ID   ETV5_HUMAN              Reviewed;         510 AA.
AC   P41161; A6NH46; B7Z7D7; Q6IBN5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=ETS translocation variant 5;
DE   AltName: Full=Ets-related protein ERM;
GN   Name=ETV5; Synonyms=ERM;
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=Testis;
RX   PubMed=8152800;
RA   Monte D., Baert J.-L., Defossez P.-A., de Launoit Y., Stehelin D.;
RT   "Molecular cloning and characterization of human ERM, a new member of the
RT   Ets family closely related to mouse PEA3 and ER81 transcription factors.";
RL   Oncogene 9:1397-1406(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8661127; DOI=10.1006/geno.1996.0345;
RA   Monte D., Coutte L., Dewitte F., Defossez P.-A., le Coniat D., Stehelin R.,
RA   Berger Y., de Launoit Y.;
RT   "Genomic organization of the human ERM (ETV5) gene, a PEA3 group member of
RT   ETS transcription factors.";
RL   Genomics 35:236-240(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skin;
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   [9]
RP   MASS SPECTROMETRY.
RC   TISSUE=Mammary cancer;
RX   PubMed=11840567;
RX   DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA   Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA   Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA   Zvelebil M.J.;
RT   "Cluster analysis of an extensive human breast cancer cell line protein
RT   expression map database.";
RL   Proteomics 2:212-223(2002).
RN   [10]
RP   INTERACTION WITH ZMYM5.
RX   PubMed=17126306; DOI=10.1016/j.brainres.2006.10.056;
RA   Pastorcic M., Das H.K.;
RT   "Analysis of transcriptional modulation of the presenilin 1 gene promoter
RT   by ZNF237, a candidate binding partner of the Ets transcription factor
RT   ERM.";
RL   Brain Res. 1128:21-32(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY
RP   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   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-350, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-350, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: Binds to DNA sequences containing the consensus nucleotide
CC       core sequence 5'-GGAA.-3'. {ECO:0000269|PubMed:8152800}.
CC   -!- SUBUNIT: Interacts (via C-terminal) with ZMYM5 (via N-terminal 120
CC       amino acid region). {ECO:0000269|PubMed:17126306}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P41161-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P41161-2; Sequence=VSP_055489;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- MASS SPECTROMETRY: Mass=57837.98; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11840567};
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR   EMBL; X76184; CAA53778.1; -; mRNA.
DR   EMBL; X96381; CAA65246.1; -; Genomic_DNA.
DR   EMBL; X96380; CAA65246.1; JOINED; Genomic_DNA.
DR   EMBL; X96382; CAA65246.1; JOINED; Genomic_DNA.
DR   EMBL; X96379; CAA65246.1; JOINED; Genomic_DNA.
DR   EMBL; X96378; CAA65246.1; JOINED; Genomic_DNA.
DR   EMBL; X96377; CAA65246.1; JOINED; Genomic_DNA.
DR   EMBL; X96376; CAA65246.1; JOINED; Genomic_DNA.
DR   EMBL; X96375; CAA65246.1; JOINED; Genomic_DNA.
DR   EMBL; AK301878; BAH13573.1; -; mRNA.
DR   EMBL; CR456767; CAG33048.1; -; mRNA.
DR   EMBL; BT006713; AAP35359.1; -; mRNA.
DR   EMBL; AC108671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC112649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW78200.1; -; Genomic_DNA.
DR   EMBL; BC007333; AAH07333.1; -; mRNA.
DR   CCDS; CCDS33906.1; -. [P41161-1]
DR   PIR; S43692; S43692.
DR   RefSeq; NP_004445.1; NM_004454.2. [P41161-1]
DR   PDB; 4UNO; X-ray; 1.95 A; A=365-462.
DR   PDB; 5ILV; X-ray; 1.80 A; A=366-457.
DR   PDBsum; 4UNO; -.
DR   PDBsum; 5ILV; -.
DR   AlphaFoldDB; P41161; -.
DR   SMR; P41161; -.
DR   BioGRID; 108420; 35.
DR   IntAct; P41161; 22.
DR   STRING; 9606.ENSP00000306894; -.
DR   GlyGen; P41161; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P41161; -.
DR   PhosphoSitePlus; P41161; -.
DR   BioMuta; ETV5; -.
DR   DMDM; 729441; -.
DR   jPOST; P41161; -.
DR   MassIVE; P41161; -.
DR   PaxDb; 9606-ENSP00000306894; -.
DR   PeptideAtlas; P41161; -.
DR   ProteomicsDB; 55407; -. [P41161-1]
DR   ProteomicsDB; 6857; -.
DR   Antibodypedia; 34851; 381 antibodies from 34 providers.
DR   DNASU; 2119; -.
DR   Ensembl; ENST00000306376.10; ENSP00000306894.5; ENSG00000244405.8. [P41161-1]
DR   Ensembl; ENST00000434744.5; ENSP00000413755.1; ENSG00000244405.8. [P41161-1]
DR   GeneID; 2119; -.
DR   KEGG; hsa:2119; -.
DR   MANE-Select; ENST00000306376.10; ENSP00000306894.5; NM_004454.3; NP_004445.1.
DR   UCSC; uc003fpz.4; human. [P41161-1]
DR   AGR; HGNC:3494; -.
DR   CTD; 2119; -.
DR   DisGeNET; 2119; -.
DR   GeneCards; ETV5; -.
DR   HGNC; HGNC:3494; ETV5.
DR   HPA; ENSG00000244405; Low tissue specificity.
DR   MIM; 601600; gene.
DR   neXtProt; NX_P41161; -.
DR   OpenTargets; ENSG00000244405; -.
DR   PharmGKB; PA27908; -.
DR   VEuPathDB; HostDB:ENSG00000244405; -.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000160680; -.
DR   HOGENOM; CLU_030025_1_0_1; -.
DR   InParanoid; P41161; -.
DR   OMA; MIPENQY; -.
DR   OrthoDB; 3915960at2759; -.
DR   PhylomeDB; P41161; -.
DR   TreeFam; TF316214; -.
DR   PathwayCommons; P41161; -.
DR   SignaLink; P41161; -.
DR   SIGNOR; P41161; -.
DR   BioGRID-ORCS; 2119; 22 hits in 1190 CRISPR screens.
DR   ChiTaRS; ETV5; human.
DR   GenomeRNAi; 2119; -.
DR   Pharos; P41161; Tbio.
DR   PRO; PR:P41161; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P41161; Protein.
DR   Bgee; ENSG00000244405; Expressed in buccal mucosa cell and 177 other cell types or tissues.
DR   ExpressionAtlas; P41161; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
DR   GO; GO:0048133; P:male germ-line stem cell asymmetric division; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR   GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR046328; ETS_fam.
DR   InterPro; IPR006715; ETS_PEA3_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11849; ETS; 1.
DR   PANTHER; PTHR11849:SF160; ETS TRANSLOCATION VARIANT 5; 1.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF04621; ETS_PEA3_N; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   Genevisible; P41161; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..510
FT                   /note="ETS translocation variant 5"
FT                   /id="PRO_0000204118"
FT   DNA_BIND        368..448
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          131..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..158
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..203
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        350
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1
FT                   /note="M -> MSERRCPPEHREGVNDTGGSLFPQKLLNAETSQSGIRDAESTM (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055489"
FT   VARIANT         348
FT                   /note="K -> R (in dbSNP:rs2228269)"
FT                   /id="VAR_048951"
FT   HELIX           370..378
FT                   /evidence="ECO:0007829|PDB:5ILV"
FT   HELIX           381..383
FT                   /evidence="ECO:0007829|PDB:5ILV"
FT   TURN            384..386
FT                   /evidence="ECO:0007829|PDB:5ILV"
FT   STRAND          387..389
FT                   /evidence="ECO:0007829|PDB:5ILV"
FT   STRAND          395..400
FT                   /evidence="ECO:0007829|PDB:5ILV"
FT   HELIX           401..412
FT                   /evidence="ECO:0007829|PDB:5ILV"
FT   HELIX           419..431
FT                   /evidence="ECO:0007829|PDB:5ILV"
FT   STRAND          434..437
FT                   /evidence="ECO:0007829|PDB:5ILV"
FT   STRAND          442..449
FT                   /evidence="ECO:0007829|PDB:5ILV"
FT   HELIX           453..455
FT                   /evidence="ECO:0007829|PDB:5ILV"
SQ   SEQUENCE   510 AA;  57838 MW;  B7CE40A33927F46E CRC64;
     MDGFYDQQVP FMVPGKSRSE ECRGRPVIDR KRKFLDTDLA HDSEELFQDL SQLQEAWLAE
     AQVPDDEQFV PDFQSDNLVL HAPPPTKIKR ELHSPSSELS SCSHEQALGA NYGEKCLYNY
     CAYDRKPPSG FKPLTPPTTP LSPTHQNPLF PPPQATLPTS GHAPAAGPVQ GVGPAPAPHS
     LPEPGPQQQT FAVPRPPHQP LQMPKMMPEN QYPSEQRFQR QLSEPCHPFP PQPGVPGDNR
     PSYHRQMSEP IVPAAPPPPQ GFKQEYHDPL YEHGVPGMPG PPAHGFQSPM GIKQEPRDYC
     VDSEVPNCQS SYMRGGYFSS SHEGFSYEKD PRLYFDDTCV VPERLEGKVK QEPTMYREGP
     PYQRRGSLQL WQFLVTLLDD PANAHFIAWT GRGMEFKLIE PEEVARRWGI QKNRPAMNYD
     KLSRSLRYYY EKGIMQKVAG ERYVYKFVCD PDALFSMAFP DNQRPFLKAE SECHLSEEDT
     LPLTHFEDSP AYLLDMDRCS SLPYAEGFAY
//