GenomeNet

Database: UniProt
Entry: A3KFM7
LinkDB: A3KFM7
Original site: A3KFM7 
ID   CHD6_MOUSE              Reviewed;        2711 AA.
AC   A3KFM7; B9EKA7; Q3UQS6; Q80TE9;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   16-OCT-2019, entry version 108.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 6;
DE            Short=CHD-6;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD6;
GN   Name=Chd6; Synonyms=Kiaa1335;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1733 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Heart;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-283 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=17027977; DOI=10.1016/j.febslet.2006.09.049;
RA   Lutz T., Stoger R., Nieto A.;
RT   "CHD6 is a DNA-dependent ATPase and localizes at nuclear sites of mRNA
RT   synthesis.";
RL   FEBS Lett. 580:5851-5857(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1865, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=20111866; DOI=10.1007/s00335-010-9248-8;
RA   Lathrop M.J., Chakrabarti L., Eng J., Rhodes C.H., Lutz T., Nieto A.,
RA   Liggitt H.D., Warner S., Fields J., Stoger R., Fiering S.;
RT   "Deletion of the Chd6 exon 12 affects motor coordination.";
RL   Mamm. Genome 21:130-142(2010).
CC   -!- FUNCTION: DNA-dependent ATPase that plays a role in chromatin
CC       remodeling. Regulates transcription by disrupting nucleosomes in a
CC       largely non-sliding manner which strongly increases the
CC       accessibility of chromatin. Activates transcription of specific
CC       genes in response to oxidative stress through interaction with
CC       NFE2L2. {ECO:0000250|UniProtKB:Q8TD26}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000250|UniProtKB:Q8TD26};
CC   -!- SUBUNIT: Interacts with NFE2L2; involved in activation of the
CC       transcription. {ECO:0000250|UniProtKB:Q8TD26}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q8TD26}. Note=Enriched at sites of mRNA
CC       synthesis. {ECO:0000250|UniProtKB:Q8TD26}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A3KFM7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A3KFM7-2; Sequence=VSP_054901;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:17027977}.
CC   -!- DISRUPTION PHENOTYPE: Mice with targeted deletion of exon 12
CC       lacking part of the Helicase ATP-binding domain are born in normal
CC       Mendelian ratios and are viable. They are fertile and exhibit no
CC       obvious morphological or histological difference. However, they
CC       display a coordination deficiency which is not due to muscle
CC       weakness or bradykinesia. {ECO:0000269|PubMed:20111866}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65778.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC65778.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. Spurious priming from an intronic poly-A tract.; Evidence={ECO:0000305};
DR   EMBL; AL590430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL591763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC150806; AAI50807.1; -; mRNA.
DR   EMBL; AK142177; BAE24963.1; -; mRNA.
DR   EMBL; AK122496; BAC65778.2; ALT_SEQ; mRNA.
DR   CCDS; CCDS17000.1; -. [A3KFM7-1]
DR   RefSeq; NP_775544.2; NM_173368.3. [A3KFM7-1]
DR   RefSeq; XP_011238078.1; XM_011239776.2. [A3KFM7-2]
DR   RefSeq; XP_017174747.1; XM_017319258.1. [A3KFM7-1]
DR   SMR; A3KFM7; -.
DR   IntAct; A3KFM7; 1.
DR   STRING; 10090.ENSMUSP00000042291; -.
DR   iPTMnet; A3KFM7; -.
DR   PhosphoSitePlus; A3KFM7; -.
DR   MaxQB; A3KFM7; -.
DR   PaxDb; A3KFM7; -.
DR   PeptideAtlas; A3KFM7; -.
DR   PRIDE; A3KFM7; -.
DR   Ensembl; ENSMUST00000039782; ENSMUSP00000042291; ENSMUSG00000057133. [A3KFM7-1]
DR   GeneID; 71389; -.
DR   KEGG; mmu:71389; -.
DR   UCSC; uc008nrn.2; mouse. [A3KFM7-1]
DR   UCSC; uc008nrp.2; mouse. [A3KFM7-2]
DR   CTD; 84181; -.
DR   MGI; MGI:1918639; Chd6.
DR   eggNOG; KOG0383; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   GeneTree; ENSGT00940000158986; -.
DR   HOGENOM; HOG000246942; -.
DR   InParanoid; A3KFM7; -.
DR   KO; K14436; -.
DR   OMA; AKDERKH; -.
DR   OrthoDB; 7181at2759; -.
DR   PhylomeDB; A3KFM7; -.
DR   TreeFam; TF313572; -.
DR   ChiTaRS; Chd6; mouse.
DR   PRO; PR:A3KFM7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000057133; Expressed in 263 organ(s), highest expression level in substantia nigra.
DR   ExpressionAtlas; A3KFM7; baseline and differential.
DR   Genevisible; A3KFM7; MM.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; ISS:UniProtKB.
DR   GO; GO:0001221; F:transcription cofactor binding; ISO:MGI.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISS:UniProtKB.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00592; BRK; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54160; SSF54160; 2.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Chromatin regulator;
KW   Complete proteome; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation.
FT   CHAIN         1   2711       Chromodomain-helicase-DNA-binding protein
FT                                6.
FT                                /FTId=PRO_0000429353.
FT   DOMAIN      291    342       Chromo 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      374    438       Chromo 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      472    646       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      786    955       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     1448   1502       Myb-like.
FT   NP_BIND     485    492       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1    746       Required for DNA-dependent ATPase
FT                                activity. {ECO:0000250}.
FT   MOTIF       597    600       DEAH box.
FT   MOD_RES    1865   1865       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   VAR_SEQ     184    184       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_054901.
FT   CONFLICT    756    756       K -> R (in Ref. 3; BAE24963).
FT                                {ECO:0000305}.
FT   CONFLICT   1305   1305       L -> H (in Ref. 3; BAE24963).
FT                                {ECO:0000305}.
FT   CONFLICT   1741   1741       I -> V (in Ref. 2; AAI50807).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2711 AA;  305397 MW;  256A4983B8EA3544 CRC64;
     MKMKIQKKEK QLSKLRALNH SPMSDASVNF DYKSPSPFDC SPDQGENIEE AANHCLPHKN
     LYTTEEEADT LFSRKLTSHN GMEDSGGRGT GVKKKRKKKE PGEQEGTKGS KDREPKPKRK
     REPKEPKEPR RAKEPKRAKE PKETKQKDGV KKPRKHREAS GTKEGKEKRS CTDYGSRTKS
     KKASREQGPT PVERKKKGKR KNETTVESLE LDHSLPNPSL QSPEEPSESA DSQKRRSGRQ
     VKRRKYNEDL DFKVVDDDGE TIAVLGAGRT SALSASTLAW QAEEPPEDDA NIIEKILASK
     TVQEVHPGEP PFDLELFYVK YRNFSYLHCK WATMEELEKD PRIAQKIKRF RNKQAQMKHI
     FTEPDEDLFN PDYIEIDRIL EVAHTKDAET GEEVTHYLVK WCSLPYEEST WELEEDVDPA
     KVKEFESLQI LPEVKHVERP ASDAWQKLET SREYRNSNRL REYQLEGMNW LLFNWYNRKN
     CILADEMGLG KTIQSIAFLS EIFVRGIHGP FLIIAPLSTI TNWEREFRTW TEMNAIVYHG
     SQISRQMIQQ YEMVYRDAQG NPLSGVFKFH VVITTFEMIL ADCPELKKIH WSCVIIDEAH
     RLKNRNCKLL EGLKLMALEH KVLLTGTPLQ NSVEELFSLL NFLEPSQFPS ETAFLEEFGD
     LKTEEQVKKL QSILKPMMLR RLKDDVEKNL APKQETIIEV ELTNIQKKYY RAILEKNFSF
     LTKGANQHNM PNLINTMMEL RKCCNHPYLI NGAEEKILED FRKAHSSEAS DFQLQAMIQA
     AGKLVLIDKL LPKLIAGGHK VLIFSQMVRC LDILEDYLIQ RRYTYERIDG RVRGNLRQAA
     IDRFCKPDSD RFVFLLCTRA GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQSKA
     VKVYRLITRN SYEREMFDKA SLKLGLDKAI LQDINRKGST NGVQQLSKME VEDLLRKGAY
     GALMDEEDEG SKFCEEDIDQ ILQRRTHTIT IQSEGKGSTF AKASFVASGN RTDISLDDPN
     FWQKWAKIAE LDTEANNEKE SLVIDRPRVR KQTKHYNSFE EDELMEFSEL DSDSDERPTR
     SRRLSDRARR YLRAECFRVE KNLLIFGWGR WKDILTHGRF KWPLNEKDME MICRALLVYC
     VKHYKGDEKI KSFIWELITP SKDGQVQTLQ NHSGLSAPVP RGRKGKKTKN QLLLPELKNA
     DWLATCNPEV VLHDDGYKKH LKQHCNKVLL RVRMLYYLKA EILGEAADKA FEGTPARELD
     VLLPDIDYVE IPVDWWDAEA DKSLLIGVFK HGYERYNAMR ADPALCFLEK VGMPDEKSLS
     AEQGVTDGTS DIPERGNIDK EDSAEDKLDG LQKQTASPSD GSDGIFGEKK DDSQAAQDGS
     DPDKSPWPVS SALTARLRRL VTIYQRCNRK ELCRPEILGP GNQGYWVQEE VFRRTSEMDL
     INKEAQKRWT RREQADFYRT VSSFGVVYDQ EKKAFDWTQF RIISRLDKKS DESLEHYFYS
     FVAMCRNVCR LPAWKDDGPP DASIYVEPIT EERAAKTLYR IELLRKVREQ VLMCPQLHER
     LQLCRPSLYL PVWWECGKHD RDLLIGTAKH GLNRTDYYIM NDPQLSFLDA YRNYAQHKRT
     DTQAPGSLCC LYQSNSKLYE SLTYTPVSRT SESLESEPEN LMRMESRDDH LCLPEGGLPD
     ITCENFVSKV QEVISLDHDE NLLPESLENM IYGKTGLSQE PHSFQEAPTT NTQSRKNTIT
     ISASRNESCQ PPGIEAEITS ASSLMSSLEA GVAKMNIKNG KHLLVSISKE GEPCCSETGR
     RPETIGHREA KCLVSPTLDT GHESGFVDLC SLSVYDPKRN FSSDQQLIDL LENKSLESKL
     ILNQSDEEEE ENEDETLAIV ASATEKPEVL DFPKPTVNIP RGKNLSFHQD EAKKGRLEVV
     SKTAGPQRVF PPPANQCHCK HIERWAHGLG SEDSEVEKPK AYQPDLYRSK ANNSTVEGET
     AVIPTEPFKL KHELLKEPWK ESSEGGKSFS MYAPEGSEPK PEDMDFENKD DYEKDGTCLS
     QDYPGKYSEE ESKSSASGIA GDLGEEAQEV RAPTIAQLLQ EKTLYSFSEW PKDRVIINRL
     DNICHVVLKG KWPCSHQYEP SGALPTPVLS SSAGSRSSLS EPEATEHGFS NGAALAAQIQ
     KESFLAPVFT KDEQKHRRPY EFEVERDAKA RSLEEYSATH GRPPIVLNGW HGESAIDLSC
     SSEGSPGATS PFPVSASTPK IGAISSLQGA LGMDLSGILQ AGLIHPVTGQ IVNGSLRRDD
     AAMRRRRGRR KHIEGGMDLI FLKEQTLQAG ILEVHEDAGQ TTLSTTHPEV PGATSSAPEP
     TAAASSQAEK AVPSKSLLDW LRQQADYSLD VPGFGTSFSD KPKQRRPRCK EPGKLDISSL
     GGEERVPAVP KEPGLRGFLP ESKFNHTLAE PVLRDAGPRR RGRRPRNELL KAPAIVADSP
     SGMGPLFMNG LIAGMDLVGL QNVRNIPGIP LTGLVGFPAG FATMPTGEEV KNTLSMLPMM
     LPGMAAVPQM FGVGGLLNTP MATTCTTTAS ASLASTKSGT SATEKSTEDK LSGHDVNTDA
     LVDDKPGPSP FSDQSEPTIT TSSPVAFNPF LIPGVSPGLI YPSMFLSPGM GMALPAMQQA
     RHSEMVGLET QKRKKKKTKG DSPTQEPASV CEKEPGSDQN CTESSATVSP EREHVAQARE
     EGLKDSNEDT N
//
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