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Database: UniProt
Entry: Q8IWX8
LinkDB: Q8IWX8
Original site: Q8IWX8 
ID   CHERP_HUMAN             Reviewed;         916 AA.
AC   Q8IWX8; O00302; Q4G0Y5; Q8WU30; Q99492;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   29-OCT-2014, entry version 99.
DE   RecName: Full=Calcium homeostasis endoplasmic reticulum protein;
DE   AltName: Full=ERPROT 213-21;
DE   AltName: Full=SR-related CTD-associated factor 6;
GN   Name=CHERP {ECO:0000312|HGNC:HGNC:16930};
GN   Synonyms=DAN26 {ECO:0000312|EMBL:CAA69591.1},
GN   SCAF6 {ECO:0000312|EMBL:AAN77183.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAN77183.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-199.
RA   Sampson N.D., Hewitt J.E.;
RT   "Functional characterization of the novel SR-related CTD associated
RT   factor, SCAF6.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   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   [3] {ECO:0000305, ECO:0000312|EMBL:AAH21294.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus {ECO:0000312|EMBL:AAH21294.1};
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   [4] {ECO:0000305, ECO:0000312|EMBL:CAA69591.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-607.
RC   TISSUE=Lymphoblast {ECO:0000312|EMBL:CAA69591.1};
RX   PubMed=8896557; DOI=10.1038/ng1196-285;
RA   Imbert G., Saudou F., Yvert G., Devys D., Trottier Y., Garnier J.-M.,
RA   Weber C., Mandel J.-L., Cancel G., Abbas N., Duerr A., Didierjean O.,
RA   Stevanin G., Agid Y., Brice A.;
RT   "Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with
RT   high sensitivity to expanded CAG/glutamine repeats.";
RL   Nat. Genet. 14:285-291(1996).
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAB53327.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-916, FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND VARIANT HIS-199.
RX   PubMed=10794731; DOI=10.1042/0264-6021:3480189;
RA   LaPlante J.M., O'Rourke F., Lu X., Fein A., Olsen A., Feinstein M.B.;
RT   "Cloning of human Ca2+ homoeostasis endoplasmic reticulum protein
RT   (CHERP): regulated expression of antisense cDNA depletes CHERP,
RT   inhibits intracellular Ca2+ mobilization and decreases cell
RT   proliferation.";
RL   Biochem. J. 348:189-199(2000).
RN   [6] {ECO:0000305}
RP   SUBCELLULAR LOCATION.
RX   PubMed=8010949;
RA   O'Rourke F., Soons K., Flaumenhauft R., Watras J., Baio-Larue C.,
RA   Matthews E., Feinstein M.B.;
RT   "Ca2+ release by inositol 1,4,5-trisphosphate is blocked by the K(+)-
RT   channel blockers apamin and tetrapentylammonium ion, and a monoclonal
RT   antibody to a 63 kDa membrane protein: reversal of blockade by K+
RT   ionophores nigericin and valinomycin and purification of the 63 kDa
RT   antibody-binding protein.";
RL   Biochem. J. 300:673-683(1994).
RN   [7] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12656674; DOI=10.1042/BJ20030013;
RA   O'Rourke F.A., LaPlante J.M., Feinstein M.B.;
RT   "Antisense-mediated loss of calcium homoeostasis endoplasmic reticulum
RT   protein (CHERP; ERPROT213-21) impairs Ca2+ mobilization, nuclear
RT   factor of activated T-cells (NFAT) activation and cell proliferation
RT   in Jurkat T-lymphocytes.";
RL   Biochem. J. 373:133-143(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813; SER-815; SER-817;
RP   THR-819; SER-828 AND SER-904, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815 AND SER-817, AND
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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18 AND LYS-879, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813; SER-815; SER-817
RP   AND THR-819, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Involved in calcium homeostasis, growth and
CC       proliferation. {ECO:0000269|PubMed:10794731,
CC       ECO:0000269|PubMed:12656674}.
CC   -!- INTERACTION:
CC       Q14562:DHX8; NbExp=2; IntAct=EBI-2555370, EBI-2511477;
CC       Q70Z53:FRA10AC1; NbExp=2; IntAct=EBI-2555370, EBI-710176;
CC       Q9NQ29:LUC7L; NbExp=2; IntAct=EBI-2555370, EBI-473747;
CC       Q8WVK2:SNRNP27; NbExp=2; IntAct=EBI-2555370, EBI-2512550;
CC       P26368:U2AF2; NbExp=2; IntAct=EBI-2555370, EBI-742339;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10794731,
CC       ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}.
CC       Cytoplasm, perinuclear region {ECO:0000269|PubMed:10794731,
CC       ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:10794731,
CC       ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}.
CC       Note=Distributed throughout the cytoplasm and also localizes to
CC       the perinuclear region of both human erythroleukemia (HEL) cells
CC       and Jurkat cells. Colocalizes with ITPR1.
CC       {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674,
CC       ECO:0000269|PubMed:8010949}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, placenta, lung, liver,
CC       kidney, pancreas, cardiac and skeletal muscle, and in cultured HEL
CC       and Dami cells. {ECO:0000269|PubMed:10794731}.
CC   -!- SIMILARITY: Contains 1 CID domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00724}.
CC   -!- SIMILARITY: Contains 1 G-patch domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00092}.
CC   -!- SIMILARITY: Contains 1 SURP motif repeat. {ECO:0000255|PROSITE-
CC       ProRule:PRU00263}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB53327.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAH21294.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=CAA69591.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=CAA69591.1; Type=Frameshift; Positions=450; Evidence={ECO:0000305};
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DR   EMBL; AF536542; AAN77183.1; -; mRNA.
DR   EMBL; AC008764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021294; AAH21294.1; ALT_INIT; mRNA.
DR   EMBL; Y08265; CAA69591.1; ALT_SEQ; mRNA.
DR   EMBL; U94836; AAB53327.1; ALT_INIT; mRNA.
DR   CCDS; CCDS42518.1; -.
DR   RefSeq; NP_006378.3; NM_006387.5.
DR   UniGene; Hs.740364; -.
DR   ProteinModelPortal; Q8IWX8; -.
DR   SMR; Q8IWX8; 6-61.
DR   BioGrid; 115778; 48.
DR   IntAct; Q8IWX8; 32.
DR   MINT; MINT-4654608; -.
DR   STRING; 9606.ENSP00000198939; -.
DR   PhosphoSite; Q8IWX8; -.
DR   DMDM; 296439404; -.
DR   MaxQB; Q8IWX8; -.
DR   PaxDb; Q8IWX8; -.
DR   PRIDE; Q8IWX8; -.
DR   Ensembl; ENST00000546361; ENSP00000439856; ENSG00000085872.
DR   GeneID; 10523; -.
DR   KEGG; hsa:10523; -.
DR   UCSC; uc002nei.1; human.
DR   CTD; 10523; -.
DR   GeneCards; GC19M016629; -.
DR   HGNC; HGNC:16930; CHERP.
DR   HPA; HPA050647; -.
DR   neXtProt; NX_Q8IWX8; -.
DR   PharmGKB; PA26459; -.
DR   eggNOG; NOG267701; -.
DR   GeneTree; ENSGT00730000111147; -.
DR   HOGENOM; HOG000010294; -.
DR   HOVERGEN; HBG052716; -.
DR   InParanoid; Q8IWX8; -.
DR   KO; K12841; -.
DR   OrthoDB; EOG7H1JK4; -.
DR   PhylomeDB; Q8IWX8; -.
DR   TreeFam; TF318512; -.
DR   GenomeRNAi; 10523; -.
DR   NextBio; 39918; -.
DR   PRO; PR:Q8IWX8; -.
DR   Bgee; Q8IWX8; -.
DR   CleanEx; HS_CHERP; -.
DR   ExpressionAtlas; Q8IWX8; baseline and differential.
DR   Genevestigator; Q8IWX8; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
DR   GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0051533; P:positive regulation of NFAT protein import into nucleus; IMP:UniProtKB.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR006569; CID_dom.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR006903; RNA_pol_II-bd.
DR   InterPro; IPR000061; Surp.
DR   Pfam; PF04818; CTD_bind; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF01805; Surp; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00582; RPR; 1.
DR   SMART; SM00648; SWAP; 1.
DR   SUPFAM; SSF109905; SSF109905; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   PROSITE; PS51391; CID; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50128; SURP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; Endoplasmic reticulum;
KW   Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN         1    916       Calcium homeostasis endoplasmic reticulum
FT                                protein.
FT                                /FTId=PRO_0000299492.
FT   REPEAT       15     57       SURP motif. {ECO:0000255}.
FT   DOMAIN      149    289       CID. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00724}.
FT   DOMAIN      841    891       G-patch. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00092}.
FT   COMPBIAS    279    346       Gln-rich. {ECO:0000255}.
FT   COMPBIAS    355    682       Pro-rich. {ECO:0000255}.
FT   COMPBIAS    718    816       Arg-rich. {ECO:0000255}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000269|PubMed:19413330,
FT                                ECO:0000269|PubMed:22814378}.
FT   MOD_RES      18     18       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES     714    714       Phosphotyrosine. {ECO:0000250}.
FT   MOD_RES     813    813       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     815    815       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:19690332,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     817    817       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:19690332,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     819    819       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     828    828       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648}.
FT   MOD_RES     879    879       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES     904    904       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648}.
FT   VARIANT     199    199       N -> H (in dbSNP:rs1043448).
FT                                {ECO:0000269|PubMed:10794731,
FT                                ECO:0000269|Ref.1}.
FT                                /FTId=VAR_034833.
FT   CONFLICT     99     99       A -> D (in Ref. 4; CAA69591).
FT                                {ECO:0000305}.
FT   CONFLICT    175    175       A -> G (in Ref. 4; CAA69591).
FT                                {ECO:0000305}.
FT   CONFLICT    185    185       K -> T (in Ref. 4; CAA69591).
FT                                {ECO:0000305}.
FT   CONFLICT    189    189       H -> Y (in Ref. 4; CAA69591).
FT                                {ECO:0000305}.
FT   CONFLICT    203    203       A -> V (in Ref. 4; CAA69591).
FT                                {ECO:0000305}.
FT   CONFLICT    418    418       K -> N (in Ref. 4; CAA69591).
FT                                {ECO:0000305}.
FT   CONFLICT    490    490       S -> N (in Ref. 4; CAA69591).
FT                                {ECO:0000305}.
FT   CONFLICT    776    776       Y -> S (in Ref. 1; AAN77183).
FT                                {ECO:0000305}.
FT   CONFLICT    778    778       R -> C (in Ref. 1; AAN77183).
FT                                {ECO:0000305}.
SQ   SEQUENCE   916 AA;  103702 MW;  0C5D56F4DE4C5B9B CRC64;
     MEMPLPPDDQ ELRNVIDKLA QFVARNGPEF EKMTMEKQKD NPKFSFLFGG EFYSYYKCKL
     ALEQQQLICK QQTPELEPAA TMPPLPQPPL APAAPIPPAQ GAPSMDELIQ QSQWNLQQQE
     QHLLALRQEQ VTAAVAHAVE QQMQKLLEET QLDMNEFDNL LQPIIDTCTK DAISAGKNWM
     FSNAKSPPHC ELMAGHLRNR ITADGAHFEL RLHLIYLIND VLHHCQRKQA RELLAALQKV
     VVPIYCTSFL AVEEDKQQKI ARLLQLWEKN GYFDDSIIQQ LQSPALGLGQ YQATLINEYS
     SVVQPVQLAF QQQIQTLKTQ HEEFVTSLAQ QQQQQQQQQQ QLQMPQMEAE VKATPPPPAP
     PPAPAPAPAI PPTTQPDDSK PPIQMPGSSE YEAPGGVQDP AAAGPRGPGP HDQIPPNKPP
     WFDQPHPVAP WGQQQPPEQP PYPHHQGGPP HCPPWNNSHE GMWGEQRGDP GWNGQRDAPW
     NNQPDAAWNS QFEGPWNSQH EQPPWGGGQR EPPFRMQRPP HFRGPFPPHQ QHPQFNQPPH
     PHNFNRFPPR FMQDDFPPRH PFERPPYPHR FDYPQGDFPA EMGPPHHHPG HRMPHPGINE
     HPPWAGPQHP DFGPPPHGFN GQPPHMRRQG PPHINHDDPS LVPNVPYFDL PAGLMAPLVK
     LEDHEYKPLD PKDIRLPPPM PPSERLLAAV EAFYSPPSHD RPRNSEGWEQ NGLYEFFRAK
     MRARRRKGQE KRNSGPSRSR SRSKSRGRSS SRSNSRSSKS SGSYSRSRSR SCSRSYSRSR
     SRSRSRSRSS RSRSRSQSRS RSKSYSPGRR RRSRSRSPTP PSSAGLGSNS APPIPDSRLG
     EENKGHQMLV KMGWSGSGGL GAKEQGIQDP IKGGDVRDKW DQYKGVGVAL DDPYENYRRN
     KSYSFIARMK ARDECK
//
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