GenomeNet

Database: UniProt/SWISS-PROT
Entry: ASH1L_MOUSE
LinkDB: ASH1L_MOUSE
Original site: ASH1L_MOUSE 
ID   ASH1L_MOUSE             Reviewed;        2958 AA.
AC   Q99MY8; E9QNM2; Q3U598; Q80VY5; Q8BM69; Q8BTX0; Q8BZY6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   25-OCT-2017, entry version 130.
DE   RecName: Full=Histone-lysine N-methyltransferase ASH1L;
DE            EC=2.1.1.43;
DE   AltName: Full=ASH1-like protein;
DE   AltName: Full=Absent small and homeotic disks protein 1 homolog;
GN   Name=Ash1l;
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] OF 1-2005 AND 2048-2465.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Testis, and Thymus;
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   PROTEIN SEQUENCE OF 88-94; 1254-1265; 1730-1752 AND 2270-2277, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 290-2958.
RC   TISSUE=Thymus;
RA   Tanaka Y.;
RT   "A novel SWI/SNF family gene in mammals reveals a bromodomain lost in
RT   Drosophila ASH1.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1996-2958.
RC   TISSUE=Limb;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160 AND SER-1168, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2307; LYS-2309 AND LYS-2313,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Histone methyltransferase specifically methylating 'Lys-
CC       36' of histone H3 (H3K36me). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell junction, tight
CC       junction {ECO:0000250}. Chromosome {ECO:0000250}. Note=The
CC       relevance of tight junction localization is however unclear.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK26242.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=BAE32182.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; AC127377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK033177; BAC28183.2; -; mRNA.
DR   EMBL; AK034679; BAC28795.2; -; mRNA.
DR   EMBL; AK088497; BAC40390.1; -; mRNA.
DR   EMBL; AK153783; BAE32182.1; ALT_INIT; mRNA.
DR   EMBL; AF247132; AAK26242.1; ALT_INIT; mRNA.
DR   EMBL; BC052194; AAH52194.1; -; mRNA.
DR   CCDS; CCDS17487.1; -.
DR   RefSeq; NP_619620.3; NM_138679.5.
DR   RefSeq; XP_006501204.1; XM_006501141.2.
DR   RefSeq; XP_006501205.1; XM_006501142.2.
DR   UniGene; Mm.130752; -.
DR   ProteinModelPortal; Q99MY8; -.
DR   SMR; Q99MY8; -.
DR   BioGrid; 228672; 2.
DR   STRING; 10090.ENSMUSP00000088451; -.
DR   iPTMnet; Q99MY8; -.
DR   PhosphoSitePlus; Q99MY8; -.
DR   MaxQB; Q99MY8; -.
DR   PaxDb; Q99MY8; -.
DR   PeptideAtlas; Q99MY8; -.
DR   PRIDE; Q99MY8; -.
DR   Ensembl; ENSMUST00000090933; ENSMUSP00000088451; ENSMUSG00000028053.
DR   Ensembl; ENSMUST00000186583; ENSMUSP00000140251; ENSMUSG00000028053.
DR   GeneID; 192195; -.
DR   KEGG; mmu:192195; -.
DR   UCSC; uc008pxi.1; mouse.
DR   CTD; 55870; -.
DR   MGI; MGI:2183158; Ash1l.
DR   eggNOG; KOG1083; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   eggNOG; COG5076; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   HOVERGEN; HBG080871; -.
DR   InParanoid; Q99MY8; -.
DR   KO; K06101; -.
DR   OMA; HSEMTDY; -.
DR   OrthoDB; EOG091G02U7; -.
DR   TreeFam; TF106416; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; Ash1l; mouse.
DR   PRO; PR:Q99MY8; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000028053; -.
DR   Genevisible; Q99MY8; MM.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISO:MGI.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046697; P:decidualization; IMP:MGI.
DR   GO; GO:0097676; P:histone H3-K36 dimethylation; ISO:MGI.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IDA:MGI.
DR   GO; GO:0032635; P:interleukin-6 production; IGI:MGI.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IMP:MGI.
DR   GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IGI:MGI.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0048733; P:sebaceous gland development; IMP:MGI.
DR   GO; GO:0007338; P:single fertilization; IMP:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   GO; GO:0097722; P:sperm motility; IMP:MGI.
DR   GO; GO:1903699; P:tarsal gland development; IMP:MGI.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:1903709; P:uterine gland development; IMP:MGI.
DR   GO; GO:0061038; P:uterus morphogenesis; IMP:MGI.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00384; AT_hook; 4.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Bromodomain; Cell junction;
KW   Chromatin regulator; Chromosome; Complete proteome;
KW   Direct protein sequencing; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; S-adenosyl-L-methionine; Tight junction; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   2958       Histone-lysine N-methyltransferase ASH1L.
FT                                /FTId=PRO_0000259517.
FT   DOMAIN     2081   2132       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN     2135   2251       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     2259   2275       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DOMAIN     2452   2522       Bromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00035}.
FT   DOMAIN     2650   2787       BAH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00370}.
FT   DNA_BIND    885    897       A.T hook 1.
FT   DNA_BIND   1345   1357       A.T hook 2.
FT   DNA_BIND   1843   1855       A.T hook 3.
FT   ZN_FING    2574   2620       PHD-type.
FT   REGION     2059   2278       Catalytic domain. {ECO:0000250}.
FT   COMPBIAS   1378   1422       Pro-rich.
FT   COMPBIAS   1555   1787       Ser-rich.
FT   MOD_RES      22     22       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NR48}.
FT   MOD_RES     373    373       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9NR48}.
FT   MOD_RES    1160   1160       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1168   1168       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2307   2307       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES    2309   2309       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES    2313   2313       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   CROSSLNK     34     34       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9NR48}.
FT   CROSSLNK    424    424       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9NR48}.
FT   CONFLICT    331    331       L -> M (in Ref. 2; BAC40390).
FT                                {ECO:0000305}.
FT   CONFLICT    711    714       RKGR -> EKEE (in Ref. 4; AAK26242).
FT                                {ECO:0000305}.
FT   CONFLICT   1073   1073       Q -> K (in Ref. 4; AAK26242).
FT                                {ECO:0000305}.
FT   CONFLICT   1095   1095       A -> V (in Ref. 4; AAK26242).
FT                                {ECO:0000305}.
FT   CONFLICT   1994   1994       Y -> S (in Ref. 4; AAK26242).
FT                                {ECO:0000305}.
FT   CONFLICT   2656   2656       D -> H (in Ref. 4; AAK26242).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2958 AA;  331333 MW;  E8CA3E7AB72BEF2B CRC64;
     MDPRNTAMLG LGSDSEGFSR KSPSTINPGT LASKREAEIE GATEEEDPRK RNRERGTEAG
     KEDGSTDAQQ QFSVKETNFS EGNLKLKIGL QAKRTKKPPK NLENYVCRPA IKTTIKHSRK
     ALKSGKMTDE KNEHCPSKWD SSKLFKKAGD ATAIDCQAEE SIHLHSQGES NPLSKKLSPV
     HSQMADYISA APSLVGSRDP DIKDRALLNG GTSVTEKLAQ LIATCPPSKS SKAKPKKLGT
     GTTVGLVSKD LIRKPGVGSI AGIIHKDLIK KPALSTAVGL VTKDPGKKPM FNAAVGLINK
     DSVKKLGTGT TAVFINKDLG KKPGAITTVG LLSKESGKKL GIGIVPGLVN KESGKKLGLG
     TVVGLVNKEL GKKLSSTVGL VAKDVTKKIV ASSAMGLVNK DIGKKLLNCP MAGQLGSKDA
     LNLKSEALLP TQEQLKASCS ANISNHDSQE LPESLKDSAT GKAFEKSVMR HSKESMLEKF
     SVRKEITNLE KEMFNEGTCI QQDNFSSSER GAFETSKHEK QPPVYCTSPD FQIGGASDAS
     TAKSPFSAVG ESNLPSSSPT VSVNPVTRSP PEASSQLVPN PLLLNSTAEQ MEEISESIGK
     SQFTAESTHL NVGHRSLGHS LSIECKGIDK ELNESKNTHL DIPRISSSLG KKPSLTSDSG
     IHAITPSVVN FTSLFSNKPF LKLGAVTAPD KHCQVAESLS SSFQSKPLKK RKGRKPRWTK
     VVARSTCRSP KGLDLERSEL FKNVSCSSLS NSSEPAKFMK TIGASSFVDH DFLKRRLPKL
     SKSSAPSLAL LTDSEKPSHK SFITHKLSSS MCVTSDLLSD IYKPKRGRPK SKEMPQLEGP
     PKRTLKIPAS KVFSLQSKEE QEPPILQPEI EIPSFKQSLS VSPFPKKRGR PKRQMRSPVK
     MKPPVLSVAP FVATESPSKL ESESENHRSS SDFFESEDQL QDTDDLDDSH RQSVCSMSDL
     EMEPDKKISK RNNGQLMKTI IRKINKMKTL KRKKLLNQIL SSSVESSNKG KVQSKLHNTV
     SSLAATFGSK LGQQINVSKK GTIYIGKRRG RKPKTVLNGL LSGSPASLAV LEQTAQQAAG
     SALGQILPPL LPSPASSSEI LPSPICSQSS GTSGGQSPVS SDAGFVEPSS VPYLHVHSRQ
     GSMIQTLAMK KASKGRRRLS PPTLLPNSPS HLSELTSLKE ATPSPVSESH SDETIPSDSG
     IGTDNNSTSD RAEKFCGQKK RRHSFEHISL IPPETSTVLN SLKEKHKHKC KRRSHDYLSY
     DKMKRQKRKR KKKYPQLRNR QDPDFIAELE ELISRLSEIR ITHRSHHFIP RDLLPTIFRI
     NFNSFYTHPS FPLDPLHYIR KPDLKKKRGR PPKMREAMAE MPFMHSLSFP LSSTGFYPSY
     GMPYSPSPLT AAPIGLGYYG RYPPTLYPPP PSPSFTTPLP PPSYMHAGHL LLNPTKYHKK
     KHKLLRQEAF LTTSRTPLLS MSTYPSVPPE MAYGWMVEHK HRHRHKHREH RSEQPQVSMD
     SGSSRSVLES LKRYRFGKDT VGDRYKHKEK HRCHMSCPHL SPSKNLINRE EQWVSREPSE
     SSSLALGLQT PLQIDCSESS PSLSLGGFTP NSEPASSDEH MNLFTSAIGS CRVSNPNSSC
     RKKLTDSPGL FPVQDTALNR PHRKEPLPSS ERAIQSLAGS QSASDKPSQR SSESTNCSPT
     RKRSSSESTS STVNGVPSRS PRLVASMDDS VDSLLQRIVH HDEQESMEKN GDASITTVSA
     PPSSSPGHSY SKERALGKSD SLLVPAVPND SCSNIPLLSE KSASRCSPHH IKRSVVEAMQ
     RQARKMCNYD KILATKKNLD HVNKILKAKK LQRQARTGNN FVKRRPGRPR KCPLQAVVSM
     QAFQAAQFVS PELNEGEDMS LHLSPDTVTD VIEAVVQSVN LTSEHKKGVK RKNWLLEEQT
     RKKQKTVPEE EEQENNKSFI ETPVEIPSPL ETPAEPSEPE NTLQPVLALI PREKKAPRPP
     KKKYQRAGLY SDVYKTIDPK SRLIQLKKEK LEYTPGEHEY GLFPAPIHVG KYLRQKRIDF
     QLPYDILWQW KHNQLYKKPD VPLYKKIRSN VYVDVKPLSG YEATTCNCKK PDDDTRKGCG
     DDCLNRMIFA ECSPNTCPCG EQCCNQRIQR HEWVQCLERF RAEEKGWGIR TKEPLKAGQF
     IIEYLGEVVS EQEFRNRMIE QYHNHSDHYC LNLDSGMVID SYRMGNEARF INHSCDPNCE
     MQKWSVNGVY RIGLYALKDM PAGTELTYDY NFHSFNVEKQ QLCKCGFEKC RGIIGGKSQR
     MNGLPSHKGS QSSSTHRKSA RAKEKRKSKH KLKKRKGHPS EEPSENINTP TRLTPQLQMK
     PMSNRERNFV LKHHVFLVRN WEKIHQKQEE VKHTRDIHSA SLYTRWNGLC RDDGNIKSDV
     FMTQFSALQT ARSVRTRRLA AAEENLEVAR AARLAQIFKE ICDGIISYRD SSQQTLAAPL
     LNLPPKKKNA DYYEKISDPL DLSTIEKQIL IGYYKTVEAF DADMLKVFRN AEKYYGRKSP
     IGRDVCRLRK AYYSARHEAS AQIDEIVGET ASEADSSETS VSEKESGHEK DDDVIRCICG
     LYKDEGLMIQ CDKCMVWQHC DCMGVNTDVE HYLCEQCDPR PVDREVPMIP RPHYAQPGCV
     YFICLLRDDL LLRQGDCVYL MRDSRRTPDG HPVRQSYRLL SHINRDKLDI FRIEKLWKNE
     KEERFAFGHH YFRPHETHHS PSRRFYHNEL FRVPLYEIIP LEAVVGTCCV LDLYTYCKGR
     PKGIKEQDVY ICDYRLDKSA HLFYKIHRNR YPVCTKPYAF DHFPKKLTPK RDFSPHYVPD
     NYKRNGGRSS WKSERSKPPL KDLGQEDDAL PLIEEVLASQ EQAAREVPSP EEPDQERATG
     DIGDAEKKPE ESSQEAQLAS TPEERRHSQR ERLNQILLNL LEKIPGKNAI DVTYLLEEGS
     GRKLRRRTLF IPENSFRK
//
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