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Database: UniProt
Entry: P15036
LinkDB: P15036
Original site: P15036 
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   07-OCT-2020, entry version 201.
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; 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";
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   SMR; P15036; -.
DR   BioGRID; 108415; 29.
DR   CORUM; P15036; -.
DR   DIP; DIP-40452N; -.
DR   IntAct; P15036; 22.
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; 390 antibodies.
DR   DNASU; 2114; -.
DR   Ensembl; ENST00000360214; ENSP00000353344; ENSG00000157557.
DR   Ensembl; ENST00000360938; ENSP00000354194; ENSG00000157557.
DR   Ensembl; ENST00000653642; ENSP00000499315; ENSG00000157557.
DR   Ensembl; ENST00000662305; ENSP00000499226; ENSG00000157557.
DR   Ensembl; ENST00000666778; ENSP00000499775; ENSG00000157557.
DR   GeneID; 2114; -.
DR   KEGG; hsa:2114; -.
DR   UCSC; uc002yxf.4; human.
DR   CTD; 2114; -.
DR   DisGeNET; 2114; -.
DR   EuPathDB; HostDB:ENSG00000157557.11; -.
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   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000160202; -.
DR   HOGENOM; CLU_031197_1_1_1; -.
DR   InParanoid; P15036; -.
DR   KO; K21932; -.
DR   OMA; QDFQMFP; -.
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; 13 hits in 894 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 236 other tissues.
DR   ExpressionAtlas; P15036; baseline and differential.
DR   Genevisible; P15036; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
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; IDA:BHF-UCL.
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:0035259; F:glucocorticoid receptor binding; IEA:Ensembl.
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: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; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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; IPR000418; Ets_dom.
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   Pfam; PF00178; Ets; 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   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:0000244|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:0000244|PDB:4MHV"
FT   HELIX           85..89
FT                   /evidence="ECO:0000244|PDB:4MHV"
FT   HELIX           90..96
FT                   /evidence="ECO:0000244|PDB:4MHV"
FT   HELIX           103..105
FT                   /evidence="ECO:0000244|PDB:4MHV"
FT   HELIX           108..121
FT                   /evidence="ECO:0000244|PDB:4MHV"
FT   HELIX           129..132
FT                   /evidence="ECO:0000244|PDB:4MHV"
FT   HELIX           136..141
FT                   /evidence="ECO:0000244|PDB:4MHV"
FT   HELIX           144..150
FT                   /evidence="ECO:0000244|PDB:4MHV"
FT   HELIX           155..169
FT                   /evidence="ECO:0000244|PDB:4MHV"
FT   HELIX           331..334
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   HELIX           335..337
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   STRAND          338..342
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   STRAND          344..346
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   HELIX           351..358
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   HELIX           365..373
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   HELIX           376..378
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   TURN            379..381
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   STRAND          382..384
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   STRAND          390..392
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   HELIX           396..407
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   HELIX           414..422
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   TURN            423..428
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   STRAND          429..432
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   STRAND          439..442
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   HELIX           446..450
FT                   /evidence="ECO:0000244|PDB:4BQA"
FT   HELIX           454..457
FT                   /evidence="ECO:0000244|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
//
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