ETS2_HUMAN
ID ETS2_HUMAN Reviewed; 469 AA.
AC P15036; A6NM68; D3DSH6; Q53Y89;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Protein C-ets-2;
GN Name=ETS2;
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].
RX PubMed=2847145; DOI=10.1073/pnas.85.21.7862;
RA Watson D.K., McWilliams M.J., Lapis P., Lautenberger J.A.,
RA Schweinfest C.W., Papas T.S.;
RT "Mammalian ets-1 and ets-2 genes encode highly conserved proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7862-7866(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zimmermann W.W.K., Korenberg J., Rosenthal A., Schattevoy R.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Colon;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-469.
RX PubMed=2250910;
RA Watson D.K., Mavrothalassitis G.J., Jorcyk C.L., Smyth F.E., Papas T.S.;
RT "Molecular organization and differential polyadenylation sites of the human
RT ETS2 gene.";
RL Oncogene 5:1521-1527(1990).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 324-469.
RX PubMed=2997781; DOI=10.1073/pnas.82.21.7294;
RA Watson D.K., McWilliams-Smith M.J., Nunn M.F., Duesberg P.H., O'Brien S.J.,
RA Papas T.S.;
RT "The ets sequence from the transforming gene of avian erythroblastosis
RT virus, E26, has unique domains on human chromosomes 11 and 21: both loci
RT are transcriptionally active.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7294-7298(1985).
RN [10]
RP FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR.
RX PubMed=11909962; DOI=10.1128/mcb.22.8.2687-2702.2002;
RA Wasylyk C., Schlumberger S.E., Criqui-Filipe P., Wasylyk B.;
RT "Sp100 interacts with ETS-1 and stimulates its transcriptional activity.";
RL Mol. Cell. Biol. 22:2687-2702(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION AT SER-220 AND SER-225.
RX PubMed=24218572; DOI=10.1073/pnas.1306814110;
RA Guen V.J., Gamble C., Flajolet M., Unger S., Thollet A., Ferandin Y.,
RA Superti-Furga A., Cohen P.A., Meijer L., Colas P.;
RT "CDK10/cyclin M is a protein kinase that controls ETS2 degradation and is
RT deficient in STAR syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19525-19530(2013).
CC -!- FUNCTION: Transcription factor activating transcription. Binds
CC specifically the DNA GGAA/T core motif (Ets-binding site or EBS) in
CC gene promoters and stimulates transcription.
CC {ECO:0000269|PubMed:11909962}.
CC -!- INTERACTION:
CC P15036; Q15131: CDK10; NbExp=2; IntAct=EBI-1646991, EBI-1646959;
CC P15036; Q8NHY2: COP1; NbExp=2; IntAct=EBI-1646991, EBI-1176214;
CC P15036; Q16236: NFE2L2; NbExp=2; IntAct=EBI-1646991, EBI-2007911;
CC P15036; P17612: PRKACA; NbExp=3; IntAct=EBI-1646991, EBI-476586;
CC P15036; P50454: SERPINH1; NbExp=3; IntAct=EBI-1646991, EBI-350723;
CC P15036; P37173: TGFBR2; NbExp=3; IntAct=EBI-1646991, EBI-296151;
CC P15036; P04637: TP53; NbExp=4; IntAct=EBI-1646991, EBI-366083;
CC P15036; Q15672: TWIST1; NbExp=2; IntAct=EBI-1646991, EBI-1797287;
CC P15036; Q8WVJ9: TWIST2; NbExp=2; IntAct=EBI-1646991, EBI-1797313;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylation by CDK10 at Ser-220 and Ser-225 creates a
CC phosphodegron that targets ETS2 for proteasomal degradation.
CC {ECO:0000269|PubMed:24218572}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ETS2ID40503ch21q22.html";
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DR EMBL; J04102; AAA52412.1; -; mRNA.
DR EMBL; AF017257; AAB94057.1; -; Genomic_DNA.
DR EMBL; AK315563; BAG37939.1; -; mRNA.
DR EMBL; BT006838; AAP35484.1; -; mRNA.
DR EMBL; AL163278; CAB90468.1; -; Genomic_DNA.
DR EMBL; AP001732; BAA95514.1; -; Genomic_DNA.
DR EMBL; AP001040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09673.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09674.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09676.1; -; Genomic_DNA.
DR EMBL; BC017040; AAH17040.1; -; mRNA.
DR EMBL; BC042954; AAH42954.1; -; mRNA.
DR EMBL; X55181; CAA38966.1; -; Genomic_DNA.
DR EMBL; M11922; AAA52411.1; -; mRNA.
DR CCDS; CCDS13659.1; -.
DR PIR; B32066; TVHUE2.
DR RefSeq; NP_005230.1; NM_005239.5.
DR RefSeq; XP_005260992.1; XM_005260935.1.
DR RefSeq; XP_016883779.1; XM_017028290.1.
DR PDB; 4BQA; X-ray; 2.50 A; A/D/G=325-464.
DR PDB; 4MHV; X-ray; 2.45 A; A/B=76-170.
DR PDBsum; 4BQA; -.
DR PDBsum; 4MHV; -.
DR AlphaFoldDB; P15036; -.
DR SMR; P15036; -.
DR BioGRID; 108415; 33.
DR CORUM; P15036; -.
DR DIP; DIP-40452N; -.
DR IntAct; P15036; 26.
DR MINT; P15036; -.
DR STRING; 9606.ENSP00000353344; -.
DR iPTMnet; P15036; -.
DR PhosphoSitePlus; P15036; -.
DR BioMuta; ETS2; -.
DR DMDM; 119645; -.
DR EPD; P15036; -.
DR jPOST; P15036; -.
DR MassIVE; P15036; -.
DR MaxQB; P15036; -.
DR PaxDb; P15036; -.
DR PeptideAtlas; P15036; -.
DR PRIDE; P15036; -.
DR ProteomicsDB; 53101; -.
DR Antibodypedia; 8721; 416 antibodies from 32 providers.
DR DNASU; 2114; -.
DR Ensembl; ENST00000360214.8; ENSP00000353344.3; ENSG00000157557.13.
DR Ensembl; ENST00000360938.8; ENSP00000354194.3; ENSG00000157557.13.
DR Ensembl; ENST00000653642.1; ENSP00000499315.1; ENSG00000157557.13.
DR Ensembl; ENST00000662305.1; ENSP00000499226.1; ENSG00000157557.13.
DR Ensembl; ENST00000666778.1; ENSP00000499775.1; ENSG00000157557.13.
DR GeneID; 2114; -.
DR KEGG; hsa:2114; -.
DR MANE-Select; ENST00000360938.8; ENSP00000354194.3; NM_005239.6; NP_005230.1.
DR UCSC; uc002yxf.4; human.
DR CTD; 2114; -.
DR DisGeNET; 2114; -.
DR GeneCards; ETS2; -.
DR HGNC; HGNC:3489; ETS2.
DR HPA; ENSG00000157557; Low tissue specificity.
DR MIM; 164740; gene.
DR neXtProt; NX_P15036; -.
DR OpenTargets; ENSG00000157557; -.
DR PharmGKB; PA27903; -.
DR VEuPathDB; HostDB:ENSG00000157557; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000160202; -.
DR HOGENOM; CLU_031197_1_1_1; -.
DR InParanoid; P15036; -.
DR OMA; RSWNSQS; -.
DR OrthoDB; 526256at2759; -.
DR PhylomeDB; P15036; -.
DR TreeFam; TF316214; -.
DR PathwayCommons; P15036; -.
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR SignaLink; P15036; -.
DR SIGNOR; P15036; -.
DR BioGRID-ORCS; 2114; 23 hits in 1103 CRISPR screens.
DR ChiTaRS; ETS2; human.
DR GeneWiki; ETS2; -.
DR GenomeRNAi; 2114; -.
DR Pharos; P15036; Tbio.
DR PRO; PR:P15036; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P15036; protein.
DR Bgee; ENSG00000157557; Expressed in skin of abdomen and 201 other tissues.
DR ExpressionAtlas; P15036; baseline and differential.
DR Genevisible; P15036; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001712; P:ectodermal cell fate commitment; IEA:Ensembl.
DR GO; GO:0007498; P:mesoderm development; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0090009; P:primitive streak formation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR045688; Ets1_N_flank.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR003118; Pointed_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR016311; Transform_prot_C-ets.
DR InterPro; IPR027276; Transform_prot_C-ets-2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF19525; Ets1_N_flank; 1.
DR Pfam; PF02198; SAM_PNT; 1.
DR PIRSF; PIRSF501032; C-ets-2; 1.
DR PIRSF; PIRSF001698; Transforming_factor_C-ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SMART; SM00251; SAM_PNT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR PROSITE; PS51433; PNT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..469
FT /note="Protein C-ets-2"
FT /id="PRO_0000204077"
FT DOMAIN 85..170
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 363..443
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 264..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24218572"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24218572"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15037"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15037"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:4MHV"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:4MHV"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:4MHV"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4MHV"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:4MHV"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:4MHV"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:4MHV"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:4MHV"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:4MHV"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4BQA"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4BQA"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:4BQA"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:4BQA"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:4BQA"
FT HELIX 365..373
FT /evidence="ECO:0007829|PDB:4BQA"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:4BQA"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:4BQA"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:4BQA"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:4BQA"
FT HELIX 396..407
FT /evidence="ECO:0007829|PDB:4BQA"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:4BQA"
FT TURN 423..428
FT /evidence="ECO:0007829|PDB:4BQA"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:4BQA"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:4BQA"
FT HELIX 446..450
FT /evidence="ECO:0007829|PDB:4BQA"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:4BQA"
SQ SEQUENCE 469 AA; 53001 MW; 5944EC4B5AAB553E CRC64;
MNDFGIKNMD QVAPVANSYR GTLKRQPAFD TFDGSLFAVF PSLNEEQTLQ EVPTGLDSIS
HDSANCELPL LTPCSKAVMS QALKATFSGF KKEQRRLGIP KNPWLWSEQQ VCQWLLWATN
EFSLVNVNLQ RFGMNGQMLC NLGKERFLEL APDFVGDILW EHLEQMIKEN QEKTEDQYEE
NSHLTSVPHW INSNTLGFGT EQAPYGMQTQ NYPKGGLLDS MCPASTPSVL SSEQEFQMFP
KSRLSSVSVT YCSVSQDFPG SNLNLLTNNS GTPKDHDSPE NGADSFESSD SLLQSWNSQS
SLLDVQRVPS FESFEDDCSQ SLCLNKPTMS FKDYIQERSD PVEQGKPVIP AAVLAGFTGS
GPIQLWQFLL ELLSDKSCQS FISWTGDGWE FKLADPDEVA RRWGKRKNKP KMNYEKLSRG
LRYYYDKNII HKTSGKRYVY RFVCDLQNLL GFTPEELHAI LGVQPDTED
