TLE2_HUMAN
ID TLE2_HUMAN Reviewed; 743 AA.
AC Q04725; B4DE03; E9PEV7; F8WCH2; Q8WVY0; Q9Y6S0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Transducin-like enhancer protein 2;
DE AltName: Full=Enhancer of split groucho-like protein 2;
DE Short=ESG2;
GN Name=TLE2;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=1303260; DOI=10.1038/ng1092-119;
RA Stifani S., Blaumueller C.M., Redhead N.J., Hill R.E.,
RA Artavanis-Tsakonas S.;
RT "Human homologs of a Drosophila enhancer of split gene product define a
RT novel family of nuclear proteins.";
RL Nat. Genet. 2:119-127(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP GLY-381.
RC TISSUE=Brain, and Urinary bladder;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 OLIGOMERIZATION, AND INTERACTION WITH HES1 AND HES5.
RX PubMed=9874198; DOI=10.1046/j.1432-1327.1998.2580339.x;
RA Grbavec D., Lo R., Liu Y., Stifani S.;
RT "Transducin-like Enhancer of split 2, a mammalian homologue of Drosophila
RT Groucho, acts as a transcriptional repressor, interacts with Hairy/Enhancer
RT of split proteins, and is expressed during neuronal development.";
RL Eur. J. Biochem. 258:339-349(1998).
RN [6]
RP INTERACTION WITH UTY.
RX PubMed=9854018; DOI=10.1042/bj3370013;
RA Grbavec D., Lo R., Liu Y., Greenfield A., Stifani S.;
RT "Groucho/transducin-like enhancer of split (TLE) family members interact
RT with the yeast transcriptional co-repressor SSN6 and mammalian SSN6-related
RT proteins: implications for evolutionary conservation of transcription
RT repression mechanisms.";
RL Biochem. J. 337:13-17(1999).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND IDENTIFICATION BY
RP 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP UBIQUITINATION BY XIAP/BIRC4.
RX PubMed=22304967; DOI=10.1016/j.molcel.2011.12.032;
RA Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E.;
RT "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling.";
RL Mol. Cell 45:619-628(2012).
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). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with other family members.
CC Binds LEF1, TCF7, TCF7L1, TCF7L2, UTY, HES1 and HES5.
CC -!- INTERACTION:
CC Q04725; Q16531: DDB1; NbExp=2; IntAct=EBI-1176061, EBI-350322;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q04725-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q04725-2; Sequence=VSP_045693, VSP_045694;
CC Name=3;
CC IsoId=Q04725-3; Sequence=VSP_046162, VSP_046163, VSP_046164;
CC -!- TISSUE SPECIFICITY: In all tissues examined, mostly in heart, brain,
CC and muscle.
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. {ECO:0000269|PubMed:22304967}.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK308137; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M99436; AAA61193.1; -; mRNA.
DR EMBL; AK293407; BAG56914.1; -; mRNA.
DR EMBL; AK308137; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC007766; AAD38075.1; -; Genomic_DNA.
DR EMBL; AC011549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017364; AAH17364.1; -; mRNA.
DR CCDS; CCDS45911.1; -. [Q04725-1]
DR CCDS; CCDS45912.1; -. [Q04725-2]
DR CCDS; CCDS45913.1; -. [Q04725-3]
DR PIR; C56695; C56695.
DR RefSeq; NP_001138233.1; NM_001144761.1. [Q04725-3]
DR RefSeq; NP_001138234.1; NM_001144762.1. [Q04725-2]
DR RefSeq; NP_001287775.1; NM_001300846.1.
DR RefSeq; NP_003251.2; NM_003260.4. [Q04725-1]
DR AlphaFoldDB; Q04725; -.
DR SMR; Q04725; -.
DR BioGRID; 112944; 49.
DR CORUM; Q04725; -.
DR IntAct; Q04725; 25.
DR MINT; Q04725; -.
DR STRING; 9606.ENSP00000466542; -.
DR GlyGen; Q04725; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q04725; -.
DR PhosphoSitePlus; Q04725; -.
DR BioMuta; TLE2; -.
DR DMDM; 20532416; -.
DR EPD; Q04725; -.
DR jPOST; Q04725; -.
DR MassIVE; Q04725; -.
DR MaxQB; Q04725; -.
DR PaxDb; Q04725; -.
DR PeptideAtlas; Q04725; -.
DR PRIDE; Q04725; -.
DR ProteomicsDB; 19967; -.
DR ProteomicsDB; 31151; -.
DR ProteomicsDB; 58267; -. [Q04725-1]
DR Antibodypedia; 23107; 210 antibodies from 31 providers.
DR DNASU; 7089; -.
DR Ensembl; ENST00000262953.11; ENSP00000262953.5; ENSG00000065717.15. [Q04725-1]
DR Ensembl; ENST00000426948.6; ENSP00000392869.2; ENSG00000065717.15. [Q04725-3]
DR Ensembl; ENST00000443826.7; ENSP00000392427.2; ENSG00000065717.15. [Q04725-2]
DR Ensembl; ENST00000455444.6; ENSP00000413107.2; ENSG00000065717.15. [Q04725-2]
DR Ensembl; ENST00000591529.5; ENSP00000468279.1; ENSG00000065717.15. [Q04725-3]
DR GeneID; 7089; -.
DR KEGG; hsa:7089; -.
DR MANE-Select; ENST00000262953.11; ENSP00000262953.5; NM_003260.5; NP_003251.2.
DR UCSC; uc002lww.3; human. [Q04725-1]
DR CTD; 7089; -.
DR DisGeNET; 7089; -.
DR GeneCards; TLE2; -.
DR HGNC; HGNC:11838; TLE2.
DR HPA; ENSG00000065717; Low tissue specificity.
DR MIM; 601041; gene.
DR neXtProt; NX_Q04725; -.
DR OpenTargets; ENSG00000065717; -.
DR PharmGKB; PA36540; -.
DR VEuPathDB; HostDB:ENSG00000065717; -.
DR eggNOG; KOG0639; Eukaryota.
DR GeneTree; ENSGT01030000234519; -.
DR HOGENOM; CLU_007612_3_0_1; -.
DR InParanoid; Q04725; -.
DR OrthoDB; 546143at2759; -.
DR PhylomeDB; Q04725; -.
DR TreeFam; TF314167; -.
DR PathwayCommons; Q04725; -.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-4641265; Repression of WNT target genes.
DR SignaLink; Q04725; -.
DR SIGNOR; Q04725; -.
DR BioGRID-ORCS; 7089; 28 hits in 1083 CRISPR screens.
DR ChiTaRS; TLE2; human.
DR GeneWiki; TLE2; -.
DR GenomeRNAi; 7089; -.
DR Pharos; Q04725; Tbio.
DR PRO; PR:Q04725; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q04725; protein.
DR Bgee; ENSG00000065717; Expressed in cerebellar hemisphere and 202 other tissues.
DR ExpressionAtlas; Q04725; baseline and differential.
DR Genevisible; Q04725; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; 3.
DR PRINTS; PR01850; GROUCHOFAMLY.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation;
KW WD repeat; Wnt signaling pathway.
FT CHAIN 1..743
FT /note="Transducin-like enhancer protein 2"
FT /id="PRO_0000051278"
FT REPEAT 455..493
FT /note="WD 1"
FT REPEAT 501..540
FT /note="WD 2"
FT REPEAT 545..584
FT /note="WD 3"
FT REPEAT 587..626
FT /note="WD 4"
FT REPEAT 669..708
FT /note="WD 5"
FT REPEAT 710..742
FT /note="WD 6"
FT REGION 1..127
FT /note="Q domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 128..191
FT /note="GP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 179..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..254
FT /note="CcN domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 239..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..423
FT /note="SP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 296..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 214..217
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 214..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 228
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 249
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 253
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045693"
FT VAR_SEQ 1..8
FT /note="MYPQGRHP -> MVQSRLTATSASQDSPASGLQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046162"
FT VAR_SEQ 124..190
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045694"
FT VAR_SEQ 124
FT /note="Q -> QQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046163"
FT VAR_SEQ 683..743
FT /note="GRWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISRNNKYIVTGSGDK
FT KATVYEVVY -> VQGVVLSPEL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046164"
FT VARIANT 381
FT /note="S -> G (in dbSNP:rs199788562)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_069063"
FT CONFLICT 280
FT /note="G -> R (in Ref. 1; AAA61193)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="A -> L (in Ref. 1; AAA61193)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="G -> D (in Ref. 1; AAA61193)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="A -> R (in Ref. 1; AAA61193)"
FT /evidence="ECO:0000305"
FT CONFLICT 636..637
FT /note="LG -> PC (in Ref. 1; AAA61193)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="R -> G (in Ref. 1; AAA61193)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="S -> P (in Ref. 1; AAA61193)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 743 AA; 79841 MW; 5E3DBFAB67278219 CRC64;
MYPQGRHPTP LQSGQPFKFS ILEICDRIKE EFQFLQAQYH SLKLECEKLA SEKTEMQRHY
VMYYEMSYGL NIEMHKQAEI VKRLSGICAQ IIPFLTQEHQ QQVLQAVERA KQVTVGELNS
LIGQQLQPLS HHAPPVPLTP RPAGLVGGSA TGLLALSGAL AAQAQLAAAV KEDRAGVEAE
GSRVERAPSR SASPSPPESL VEEERPSGPG GGGKQRADEK EPSGPYESDE DKSDYNLVVD
EDQPSEPPSP ATTPCGKVPI CIPARRDLVD SPASLASSLG SPLPRAKELI LNDLPASTPA
SKSCDSSPPQ DASTPGPSSA SHLCQLAAKP APSTDSVALR SPLTLSSPFT TSFSLGSHST
LNGDLSVPSS YVSLHLSPQV SSSVVYGRSP VMAFESHPHL RGSSVSSSLP SIPGGKPAYS
FHVSADGQMQ PVPFPSDALV GAGIPRHARQ LHTLAHGEVV CAVTISGSTQ HVYTGGKGCV
KVWDVGQPGA KTPVAQLDCL NRDNYIRSCK LLPDGRSLIV GGEASTLSIW DLAAPTPRIK
AELTSSAPAC YALAVSPDAK VCFSCCSDGN IVVWDLQNQT MVRQFQGHTD GASCIDISDY
GTRLWTGGLD NTVRCWDLRE GRQLQQHDFS SQIFSLGHCP NQDWLAVGME SSNVEILHVR
KPEKYQLHLH ESCVLSLKFA SCGRWFVSTG KDNLLNAWRT PYGASIFQSK ESSSVLSCDI
SRNNKYIVTG SGDKKATVYE VVY
