GenomeNet

Database: UniProt
Entry: Q8TDI0
LinkDB: Q8TDI0
Original site: Q8TDI0 
ID   CHD5_HUMAN              Reviewed;        1954 AA.
AC   Q8TDI0; O75032; Q5TG89; Q7LGH2; Q9UFR9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   11-DEC-2019, entry version 165.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 5;
DE            Short=CHD-5;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD5;
GN   Name=CHD5 {ECO:0000312|EMBL:AAL98962.1}; Synonyms=KIAA0444;
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] {ECO:0000305, ECO:0000312|EMBL:AAL98962.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=12592387; DOI=10.1038/sj.onc.1206211;
RA   Thompson P.M., Gotoh T., Kok M., White P.S., Brodeur G.M.;
RT   "CHD5, a new member of the chromodomain gene family, is preferentially
RT   expressed in the nervous system.";
RL   Oncogene 22:1002-1011(2003).
RN   [2]
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., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., 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., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., 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., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-1954, AND VARIANT PRO-1539.
RC   TISSUE=Testis;
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., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   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 MRNA] OF 977-1954, AND VARIANT PRO-1539.
RC   TISSUE=Brain;
RX   PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA   Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA   Nomura N., Ohara O.;
RT   "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT   human brain.";
RL   DNA Res. 4:345-349(1997).
RN   [5]
RP   DISEASE.
RX   PubMed=17289567; DOI=10.1016/j.cell.2006.11.052;
RA   Bagchi A., Papazoglu C., Wu Y., Capurso D., Brodt M., Francis D.,
RA   Bredel M., Vogel H., Mills A.A.;
RT   "CHD5 is a tumor suppressor at human 1p36.";
RL   Cell 128:459-475(2007).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21931736; DOI=10.1371/journal.pone.0024515;
RA   Potts R.C., Zhang P., Wurster A.L., Precht P., Mughal M.R., Wood W.H.,
RA   Zhang Y., Becker K.G., Mattson M.P., Pazin M.J.;
RT   "CHD5, a brain-specific paralog of Mi2 chromatin remodeling enzymes,
RT   regulates expression of neuronal genes.";
RL   PLoS ONE 6:E24515-E24515(2011).
RN   [7]
RP   FUNCTION AS A TRANSCRIPTIONAL REGULATOR, FUNCTION IN NEURON
RP   DIFFERENTIATION, INTERACTION WITH HISTONE H3K27ME3, SUBCELLULAR LOCATION,
RP   CHROMO DOMAINS, AND MUTAGENESIS OF LEU-518 AND TYR-619.
RX   PubMed=23948251; DOI=10.1016/j.devcel.2013.07.008;
RA   Egan C.M., Nyman U., Skotte J., Streubel G., Turner S., O'Connell D.J.,
RA   Rraklli V., Dolan M.J., Chadderton N., Hansen K., Farrar G.J., Helin K.,
RA   Holmberg J., Bracken A.P.;
RT   "CHD5 is required for neurogenesis and has a dual role in facilitating gene
RT   expression and polycomb gene repression.";
RL   Dev. Cell 26:223-236(2013).
RN   [8]
RP   METHYLATION AT GLN-1390, AND MUTAGENESIS OF GLN-1390.
RX   PubMed=26797129; DOI=10.1074/jbc.m115.711952;
RA   Kusevic D., Kudithipudi S., Jeltsch A.;
RT   "Substrate specificity of the HEMK2 protein glutamine methyltransferase and
RT   identification of novel substrates.";
RL   J. Biol. Chem. 291:6124-6133(2016).
RN   [9]
RP   VARIANTS [LARGE SCALE ANALYSIS] MET-45; ASN-119 AND GLY-667.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Chromatin-remodeling protein that binds DNA through histones
CC       and regulates gene transcription. May specifically recognize and bind
CC       trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone
CC       H3. Plays a role in the development of the nervous system by activating
CC       the expression of genes promoting neuron terminal differentiation. In
CC       parallel, it may also positively regulate the trimethylation of histone
CC       H3 at 'Lys-27' thereby specifically repressing genes that promote the
CC       differentiation into non-neuronal cell lineages. Tumor suppressor, it
CC       regulates the expression of genes involved in cell proliferation and
CC       differentiation. Downstream activated genes may include CDKN2A that
CC       positively regulates the p53/TP53 pathway, which in turn, prevents cell
CC       proliferation. In spermatogenesis, it probably regulates histone
CC       hyperacetylation and the replacement of histones by transition proteins
CC       in chromatin, a crucial step in the condensation of spermatid chromatin
CC       and the production of functional spermatozoa.
CC       {ECO:0000269|PubMed:23948251}.
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   -!- SUBUNIT: May be part of a nucleosome remodeling and histone
CC       deacetylation, NuRD-like, complex composed at least of GATAD2B, HDAC1,
CC       HDAC2 and MTA3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21931736,
CC       ECO:0000269|PubMed:23948251}. Note=Associates with heterochromatin.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in total brain, fetal
CC       brain, and cerebellum. It is also moderately expressed in the adrenal
CC       gland and detected in testis. {ECO:0000269|PubMed:12592387,
CC       ECO:0000269|PubMed:21931736}.
CC   -!- DOMAIN: The PHD domains mediate specific binding to histone H3
CC       unmethylated at 'Lys-4' and may preferentially recruit the protein to
CC       transcriptionally inactive genes. {ECO:0000250}.
CC   -!- DOMAIN: The chromo domains mediate specific binding to histone H3
CC       trimethylated at 'Lys-27' (H3K27me3) and may be required in neuron
CC       differentiation for proper gene regulation.
CC       {ECO:0000269|PubMed:23948251}.
CC   -!- PTM: Methylated at Gln-1390 by N6AMT1. {ECO:0000269|PubMed:26797129}.
CC   -!- DISEASE: Note=Defects in CHD5 may be a cause of the development of
CC       cancers from epithelial, neural and hematopoietic origin. CHD5 is one
CC       of the missing genes in the del(1p36), a deletion which is extremely
CC       common in this type of cancers. A decrease of its expression, results
CC       in increased susceptibility of cells to Ras-mediated transformation in
CC       vitro and in vivo (PubMed:17289567). {ECO:0000269|PubMed:17289567}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000255}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CHD5ID44521ch1p36.html";
DR   EMBL; AF425231; AAL98962.1; -; mRNA.
DR   EMBL; AL031847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL035406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL117491; CAB55959.1; -; mRNA.
DR   EMBL; AB007913; BAA32289.1; -; mRNA.
DR   CCDS; CCDS57.1; -.
DR   PIR; T17269; T17269.
DR   RefSeq; NP_056372.1; NM_015557.2.
DR   SMR; Q8TDI0; -.
DR   BioGrid; 117504; 22.
DR   IntAct; Q8TDI0; 11.
DR   MINT; Q8TDI0; -.
DR   STRING; 9606.ENSP00000262450; -.
DR   iPTMnet; Q8TDI0; -.
DR   PhosphoSitePlus; Q8TDI0; -.
DR   BioMuta; CHD5; -.
DR   DMDM; 51701343; -.
DR   EPD; Q8TDI0; -.
DR   jPOST; Q8TDI0; -.
DR   MassIVE; Q8TDI0; -.
DR   MaxQB; Q8TDI0; -.
DR   PaxDb; Q8TDI0; -.
DR   PeptideAtlas; Q8TDI0; -.
DR   PRIDE; Q8TDI0; -.
DR   ProteomicsDB; 74289; -.
DR   DNASU; 26038; -.
DR   Ensembl; ENST00000262450; ENSP00000262450; ENSG00000116254.
DR   GeneID; 26038; -.
DR   KEGG; hsa:26038; -.
DR   UCSC; uc001amb.3; human.
DR   CTD; 26038; -.
DR   DisGeNET; 26038; -.
DR   EuPathDB; HostDB:ENSG00000116254.17; -.
DR   GeneCards; CHD5; -.
DR   HGNC; HGNC:16816; CHD5.
DR   HPA; HPA015809; -.
DR   MIM; 610771; gene.
DR   neXtProt; NX_Q8TDI0; -.
DR   OpenTargets; ENSG00000116254; -.
DR   PharmGKB; PA134969178; -.
DR   eggNOG; ENOG410IREB; Eukaryota.
DR   eggNOG; ENOG410XNUT; LUCA.
DR   GeneTree; ENSGT00940000159249; -.
DR   HOGENOM; HOG000231124; -.
DR   InParanoid; Q8TDI0; -.
DR   KO; K14435; -.
DR   OMA; ITWRWAV; -.
DR   OrthoDB; 54215at2759; -.
DR   PhylomeDB; Q8TDI0; -.
DR   TreeFam; TF106448; -.
DR   ChiTaRS; CHD5; human.
DR   GeneWiki; CHD5; -.
DR   GenomeRNAi; 26038; -.
DR   Pharos; Q8TDI0; Tbio.
DR   PRO; PR:Q8TDI0; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q8TDI0; protein.
DR   Bgee; ENSG00000116254; Expressed in 131 organ(s), highest expression level in frontal cortex.
DR   ExpressionAtlas; Q8TDI0; baseline and differential.
DR   Genevisible; Q8TDI0; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; 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:0061628; F:H3K27me3 modified histone binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0021895; P:cerebral cortex neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0098532; P:histone H3-K27 trimethylation; IMP:UniProtKB.
DR   GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0060850; P:regulation of transcription involved in cell fate commitment; IMP:UniProtKB.
DR   GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 2.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR028727; CHD5.
DR   InterPro; IPR012957; CHD_C2.
DR   InterPro; IPR012958; CHD_N.
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; IPR009462; DUF1086.
DR   InterPro; IPR009463; DUF1087.
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   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45623:SF6; PTHR45623:SF6; 1.
DR   Pfam; PF08074; CHDCT2; 1.
DR   Pfam; PF08073; CHDNT; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF06461; DUF1086; 1.
DR   Pfam; PF06465; DUF1087; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01146; DUF1086; 1.
DR   SMART; SM01147; DUF1087; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54160; SSF54160; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Chromatin regulator; Differentiation; DNA-binding; Helicase;
KW   Hydrolase; Metal-binding; Methylation; Neurogenesis; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW   Spermatogenesis; Transcription; Transcription regulation; Tumor suppressor;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1954
FT                   /note="Chromodomain-helicase-DNA-binding protein 5"
FT                   /id="PRO_0000080230"
FT   DOMAIN          497..554
FT                   /note="Chromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          592..653
FT                   /note="Chromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          712..896
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1028..1193
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         343..390
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         416..463
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   NP_BIND         725..732
FT                   /note="ATP"
FT                   /evidence="ECO:0000250|UniProtKB:Q14839,
FT                   ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          343..653
FT                   /note="Histone-binding"
FT   MOTIF           847..850
FT                   /note="DEAH box"
FT   COMPBIAS        49..116
FT                   /note="Lys-rich"
FT   MOD_RES         1390
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000269|PubMed:26797129"
FT   MOD_RES         1554
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2A8L1"
FT   VARIANT         45
FT                   /note="V -> M (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs1470692239)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035475"
FT   VARIANT         119
FT                   /note="D -> N (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035476"
FT   VARIANT         667
FT                   /note="R -> G (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035477"
FT   VARIANT         1253
FT                   /note="S -> I (in dbSNP:rs6657997)"
FT                   /id="VAR_048729"
FT   VARIANT         1539
FT                   /note="S -> P (in dbSNP:rs2843493)"
FT                   /evidence="ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|PubMed:9455484"
FT                   /id="VAR_048730"
FT   MUTAGEN         518
FT                   /note="L->A: Reduced affinity for trimethylated histone
FT                   H3K27me3."
FT                   /evidence="ECO:0000269|PubMed:23948251"
FT   MUTAGEN         619
FT                   /note="Y->E: Reduced affinity for trimethylated histone
FT                   H3K27me3."
FT                   /evidence="ECO:0000269|PubMed:23948251"
FT   MUTAGEN         1390
FT                   /note="Q->R: Abolishes methylation by N6AMT1."
FT                   /evidence="ECO:0000269|PubMed:26797129"
SQ   SEQUENCE   1954 AA;  223050 MW;  E333062B5B55E71F CRC64;
     MRGPVGTEEE LPRLFAEEME NEDEMSEEED GGLEAFDDFF PVEPVSLPKK KKPKKLKENK
     CKGKRKKKEG SNDELSENEE DLEEKSESEG SDYSPNKKKK KKLKDKKEKK AKRKKKDEDE
     DDNDDGCLKE PKSSGQLMAE WGLDDVDYLF SEEDYHTLTN YKAFSQFLRP LIAKKNPKIP
     MSKMMTVLGA KWREFSANNP FKGSSAAAAA AAVAAAVETV TISPPLAVSP PQVPQPVPIR
     KAKTKEGKGP GVRKKIKGSK DGKKKGKGKK TAGLKFRFGG ISNKRKKGSS SEEDEREESD
     FDSASIHSAS VRSECSAALG KKSKRRRKKK RIDDGDGYET DHQDYCEVCQ QGGEIILCDT
     CPRAYHLVCL DPELEKAPEG KWSCPHCEKE GIQWEPKDDD DEEEEGGCEE EEDDHMEFCR
     VCKDGGELLC CDACPSSYHL HCLNPPLPEI PNGEWLCPRC TCPPLKGKVQ RILHWRWTEP
     PAPFMVGLPG PDVEPSLPPP KPLEGIPERE FFVKWAGLSY WHCSWVKELQ LELYHTVMYR
     NYQRKNDMDE PPPFDYGSGD EDGKSEKRKN KDPLYAKMEE RFYRYGIKPE WMMIHRILNH
     SFDKKGDVHY LIKWKDLPYD QCTWEIDDID IPYYDNLKQA YWGHRELMLG EDTRLPKRLL
     KKGKKLRDDK QEKPPDTPIV DPTVKFDKQP WYIDSTGGTL HPYQLEGLNW LRFSWAQGTD
     TILADEMGLG KTVQTIVFLY SLYKEGHSKG PYLVSAPLST IINWEREFEM WAPDFYVVTY
     TGDKESRSVI RENEFSFEDN AIRSGKKVFR MKKEVQIKFH VLLTSYELIT IDQAILGSIE
     WACLVVDEAH RLKNNQSKFF RVLNSYKIDY KLLLTGTPLQ NNLEELFHLL NFLTPERFNN
     LEGFLEEFAD ISKEDQIKKL HDLLGPHMLR RLKADVFKNM PAKTELIVRV ELSQMQKKYY
     KFILTRNFEA LNSKGGGNQV SLLNIMMDLK KCCNHPYLFP VAAVEAPVLP NGSYDGSSLV
     KSSGKLMLLQ KMLKKLRDEG HRVLIFSQMT KMLDLLEDFL EYEGYKYERI DGGITGGLRQ
     EAIDRFNAPG AQQFCFLLST RAGGLGINLA TADTVIIYDS DWNPHNDIQA FSRAHRIGQN
     KKVMIYRFVT RASVEERITQ VAKRKMMLTH LVVRPGLGSK SGSMTKQELD DILKFGTEEL
     FKDDVEGMMS QGQRPVTPIP DVQSSKGGNL AASAKKKHGS TPPGDNKDVE DSSVIHYDDA
     AISKLLDRNQ DATDDTELQN MNEYLSSFKV AQYVVREEDG VEEVEREIIK QEENVDPDYW
     EKLLRHHYEQ QQEDLARNLG KGKRIRKQVN YNDASQEDQE WQDELSDNQS EYSIGSEDED
     EDFEERPEGQ SGRRQSRRQL KSDRDKPLPP LLARVGGNIE VLGFNARQRK AFLNAIMRWG
     MPPQDAFNSH WLVRDLRGKS EKEFRAYVSL FMRHLCEPGA DGAETFADGV PREGLSRQHV
     LTRIGVMSLV RKKVQEFEHV NGKYSTPDLI PEGPEGKKSG EVISSDPNTP VPASPAHLLP
     APLGLPDKME AQLGYMDEKD PGAQKPRQPL EVQALPAALD RVESEDKHES PASKERAREE
     RPEETEKAPP SPEQLPREEV LPEKEKILDK LELSLIHSRG DSSELRPDDT KAEEKEPIET
     QQNGDKEEDD EGKKEDKKGK FKFMFNIADG GFTELHTLWQ NEERAAVSSG KIYDIWHRRH
     DYWLLAGIVT HGYARWQDIQ NDPRYMILNE PFKSEVHKGN YLEMKNKFLA RRFKLLEQAL
     VIEEQLRRAA YLNMTQDPNH PAMALNARLA EVECLAESHQ HLSKESLAGN KPANAVLHKV
     LNQLEELLSD MKADVTRLPS MLSRIPPVAA RLQMSERSIL SRLTNRAGDP TIQQGAFGSS
     QMYSNNFGPN FRGPGPGGIV NYNQMPLGPY VTDI
//
DBGET integrated database retrieval system