GenomeNet

Database: UniProt
Entry: Q8BYH8
LinkDB: Q8BYH8
Original site: Q8BYH8 
ID   CHD9_MOUSE              Reviewed;        2885 AA.
AC   Q8BYH8; Q7TMV5; Q8BJG8; Q8BZJ2; Q8CHG8;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   16-OCT-2019, entry version 140.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 9;
DE            Short=CHD-9;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD9;
DE   AltName: Full=PPAR-alpha-interacting complex protein 320 kDa;
DE   AltName: Full=Peroxisomal proliferator-activated receptor A-interacting complex 320 kDa protein;
GN   Name=Chd9; Synonyms=Kiaa0308, Pric320;
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 [MRNA] (ISOFORM 2).
RX   PubMed=16554032; DOI=10.1016/j.bbrc.2006.02.160;
RA   Surapureddi S., Viswakarma N., Yu S., Guo D., Rao M.S., Reddy J.K.;
RT   "PRIC320, a transcription coactivator, isolated from peroxisome
RT   proliferator-binding protein complex.";
RL   Biochem. Biophys. Res. Commun. 343:535-543(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1104 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Diencephalon, Spinal cord, and Spinal ganglion;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 980-2885 (ISOFORM 2).
RC   TISSUE=Pancreatic islet;
RX   PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2207-2885 (ISOFORM 1).
RC   STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
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   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16419031; DOI=10.1002/jcp.20586;
RA   Shur I., Socher R., Benayahu D.;
RT   "In vivo association of CReMM/CHD9 with promoters in osteogenic
RT   cells.";
RL   J. Cell. Physiol. 207:374-378(2006).
CC   -!- FUNCTION: Acts as a transcriptional coactivator for PPARA and
CC       possibly other nuclear receptors. Proposed to be a ATP-dependent
CC       chromatin remodeling protein. Has DNA-dependent ATPase activity
CC       and binds to A/T-rich DNA (By similarity). Associates with A/T-
CC       rich regulatory regions in promoters of genes that participate in
CC       the differentiation of progenitors during osteogenesis.
CC       {ECO:0000250}.
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: Interacts with PPARA. Probably interacts with ESR1 and
CC       NR1I3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BYH8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYH8-2; Sequence=VSP_018087;
CC   -!- TISSUE SPECIFICITY: Expressed in osteoprogenitor cells during
CC       development and in mature bone (at protein level).
CC       {ECO:0000269|PubMed:16419031}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from embryonic day 16.5 dpc in
CC       mesenchymal cartilage surrounding bone cartilage and newly formed
CC       bone trabecular spicules. Detected in bone sections of 4-day-old
CC       newborn and 3-week-old mice. {ECO:0000269|PubMed:16419031}.
CC   -!- PTM: Phosphorylated on serine and tyrosine residues.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52896.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; DQ127229; AAZ73184.2; -; mRNA.
DR   EMBL; AK034446; BAC28711.1; -; mRNA.
DR   EMBL; AK039562; BAC30385.1; -; mRNA.
DR   EMBL; AK084000; BAC39090.1; -; mRNA.
DR   EMBL; AB093226; BAC41410.3; -; mRNA.
DR   EMBL; BC052896; AAH52896.1; ALT_INIT; mRNA.
DR   CCDS; CCDS22517.1; -. [Q8BYH8-2]
DR   CCDS; CCDS80912.1; -. [Q8BYH8-1]
DR   RefSeq; NP_001297459.1; NM_001310530.1. [Q8BYH8-1]
DR   RefSeq; NP_796198.1; NM_177224.2. [Q8BYH8-2]
DR   RefSeq; XP_006530632.1; XM_006530569.2. [Q8BYH8-1]
DR   RefSeq; XP_011246574.1; XM_011248272.2. [Q8BYH8-1]
DR   RefSeq; XP_011246575.1; XM_011248273.2. [Q8BYH8-1]
DR   RefSeq; XP_011246576.1; XM_011248274.2. [Q8BYH8-1]
DR   RefSeq; XP_011246577.1; XM_011248275.2. [Q8BYH8-1]
DR   RefSeq; XP_017168006.1; XM_017312517.1. [Q8BYH8-1]
DR   RefSeq; XP_017168007.1; XM_017312518.1. [Q8BYH8-1]
DR   SMR; Q8BYH8; -.
DR   CORUM; Q8BYH8; -.
DR   STRING; 10090.ENSMUSP00000105243; -.
DR   iPTMnet; Q8BYH8; -.
DR   PhosphoSitePlus; Q8BYH8; -.
DR   PaxDb; Q8BYH8; -.
DR   PeptideAtlas; Q8BYH8; -.
DR   PRIDE; Q8BYH8; -.
DR   Ensembl; ENSMUST00000048665; ENSMUSP00000046356; ENSMUSG00000056608. [Q8BYH8-2]
DR   Ensembl; ENSMUST00000109614; ENSMUSP00000105243; ENSMUSG00000056608. [Q8BYH8-1]
DR   Ensembl; ENSMUST00000209423; ENSMUSP00000148088; ENSMUSG00000056608. [Q8BYH8-1]
DR   GeneID; 109151; -.
DR   KEGG; mmu:109151; -.
DR   UCSC; uc009msf.2; mouse. [Q8BYH8-2]
DR   UCSC; uc009msi.2; mouse. [Q8BYH8-1]
DR   CTD; 80205; -.
DR   MGI; MGI:1924001; Chd9.
DR   eggNOG; KOG0384; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   GeneTree; ENSGT00940000155706; -.
DR   HOGENOM; HOG000246942; -.
DR   InParanoid; Q8BYH8; -.
DR   KO; K14438; -.
DR   OMA; KMTDYEQ; -.
DR   OrthoDB; 7181at2759; -.
DR   PhylomeDB; Q8BYH8; -.
DR   TreeFam; TF313572; -.
DR   Reactome; R-MMU-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
DR   ChiTaRS; Chd9; mouse.
DR   PRO; PR:Q8BYH8; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000056608; Expressed in 235 organ(s), highest expression level in manus.
DR   ExpressionAtlas; Q8BYH8; baseline and differential.
DR   Genevisible; Q8BYH8; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.28.130; -; 2.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR037259; BRK_sf.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
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; PF07533; BRK; 2.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00592; BRK; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF160481; SSF160481; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54160; SSF54160; 2.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Chromatin regulator;
KW   Complete proteome; Cytoplasm; DNA-binding; Helicase; Hydrolase;
KW   Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN         1   2885       Chromodomain-helicase-DNA-binding protein
FT                                9.
FT                                /FTId=PRO_0000233173.
FT   DOMAIN      689    760       Chromo 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      772    838       Chromo 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      871   1045       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1185   1336       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     884    891       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION     2331   2471       Binds A/T-rich DNA. {ECO:0000250}.
FT   REGION     2428   2435       A.T hook-like.
FT   MOTIF       867    871       LXXLL motif 1.
FT   MOTIF       996    999       DEAH box.
FT   MOTIF      1035   1039       LXXLL motif 2.
FT   MOTIF      2030   2034       LXXLL motif 3.
FT   MOTIF      2710   2714       LXXLL motif 4.
FT   MOTIF      2782   2787       LXXLL motif 5.
FT   MOD_RES     498    498       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   MOD_RES     549    549       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   MOD_RES     610    610       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   MOD_RES    1467   1467       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   MOD_RES    1471   1471       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   MOD_RES    2025   2025       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   MOD_RES    2057   2057       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   MOD_RES    2058   2058       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   MOD_RES    2074   2074       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   MOD_RES    2078   2078       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK    197    197       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK    595    595       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK   1587   1587       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK   1737   1737       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK   1902   1902       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK   2037   2037       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK   2073   2073       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK   2349   2349       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK   2355   2355       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK   2360   2360       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   CROSSLNK   2833   2833       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q3L8U1}.
FT   VAR_SEQ    2335   2350       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12465718,
FT                                ECO:0000303|PubMed:16554032}.
FT                                /FTId=VSP_018087.
FT   CONFLICT    101    101       N -> I (in Ref. 2; BAC39090).
FT                                {ECO:0000305}.
FT   CONFLICT    584    584       Y -> D (in Ref. 2; BAC28711).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2885 AA;  323860 MW;  B820BE8EA9CC2915 CRC64;
     MTDPMMDFFD DANLFGETLE GLSDDTFVQP GPVSLVDELN LGAEFEPLHI DSLNHVQGTP
     THQKMADFEQ LSQFDSMKFH PVNQSFGSPV EHVLSPHSQF NCSPIHPPNQ PNGLFQDVAD
     GSPMWGHQTA TGLANQNGSP FHQPGHSHSL HQNKSFVAHP DFALFQASEH QTQCSSLHSQ
     QSRSNLNPGQ NSLGQAKNFL DANVSGAHRV NVNHLATAPS SQQTLPVQFS PTANPPAHFL
     KCSSHQEGNY NRPSPSMTSC SVSNSQQFPS HYSFSSGHVS PSSLLQSSAG LAPGHTNQAL
     SDFAGSNSFS PHRGMKQEPT QHLLNPTPSL NSNNFQILHS SHPQGNYSNS KLSPVHMNFP
     DPVDAGPPVG HFNDHAETNG FSSLEENLLH HVDSHAEPFA GLDPEDLLQE GLLPQFDESP
     FGQDNSNHVL DHDLDRQFTS HLVSRPSDMA QTQLQYQARG WPSPLSTNHQ HLHSRNHLCL
     QRQPPSSKKS DGSGTYTKLQ NTQVRVMSEK KPRKRVESES KQEKANRIIS EAIARAKERG
     ERNIPRVMSP ENFPSASVEG KEEKRGRRMK SKPKDRDNKK PKTYSKLKEK TKIGKLIITL
     GKKHKRRNES SDELSDAEQR SQHTFKEQHS QKRRSNRQIK RKKYAEDAEG KQSEEEVKGS
     LRVKRNSAPP PGEQPLQLFV ENPSEEDAAI VDKILACRTV KKEVSPGVML DIEEFFVKYK
     NYSYLHCEWA TEQQLLKDKR IQQKIKRFKL RQAQRAHFLA DMEEEPFNPD YVEVDRILEV
     SFCEDKDTGE SVIYYLVKWC SLPYEDSTWE LKEDVDLAKI EEFEQLQASR PDTRHLDRPP
     SNIWKKIEQS REYKNGNQLR EYQLEGLNWL LFNWYNRRNC ILADEMGLGK TIQSITFLYE
     ILLTGIRGPF LIIAPLSTIA NWEREFRTWT DINVVVYHGS LISRQMIQQY EMYFRDSQGR
     IIRGAYRFQA IITTFEMILG GCGELNAIDW RCVIIDEAHR LKNKNCKLLE GLKLMNLEHK
     VLLTGTPLQN TVEELFSLLH FLEPLRFPSE STFMQEFGDL KTEEQVQKLQ AILKPMMLRR
     LKEDVEKKLA PKEETIIEVE LTNIQKKYYR AILEKNFSFL SKGAGQTNVP NLVNTMMELR
     KCCNHPYLIK GAEEKILGEF RDTYNPSASD FHLQAMIQSA GKLVLIDKLL PKMKAGGHKV
     LIFSQMVRCL DILEDYLIHK RYLYERIDGR VRGNLRQAAI DRFSKPDSDR FVFLLCTRAG
     GLGINLTAAD TCIIFDSDWN PQNDLQAQAR CHRIGQNKAV KVYRLVTRNS YEREMFDRAS
     LKLGLDKAVL QSMSGRDSNV SGIQQLSKKE IEDLLRRGAY GAIMEEEDEG SKFCEEDIDQ
     ILLRRTKTIT IESEGRGSTF AKASFVASGN RTDISLDDPN FWQKWAKKAE LDIDTISGRN
     SLVIDTPRIR KQTRPFSATK DELAELSEAE SEGEEKPKLR RPCDRSGGYG RTECFRVEKN
     LLVYGWGRWR EILSHGRFKR QLNEHDVEVI CRALLAYCLI HYRGDEKIKG FIWDLITPTE
     DGQTRELQNH LGLSAPVPRG RKGKKVKTQT SSFDIQKAEW LRKYNPEQLL QDEGYKKHVK
     HHCNKVLLRV RMLYYLKQEV IGNESQKVFD GVDASDIDVW VPEPDHSEVP AAWWDFDADK
     SLLIGVFKHG YEKYNTIRAD PALCFLERVG KPDDKAVAAE QRANDYMDGD VEDPEYKPAP
     AIFKDDIEDD VSSPGDLVIA DGEGQLMEGD KVYWPTPSAL TTRLRRLITA YQRTNKNRHI
     QQMQPTFSLP ANAMQPLYEE ATLNPKMAAK IERQQRWTRR EEADFYRVVS TFGVVFDPDR
     GQFDWTKFRA LARLHKKTDN SLEKYLCAFM SMCRRVCRLP SKEELVDPNI FIQPITEERA
     SRTLYRIELL RKVREQALRH PQLFERLKLC HPNPDLPIWW ECGSHDRDLL IGAAKHGVSR
     TDYHILRDPE LSFMAAQRNY NQSKAAHSRT SAPLLQQYQV ALSASPLTSL PRLLGAKGTL
     LEDMKVKSES LTEEPQSSEE ESMSSMETRT RVKSEPVSPK NGVLSQATGD QKSGGKSETD
     RRMVAARTEP LTPNPASKKP RVHKRGSQSS SDSDSDSARS SCSSRSSSSS SSSSSCSHSR
     SGSSSSSSSS CSSASSSSSS SSSSSSSSSS SSSEESDSEE DVQKREGTPH RKAYDEESVA
     SLSTTQDETQ DSFQANNGTP ESAYLLQGGY MLAASYWPKD RVMINRLDSI CQTVLKGKWP
     SARRHYDANT VASFYTTKLL DSPGAATERG EPSVPTPPAV AVREEHEQSA QMSKVKKHVR
     EKEFTVKIKD EGGLKLTFQK QGLAQKRPFD GEDGALGQQQ YLTRLRELQS TSETSLVNLP
     KAVPASGTSI QPTLGANGAI LDSQPIVKKR RGRRRNVEGA DILFLNRNKP PNHIPTGMNP
     ALSYPQPQRI PDTESPVPVI NLKDGTRLAG DDAPKRKDLD RWLKEHPGYV EDLGAFIPRV
     QLHEGRPKQK RHRCRNPNKL DINSLTGEER VQLINRRNAR KVGGAFAPPL KDLCRFLKEN
     SEYGVAPEWG DVVKQSGFLP ESMFERILTG PVVREEVSRR GRRPKSGIAK ATTAAAVPAG
     SVPGNPLLAN GLLPGVDLTA LQALQQNLQN LQSLQVTAGL MGMPAGLSSG GETKNMAAMF
     PMLFSGMAGL PNLLGMGGLL SKTAESGAEE KRGNDSKELE GKKERTESQS PENGGERCVP
     GSPSTSSTAA LSSAAAAKPI ALNPLLLSNI LYPGMLLTPG LNLHLPTLSQ SNAFDVQKNK
     SDDLDSSKSV EIKEENSRVR DQEEKGGTEP SPLNENSTDE GSERASSGSD SSSSSSEDSD
     SSNED
//
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