GenomeNet

Database: UniProt
Entry: Q6P2L6
LinkDB: Q6P2L6
Original site: Q6P2L6 
ID   NSD3_MOUSE              Reviewed;        1439 AA.
AC   Q6P2L6; Q3TDS4; Q3U0L8; Q3V131; Q8BJT3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   10-APR-2019, entry version 131.
DE   RecName: Full=Histone-lysine N-methyltransferase NSD3;
DE            EC=2.1.1.43;
DE   AltName: Full=Nuclear SET domain-containing protein 3;
DE   AltName: Full=Wolf-Hirschhorn syndrome candidate 1-like protein 1 homolog;
DE            Short=WHSC1-like protein 1;
GN   Name=Nsd3; Synonyms=Whsc1l1;
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 MRNA] (ISOFORMS 2; 3 AND 4).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Spleen, Testis, and Vein;
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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]
RP   PROTEIN SEQUENCE OF 899-914, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver, Spleen, and Testis;
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Histone methyltransferase. Preferentially methylates
CC       'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation, while 'Lys-27' is a mark for transcriptional
CC       repression (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC   -!- SUBUNIT: Interacts with BRD4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6P2L6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P2L6-2; Sequence=VSP_021432, VSP_021435, VSP_021436;
CC       Name=3;
CC         IsoId=Q6P2L6-3; Sequence=VSP_021431, VSP_021437, VSP_021438;
CC         Note=No experimental confirmation available.;
CC       Name=4;
CC         IsoId=Q6P2L6-4; Sequence=VSP_021432, VSP_021433, VSP_021434;
CC         Note=No experimental confirmation available.;
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}.
DR   EMBL; AK079952; BAC37792.1; -; mRNA.
DR   EMBL; AK132725; BAE21322.1; -; mRNA.
DR   EMBL; AK156746; BAE33834.1; -; mRNA.
DR   EMBL; AK170040; BAE41526.1; -; mRNA.
DR   EMBL; AC156990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC064447; AAH64447.1; -; mRNA.
DR   CCDS; CCDS40305.1; -. [Q6P2L6-2]
DR   CCDS; CCDS85518.1; -. [Q6P2L6-4]
DR   RefSeq; NP_001001735.1; NM_001001735.2. [Q6P2L6-2]
DR   RefSeq; NP_001295410.1; NM_001308481.1. [Q6P2L6-2]
DR   RefSeq; NP_001295411.1; NM_001308482.1. [Q6P2L6-4]
DR   UniGene; Mm.217337; -.
DR   ProteinModelPortal; Q6P2L6; -.
DR   SMR; Q6P2L6; -.
DR   BioGrid; 231497; 1.
DR   IntAct; Q6P2L6; 2.
DR   MINT; Q6P2L6; -.
DR   STRING; 10090.ENSMUSP00000115470; -.
DR   iPTMnet; Q6P2L6; -.
DR   PhosphoSitePlus; Q6P2L6; -.
DR   jPOST; Q6P2L6; -.
DR   PaxDb; Q6P2L6; -.
DR   PeptideAtlas; Q6P2L6; -.
DR   PRIDE; Q6P2L6; -.
DR   DNASU; 234135; -.
DR   Ensembl; ENSMUST00000136107; ENSMUSP00000147840; ENSMUSG00000054823. [Q6P2L6-4]
DR   Ensembl; ENSMUST00000146919; ENSMUSP00000115470; ENSMUSG00000054823. [Q6P2L6-2]
DR   Ensembl; ENSMUST00000153597; ENSMUSP00000123028; ENSMUSG00000054823. [Q6P2L6-3]
DR   Ensembl; ENSMUST00000155861; ENSMUSP00000117596; ENSMUSG00000054823. [Q6P2L6-2]
DR   GeneID; 234135; -.
DR   KEGG; mmu:234135; -.
DR   UCSC; uc009lgk.1; mouse. [Q6P2L6-4]
DR   UCSC; uc009lgm.1; mouse. [Q6P2L6-2]
DR   UCSC; uc009lgp.1; mouse. [Q6P2L6-3]
DR   CTD; 54904; -.
DR   MGI; MGI:2142581; Nsd3.
DR   eggNOG; KOG1081; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000155355; -.
DR   HOGENOM; HOG000230893; -.
DR   HOVERGEN; HBG079979; -.
DR   InParanoid; Q6P2L6; -.
DR   KO; K11425; -.
DR   OrthoDB; 507784at2759; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; Whsc1l1; mouse.
DR   PRO; PR:Q6P2L6; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000054823; Expressed in 251 organ(s), highest expression level in mesenteric lymph node.
DR   ExpressionAtlas; Q6P2L6; baseline and differential.
DR   Genevisible; Q6P2L6; MM.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:MGI.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:MGI.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0016571; P:histone methylation; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:2001255; P:positive regulation of histone H3-K36 trimethylation; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 4.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP_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; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF00855; PWWP; 2.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00249; PHD; 5.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00293; PWWP; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; SSF57903; 3.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50812; PWWP; 2.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromatin regulator; Chromosome;
KW   Coiled coil; Complete proteome; Direct protein sequencing;
KW   Isopeptide bond; Metal-binding; Methyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1439       Histone-lysine N-methyltransferase NSD3.
FT                                /FTId=PRO_0000259522.
FT   DOMAIN      270    333       PWWP 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN      960   1025       PWWP 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN     1096   1146       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN     1148   1265       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1272   1288       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING     701    748       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     749    805       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     862    955       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1323   1370       PHD-type 4; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00146}.
FT   COILED     1036   1065       {ECO:0000255}.
FT   MOD_RES     150    150       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   MOD_RES     457    457       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   MOD_RES     585    585       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   MOD_RES     587    587       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   MOD_RES     590    590       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   MOD_RES     655    655       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   MOD_RES     790    790       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   CROSSLNK    218    218       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   CROSSLNK    245    245       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   CROSSLNK    413    413       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   CROSSLNK    502    502       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   CROSSLNK    532    532       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   CROSSLNK    628    628       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   CROSSLNK   1154   1154       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9BZ95}.
FT   VAR_SEQ       1    941       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_021431.
FT   VAR_SEQ     135    135       P -> PLPPPPPPPPP (in isoform 2 and
FT                                isoform 4). {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_021432.
FT   VAR_SEQ     603    611       QVETAPQAS -> QVGFLHVES (in isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_021433.
FT   VAR_SEQ     612   1439       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_021434.
FT   VAR_SEQ     620    645       ASEISDSCKPLKKRSRASTDVETASC -> SADRGAQGSVR
FT                                FSDSSVSAAKEETVD (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_021435.
FT   VAR_SEQ     646   1439       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_021436.
FT   VAR_SEQ     973    975       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_021437.
FT   VAR_SEQ    1199   1209       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_021438.
FT   CONFLICT    122    122       H -> R (in Ref. 1; BAE33834).
FT                                {ECO:0000305}.
FT   CONFLICT    950    950       N -> K (in Ref. 1; BAE21322).
FT                                {ECO:0000305}.
FT   CONFLICT   1149   1149       D -> N (in Ref. 1; BAE21322).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1439 AA;  161002 MW;  917C7ADCD1248525 CRC64;
     MDFSFSFMQG IMGNTIQQPP QLIDSANIRQ EDAFDNHSDI VEDGGPTPFE ATLQQGFQYP
     PTTEDLPPLT NGYPPSISLY ETQTKYPPYN QYPNGSANGF GAVRNFSPTD YYHSEIPNTR
     PHEILEKPSP PQPPPPPSVP QTVIPKKTGS PEIKLKITKT IQNGRELFES SLCGDLLNEV
     QASEHTKSKH ESRKEKRKKS NRHESSRSEE RRSHKIPKLE PEGQNRPNER VDTAPEKPRE
     EPVLKEAIPV QPILSSVPTT ETSTGVKFQV GDLVWSKVGT YPWWPCMVSS DPQLEVHSKI
     NTRGAREYHV QFFSNQPERA WVHEKRVREY KGHEQYEELL AEAAKQASNH SEKQKIRKPR
     PQRERAQWDI GIAHAEKALK MTREERVEQY TFIYIDKQPE EASSQAKKNV TSKTEVKKPR
     RPRSVLNSQP EQTNAGEVAS SQSSTDLRRQ SQRRHTSLEE EEPPPVKIAW KTAAARKSLP
     ASITMHKGSL DLQKCNMSPV VKIEQVFALQ NATGDGKFID QFVYSTKGIG NKTEISVRGQ
     DRLIISSPSQ RSEKPAQSAS SPEATSGSAG PVEKKQQRRS IRTRSESEKS AEVVPKKKIK
     KEQVETAPQA SLKTGLQKGA SEISDSCKPL KKRSRASTDV ETASCTYRDT SDSDSRGLSD
     GQVGFGKQVD SPSATADADA SDAQSVDSSL SRRGVGTSKK DTVCQVCEKA GDCLVACEGE
     CCRHFHVECL GLTAVPEGHF TCEECETGQH PCFSCKVSGK DVKRCSVSVC GKFYHEACVR
     KFPTAIFESK GFRCPQHCCS SCSMEKDIHK ASKGRMMRCL RCPVAYHVGD ACVAAGSVSV
     SSHILICSNH SKRSSQSAAI NVGFCFVCAR GLIVQDHSDP MFSSYAYKSH YLLSESNRAE
     LMKLPMIPSS SASKKRCEKG GRLLCCESCP ASFHPECLSI DMPEGCWNCN DCKAGKKLHY
     KQIVWVKLGN YRQVLWWPAE ICSPRSVPLN IQGLKHDLGD FPVFFFGSHD YYWVHQGRVF
     PYVEGDKHFA EGQTSINKTF KKALEEAAKR FQELKAQRES KEALEMERTS RKPPPYKHIK
     ANKVIGKVQV QVADLSEIPR CNCKPGDENP CGLESQCLNR MSQYECHPQV CPAGDRCQNQ
     CFTKRLYPDA EVIKTERRGW GLRTKRSIKK GEFVNEYVGE LIDEEECRLR IKRAHENSVT
     NFYMLTVTKD RIIDAGPKGN YSRFMNHSCN PNCETQKWTV NGDVRVGLFA LCDIPAGMEL
     TFNYNLDCLG NGRTVCHCGA DNCSGFLGVR PKSACTSAVD EKTKNAKLKK RRKVKAEAKP
     IHEDYCFQCG DGGELVMCDK KDCPKAYHLL CLNLTQPPHG KWECPWHRCD ECGSVAVSFC
     EFCPHSFCKA HGKGALVPSA LEGRLCCSSH DPASPVSPEY WSKIRCKWES QDSGEEVKE
//
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