00000063988; ENSMUSP00000067164; ENSMUSG00000027630.
DR Ensembl; ENSMUST00000192328; ENSMUSP00000141363; ENSMUSG00000027630.
DR Ensembl; ENSMUST00000193734; ENSMUSP00000142184; ENSMUSG00000027630.
DR Ensembl; ENSMUST00000202747; ENSMUSP00000144436; ENSMUSG00000027630.
DR GeneID; 81004; -.
DR KEGG; mmu:81004; -.
DR UCSC; uc008osw.1; mouse.
DR CTD; 79718; -.
DR MGI; MGI:2441730; Tbl1xr1.
DR VEuPathDB; HostDB:ENSMUSG00000027630; -.
DR eggNOG; KOG0273; Eukaryota.
DR GeneTree; ENSGT00940000153421; -.
DR HOGENOM; CLU_007609_2_0_1; -.
DR InParanoid; Q8BHJ5; -.
DR OMA; YVASGCF; -.
DR OrthoDB; 1463197at2759; -.
DR PhylomeDB; Q8BHJ5; -.
DR TreeFam; TF323190; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 81004; 4 hits in 79 CRISPR screens.
DR ChiTaRS; Tbl1xr1; mouse.
DR PRO; PR:Q8BHJ5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BHJ5; protein.
DR Bgee; ENSMUSG00000027630; Expressed in metanephric mesenchyme and 256 other tissues.
DR ExpressionAtlas; Q8BHJ5; baseline and differential.
DR Genevisible; Q8BHJ5; MM.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:MGI.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0060613; P:fat pad development; IMP:MGI.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; IMP:MGI.
DR GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR GO; GO:0050872; P:white fat cell differentiation; IMP:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045183; Ebi-like.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
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; PTHR22846; PTHR22846; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Chromatin regulator; Isopeptide bond;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Ubl conjugation pathway;
KW WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BZK7"
FT CHAIN 2..514
FT /note="F-box-like/WD repeat-containing protein TBL1XR1"
FT /id="PRO_0000051267"
FT DOMAIN 4..36
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 41..86
FT /note="F-box-like"
FT REPEAT 167..206
FT /note="WD 1"
FT REPEAT 223..262
FT /note="WD 2"
FT REPEAT 264..303
FT /note="WD 3"
FT REPEAT 306..344
FT /note="WD 4"
FT REPEAT 347..386
FT /note="WD 5"
FT REPEAT 389..437
FT /note="WD 6"
FT REPEAT 440..479
FT /note="WD 7"
FT REPEAT 481..513
FT /note="WD 8"
FT REGION 114..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZK7"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BZK7"
FT MUTAGEN 171
FT /note="E->A: Significantly decreases interaction with
FT MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT MUTAGEN 171
FT /note="E->Q: Significantly decreases interaction with
FT MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT MUTAGEN 214
FT /note="C->S: Does not affect interaction with MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT MUTAGEN 313
FT /note="D->N: Abolishes interaction with MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT MUTAGEN 351
FT /note="E->A: Weakly decreases interaction with MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT MUTAGEN 351
FT /note="E->D: Does not affect interaction with MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT MUTAGEN 369
FT /note="D->A: Abolishes interaction with MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT MUTAGEN 369
FT /note="D->E: Substantially reduces interaction with MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT MUTAGEN 444
FT /note="P->R: Mildly affects interaction with MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT MUTAGEN 446
FT /note="Y->F: Does not affect interaction with MECP2."
FT /evidence="ECO:0000269|PubMed:28348241"
FT CONFLICT 185
FT /note="A -> V (in Ref. 1; AAG44738)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="K -> R (in Ref. 2; BAC29294)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="Y -> C (in Ref. 3; AAH18512)"
FT /evidence="ECO:0000305"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5NAF"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 311..326
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:5NAF"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 454..461
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:5NAF"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 493..502
FT /evidence="ECO:0007829|PDB:5NAF"
FT STRAND 507..511
FT /evidence="ECO:0007829|PDB:5NAF"
SQ SEQUENCE 514 AA; 55661 MW; 13BEC1C2C7F8BF14 CRC64;
MSISSDEVNF LVYRYLQESG FSHSAFTFGI ESHISQSNIN GALVPPAALI SIIQKGLQYV
EAEVSINEDG TLFDGRPIES LSLIDAVMPD VVQTRQQAYR DKLAQQHAAA AAAAAAATNQ
QGSAKNGENT ANGEENGAHT IANNHTDMME VDGDVEIPSN KAVVLRGHES EVFICAWNPV
SDLLASGSGD STARIWNLSE NSTSGPTQLV LRHCIREGGQ DVPSNKDVTS LDWNSEGTLL
ATGSYDGFAR IWTKDGNLAS TLGQHKGPIF ALKWNKKGNF ILSAGVDKTT IIWDAHTGEA
KQQFPFHSAP ALDVDWQSNN TFASCSTDMC IHVCKLGQDR PIKTFQGHTN EVNAIKWDPT
GNLLASCSDD MTLKIWSMKQ DNCVHDLQAH NKEIYTIKWS PTGPGTNNPN ANLMLASASF
DSTVRLWDVD RGICIHTLTK HQEPVYSVAF SPDGRYLASG SFDKCVHIWN TQTGALVHSY
RGTGGIFEVC WNAAGDKVGA SASDGSVCVL DLRK
