GenomeNet

Database: UniProt
Entry: Q86WJ1
LinkDB: Q86WJ1
Original site: Q86WJ1 
ID   CHD1L_HUMAN             Reviewed;         897 AA.
AC   Q86WJ1; A5YM64; Q53EZ3; Q5VXX7; Q6DD94; Q6PK83; Q86XH3; Q96HF7;
AC   Q96SP3; Q9BVJ1; Q9NVV8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 2.
DT   19-MAR-2014, entry version 99.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 1-like;
DE            EC=3.6.4.12;
DE   AltName: Full=Amplified in liver cancer protein 1;
GN   Name=CHD1L; Synonyms=ALC1;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND VARIANT SER-885.
RX   PubMed=18023026; DOI=10.1002/hep.22072;
RA   Ma N.-F., Hu L., Fung J.-M., Xie D., Zheng B.-J., Chen L., Tang D.-J.,
RA   Fu L., Wu Z., Chen M., Fang Y., Guan X.-Y.;
RT   "Isolation and characterization of a novel oncogene, amplified in
RT   liver cancer 1, within a commonly amplified region at 1q21 in
RT   hepatocellular carcinoma.";
RL   Hepatology 47:503-510(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-831 (ISOFORM 1), AND VARIANT SER-885.
RC   TISSUE=Neuron;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP   GLN-350 AND SER-885.
RC   TISSUE=Retina;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 2-897 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 15-897 (ISOFORM 2), AND VARIANTS PRO-25; CYS-743
RP   AND SER-885.
RC   TISSUE=Brain, Eye, Prostate, and 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-798.
RC   TISSUE=Hepatocyte;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891, VARIANT [LARGE
RP   SCALE ANALYSIS] SER-885, 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   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN MACRO, ADP-RIBOSE-BINDING,
RP   INTERACTION WITH PARP1, AND MUTAGENESIS OF LYS-77 AND ASP-723.
RX   PubMed=19661379; DOI=10.1126/science.1177321;
RA   Ahel D., Horejsi Z., Wiechens N., Polo S.E., Garcia-Wilson E.,
RA   Ahel I., Flynn H., Skehel M., West S.C., Jackson S.P., Owen-Hughes T.,
RA   Boulton S.J.;
RT   "Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin
RT   remodeling enzyme ALC1.";
RL   Science 325:1240-1243(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] SER-885, AND IDENTIFICATION BY MASS
RP   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).
CC   -!- FUNCTION: DNA helicase which plays a role in chromatin-remodeling
CC       following DNA damage. Targeted to sites of DNA damage through
CC       interaction with poly(ADP-ribose) and functions to regulate
CC       chromatin during DNA repair. Able to catalyze nucleosome sliding
CC       in an ATP-dependent manner. Helicase activity is strongly
CC       stimulated upon poly(ADP-ribose)-binding.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Interacts with PARP1; interacts only when PARP1 is poly-
CC       ADP-ribosylated (PARylated).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Localizes at sites of DNA
CC       damage. Probably recruited to DNA damage sites by PARylated PARP1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q86WJ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86WJ1-2; Sequence=VSP_033342;
CC       Name=3;
CC         IsoId=Q86WJ1-3; Sequence=VSP_033341;
CC       Name=4;
CC         IsoId=Q86WJ1-4; Sequence=VSP_033340;
CC   -!- TISSUE SPECIFICITY: Frequently overexpressed in hepatomacellular
CC       carcinomas.
CC   -!- DOMAIN: The macro domain mediates non-covalent poly(ADP-ribose)-
CC       binding and recruitment to DNA damage sites.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 Macro domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB55248.1; Type=Frameshift; Positions=597;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF537213; AAO49505.1; -; mRNA.
DR   EMBL; AK001342; BAA91637.1; -; mRNA.
DR   EMBL; AK027631; BAB55248.1; ALT_FRAME; mRNA.
DR   EMBL; EF560738; ABQ59048.1; -; mRNA.
DR   EMBL; AL356378; CAH72650.1; -; Genomic_DNA.
DR   EMBL; BC001171; AAH01171.1; -; mRNA.
DR   EMBL; BC005038; AAH05038.1; -; mRNA.
DR   EMBL; BC008649; AAH08649.1; -; mRNA.
DR   EMBL; BC043501; AAH43501.1; -; mRNA.
DR   EMBL; BC077717; AAH77717.1; -; mRNA.
DR   EMBL; AK223496; BAD97216.1; -; mRNA.
DR   RefSeq; NP_001243265.1; NM_001256336.1.
DR   RefSeq; NP_001243266.1; NM_001256337.1.
DR   RefSeq; NP_001243267.1; NM_001256338.1.
DR   RefSeq; NP_004275.4; NM_004284.4.
DR   RefSeq; NP_078844.2; NM_024568.2.
DR   UniGene; Hs.191164; -.
DR   ProteinModelPortal; Q86WJ1; -.
DR   SMR; Q86WJ1; 41-547, 719-873.
DR   BioGrid; 114929; 29.
DR   DIP; DIP-48933N; -.
DR   IntAct; Q86WJ1; 6.
DR   MINT; MINT-7944527; -.
DR   PhosphoSite; Q86WJ1; -.
DR   DMDM; 311033359; -.
DR   PaxDb; Q86WJ1; -.
DR   PRIDE; Q86WJ1; -.
DR   Ensembl; ENST00000369258; ENSP00000358262; ENSG00000131778. [Q86WJ1-1]
DR   Ensembl; ENST00000369259; ENSP00000358263; ENSG00000131778. [Q86WJ1-3]
DR   Ensembl; ENST00000431239; ENSP00000389031; ENSG00000131778. [Q86WJ1-2]
DR   Ensembl; ENST00000579763; ENSP00000463454; ENSG00000264980.
DR   Ensembl; ENST00000583055; ENSP00000464521; ENSG00000264980.
DR   GeneID; 9557; -.
DR   KEGG; hsa:9557; -.
DR   UCSC; uc001epm.5; human. [Q86WJ1-1]
DR   UCSC; uc001epo.5; human. [Q86WJ1-3]
DR   UCSC; uc009wjh.4; human. [Q86WJ1-2]
DR   CTD; 9557; -.
DR   GeneCards; GC01P146717; -.
DR   H-InvDB; HIX0000988; -.
DR   H-InvDB; HIX0028745; -.
DR   HGNC; HGNC:1916; CHD1L.
DR   HPA; HPA027789; -.
DR   HPA; HPA028670; -.
DR   MIM; 613039; gene.
DR   neXtProt; NX_Q86WJ1; -.
DR   PharmGKB; PA26452; -.
DR   eggNOG; COG0553; -.
DR   HOVERGEN; HBG077542; -.
DR   InParanoid; Q86WJ1; -.
DR   OMA; AFVFMIS; -.
DR   PhylomeDB; Q86WJ1; -.
DR   TreeFam; TF333326; -.
DR   ChiTaRS; CHD1L; human.
DR   GeneWiki; CHD1L; -.
DR   NextBio; 35849; -.
DR   PRO; PR:Q86WJ1; -.
DR   ArrayExpress; Q86WJ1; -.
DR   Bgee; Q86WJ1; -.
DR   CleanEx; HS_CHD1L; -.
DR   Genevestigator; Q86WJ1; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; TAS:UniProtKB.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Coiled coil; Complete proteome;
KW   DNA damage; DNA repair; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome.
FT   CHAIN         1    897       Chromodomain-helicase-DNA-binding protein
FT                                1-like.
FT                                /FTId=PRO_0000332141.
FT   DOMAIN       58    223       Helicase ATP-binding.
FT   DOMAIN      351    513       Helicase C-terminal.
FT   DOMAIN      704    897       Macro.
FT   NP_BIND      71     78       ATP (By similarity).
FT   COILED      638    675       Potential.
FT   MOTIF       174    177       DEAH box.
FT   MOD_RES     636    636       Phosphoserine.
FT   MOD_RES     891    891       Phosphoserine.
FT   VAR_SEQ       1    113       Missing (in isoform 4).
FT                                /FTId=VSP_033340.
FT   VAR_SEQ      43    246       Missing (in isoform 3).
FT                                /FTId=VSP_033341.
FT   VAR_SEQ     331    424       Missing (in isoform 2).
FT                                /FTId=VSP_033342.
FT   VARIANT      25     25       R -> P (in dbSNP:rs11588753).
FT                                /FTId=VAR_042954.
FT   VARIANT     350    350       H -> Q (in dbSNP:rs17356233).
FT                                /FTId=VAR_042955.
FT   VARIANT     649    649       E -> A (in dbSNP:rs13374920).
FT                                /FTId=VAR_042956.
FT   VARIANT     743    743       S -> C (in dbSNP:rs2275249).
FT                                /FTId=VAR_042957.
FT   VARIANT     885    885       A -> S (in dbSNP:rs4950394).
FT                                /FTId=VAR_042958.
FT   MUTAGEN      77     77       K->R: Abolishes ATPase activity.
FT   MUTAGEN     723    723       D->A: Strongly reduces poly(ADP-ribose)-
FT                                binding but not ATPase activity.
FT   CONFLICT    192    192       E -> EVFE (in Ref. 3; ABQ59048).
FT   CONFLICT    379    379       L -> P (in Ref. 2; BAB55248).
FT   CONFLICT    447    447       N -> D (in Ref. 6; BAD97216).
FT   CONFLICT    597    597       N -> S (in Ref. 6; BAD97216).
FT   CONFLICT    674    674       M -> V (in Ref. 2; BAA91637).
SQ   SEQUENCE   897 AA;  100984 MW;  226A1F8A5272F9FE CRC64;
     MERAGATSRG GQAPGFLLRL HTEGRAEAAR VQEQDLRQWG LTGIHLRSYQ LEGVNWLAQR
     FHCQNGCILG DEMGLGKTCQ TIALFIYLAG RLNDEGPFLI LCPLSVLSNW KEEMQRFAPG
     LSCVTYAGDK EERACLQQDL KQESRFHVLL TTYEICLKDA SFLKSFPWSV LVVDEAHRLK
     NQSSLLHKTL SEFSVVFSLL LTGTPIQNSL QELYSLLSFV EPDLFSKEEV GDFIQRYQDI
     EKESESASEL HKLLQPFLLR RVKAEVATEL PKKTEVVIYH GMSALQKKYY KAILMKDLDA
     FENETAKKVK LQNILSQLRK CVDHPYLFDG VEPEPFEVGD HLTEASGKLH LLDKLLAFLY
     SGGHRVLLFS QMTQMLDILQ DYMDYRGYSY ERVDGSVRGE ERHLAIKNFG QQPIFVFLLS
     TRAGGVGMNL TAADTVIFVD SDFNPQNDLQ AAARAHRIGQ NKSVKVIRLI GRDTVEEIVY
     RKAASKLQLT NMIIEGGHFT LGAQKPAADA DLQLSEILKF GLDKLLASEG STMDEIDLES
     ILGETKDGQW VSDALPAAEG GSRDQEEGKN HMYLFEGKDY SKEPSKEDRK SFEQLVNLQK
     TLLEKASQEG RSLRNKGSVL IPGLVEGSTK RKRVLSPEEL EDRQKKRQEA AAKRRRLIEE
     KKRQKEEAEH KKKMAWWESN NYQSFCLPSE ESEPEDLENG EESSAELDYQ DPDATSLKYV
     SGDVTHPQAG AEDALIVHCV DDSGHWGRGG LFTALEKRSA EPRKIYELAG KMKDLSLGGV
     LLFPVDDKES RNKGQDLLAL IVAQHRDRSN VLSGIKMAAL EEGLKKIFLA AKKKKASVHL
     PRIGHATKGF NWYGTERLIR KHLAARGIPT YIYYFPRSKS AVLHAQSSSS SSRQLVP
//
DBGET integrated database retrieval system