GenomeNet

Database: UniProt
Entry: Q6PDK2
LinkDB: Q6PDK2
Original site: Q6PDK2 
ID   KMT2D_MOUSE             Reviewed;        5588 AA.
AC   Q6PDK2;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   10-APR-2019, entry version 131.
DE   RecName: Full=Histone-lysine N-methyltransferase 2D;
DE            Short=Lysine N-methyltransferase 2D;
DE            EC=2.1.1.43;
DE   AltName: Full=ALL1-related protein;
DE   AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 2;
GN   Name=Kmt2d; Synonyms=Mll2, Mll4;
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 4339-5588.
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4789, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1627, AND IDENTIFICATION
RP   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727; THR-1223; SER-1226;
RP   SER-1627; THR-1822; SER-2266; SER-2299; SER-2597; SER-4410 AND
RP   SER-4789, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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   [6]
RP   IDENTIFICATION IN THE MLL COMPLEX, AND INTERACTION WITH ASH2L; DPY30;
RP   KMT2A; RRBP5 AND WDR5.
RX   PubMed=21335234; DOI=10.1016/j.cell.2011.01.020;
RA   Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.;
RT   "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4
RT   methylation within bivalent domains.";
RL   Cell 144:513-525(2011).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3071, 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).
RN   [8]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2492; ARG-2829; ARG-3725 AND
RP   ARG-4255, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.O113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
RA   Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA   Vemulapalli V., Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone
CC       H3 (H3K4me). H3K4me represents a specific tag for epigenetic
CC       transcriptional activation. Acts as a coactivator for estrogen
CC       receptor by being recruited by ESR1, thereby activating
CC       transcription (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 ESR1; interaction is direct (By
CC       similarity). Component of the MLL2/3 complex (also named ASCOM
CC       complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L,
CC       RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and
CC       alpha- and beta-tubulin. {ECO:0000250,
CC       ECO:0000269|PubMed:21335234}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: LXXLL motifs 5 and 6 are essential for the association
CC       with ESR1 nuclear receptor. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- CAUTION: Human protein KMT2B/MLL4 was first named MLL2 (see AC
CC       Q9UMN6). Thus, also mouse Mll4 is often referred to as Mll2 and
CC       vice versa in the literature. {ECO:0000305}.
DR   EMBL; AC161165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC058659; AAH58659.1; -; mRNA.
DR   CCDS; CCDS49725.2; -.
DR   UniGene; Mm.264889; -.
DR   ProteinModelPortal; Q6PDK2; -.
DR   SMR; Q6PDK2; -.
DR   IntAct; Q6PDK2; 3.
DR   STRING; 10090.ENSMUSP00000023741; -.
DR   iPTMnet; Q6PDK2; -.
DR   PhosphoSitePlus; Q6PDK2; -.
DR   EPD; Q6PDK2; -.
DR   jPOST; Q6PDK2; -.
DR   MaxQB; Q6PDK2; -.
DR   PaxDb; Q6PDK2; -.
DR   PeptideAtlas; Q6PDK2; -.
DR   PRIDE; Q6PDK2; -.
DR   Ensembl; ENSMUST00000178486; ENSMUSP00000135941; ENSMUSG00000048154.
DR   MGI; MGI:2682319; Kmt2d.
DR   eggNOG; KOG4443; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000156707; -.
DR   HOGENOM; HOG000168503; -.
DR   InParanoid; Q6PDK2; -.
DR   OMA; HLRIPPQ; -.
DR   PhylomeDB; Q6PDK2; -.
DR   Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   ChiTaRS; Kmt2d; mouse.
DR   PRO; PR:Q6PDK2; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000048154; Expressed in 242 organ(s), highest expression level in mesenteric lymph node.
DR   ExpressionAtlas; Q6PDK2; baseline and differential.
DR   Genevisible; Q6PDK2; MM.
DR   GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR   GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
DR   GO; GO:0006342; P:chromatin silencing; IMP:UniProtKB.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IMP:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0001555; P:oocyte growth; IMP:UniProtKB.
DR   GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 6.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR037890; KMT2D.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22884:SF380; PTHR22884:SF380; 2.
DR   Pfam; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF00628; PHD; 3.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM00249; PHD; 7.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00184; RING; 6.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   SUPFAM; SSF57903; SSF57903; 5.
DR   PROSITE; PS51805; EPHD; 2.
DR   PROSITE; PS51543; FYRC; 1.
DR   PROSITE; PS51542; FYRN; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 5.
DR   PROSITE; PS50016; ZF_PHD_2; 4.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Coiled coil; Complete proteome;
KW   Isopeptide bond; Metal-binding; Methylation; Methyltransferase;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   5588       Histone-lysine N-methyltransferase 2D.
FT                                /FTId=PRO_0000401938.
FT   REPEAT      442    446       1.
FT   REPEAT      460    464       2.
FT   REPEAT      469    473       4.
FT   REPEAT      477    481       5.
FT   REPEAT      520    524       7.
FT   REPEAT      529    533       8.
FT   REPEAT      538    542       9.
FT   REPEAT      547    551       10.
FT   REPEAT      574    578       11.
FT   REPEAT      583    587       12.
FT   REPEAT      592    596       13.
FT   REPEAT      610    614       14.
FT   REPEAT      637    641       15.
FT   DOMAIN     5226   5286       FYR N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00875}.
FT   DOMAIN     5287   5372       FYR C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00876}.
FT   DOMAIN     5448   5564       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     5572   5588       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING     104    149       C2HC pre-PHD-type 1; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01146}.
FT   ZN_FING     170    218       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   ZN_FING     226    276       PHD-type 2; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00146}.
FT   ZN_FING     229    274       RING-type 1; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   ZN_FING     270    323       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     276    321       RING-type 2; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   ZN_FING    1071   1124       PHD-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1121   1171       PHD-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1198   1253       PHD-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1201   1251       RING-type 3; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   ZN_FING    4829   4874       RING-type 4; degenerate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   ZN_FING    5080   5120       C2HC pre-PHD-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01146}.
FT   ZN_FING    5141   5188       PHD-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   REGION      439    642       15 X 5 AA repeats of S/P-P-P-E/P-E/A.
FT   REGION     5525   5526       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COILED     2627   2665       {ECO:0000255}.
FT   COILED     2768   2813       {ECO:0000255}.
FT   COILED     3559   3613       {ECO:0000255}.
FT   COILED     3712   3747       {ECO:0000255}.
FT   COILED     3854   3883       {ECO:0000255}.
FT   COILED     3912   4052       {ECO:0000255}.
FT   MOTIF      2644   2648       LXXLL motif 1.
FT   MOTIF      3030   3034       LXXLL motif 2.
FT   MOTIF      4279   4293       LXXLL motif 3.
FT   MOTIF      4310   4314       LXXLL motif 4.
FT   MOTIF      4514   4518       LXXLL motif 5.
FT   MOTIF      5041   5045       LXXLL motif 6.
FT   COMPBIAS   1307   1311       Poly-Glu.
FT   COMPBIAS   2064   2583       Pro-rich.
FT   COMPBIAS   2610   2613       Poly-Ser.
FT   COMPBIAS   2769   2812       Gln-rich.
FT   COMPBIAS   2813   2819       Poly-Ala.
FT   COMPBIAS   3255   4332       Gln-rich.
FT   COMPBIAS   4841   4844       Poly-Ala.
FT   COMPBIAS   4960   5028       Pro-rich.
FT   METAL      5528   5528       Zinc. {ECO:0000250}.
FT   METAL      5576   5576       Zinc. {ECO:0000250}.
FT   METAL      5578   5578       Zinc. {ECO:0000250}.
FT   METAL      5583   5583       Zinc. {ECO:0000250}.
FT   BINDING    5502   5502       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES     727    727       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1107   1107       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    1205   1205       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    1223   1223       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1226   1226       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1562   1562       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    1627   1627       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1791   1791       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    1822   1822       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2196   2196       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    2197   2197       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    2203   2203       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    2217   2217       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    2231   2231       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    2266   2266       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2268   2268       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    2299   2299       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2492   2492       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    2597   2597       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2829   2829       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    3071   3071       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES    3122   3122       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    3193   3193       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    3430   3430       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    3725   3725       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    4255   4255       Asymmetric dimethylarginine.
FT                                {ECO:0000244|PubMed:24129315}.
FT   MOD_RES    4272   4272       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    4410   4410       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    4516   4516       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   MOD_RES    4789   4789       Phosphoserine.
FT                                {ECO:0000244|PubMed:16452087,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES    4827   4827       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   CROSSLNK   4807   4807       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:O14686}.
FT   CROSSLNK   4931   4931       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:O14686}.
SQ   SEQUENCE   5588 AA;  600245 MW;  37A0E5D319A5F1A6 CRC64;
     MDSQKPPAED KDSDPAADGL AAPEKPGATE PDLPILCIGE VSVPGSGGSR PQKPPHDCSR
     GPARRCALCN CGEPGLHGQR ELQRFELPSD WPGFPVVPSG GNSGPCEAVL PKEDASQIGF
     PEGLTPAHLG EPGGHCWAHH WCAAWSAGVW GQEGPELCGV DKAIFSGISQ RCSHCARFGA
     SVPCRSPGCS RLYHFPCATA SGSFLSMKTL QLLCPEHSDG AAHLEEARCA VCEGPGQLCD
     LLFCTSCGHH YHGACLDTAL TARKRASWQC PECKVCQSCR KPGNDSKMLV CETCDKGYHT
     FCLKPPMEDL PAHSWKCKTC RLCRACGAGS AELNPNSEWF ENYSLCHRCH KAQGSQPVTS
     VAEQHPAVCS RLSPPEPGEI PIDAPDALYV ACQGQPKGGH VTSMQPKELA PLQCEAKPLG
     RAGTQLEAQL EAPLHEEMPL LPPPEESPLS PPPEESPTSP PPEASRLSPP TEESPLSPPP
     ESSPFSPLEG CPPSPALDTP LSPPPEASPL SPPFEESPLS PPPEELPSSP PPEASRLSPP
     PEESPMSPPP EESPMSPPPE ASRLFPPFEE SPLSPPPEDS PLSPPPEASR LSPPPEDSPM
     SPPPEDSPMS PPPEVSRFLP LPVLSHLSPL PEVSRLSPPP EESPLSPPPE DSPASPPPEA
     SRLSPPPEDS PASPPPEASR LSRPREDSPA SPPPEDSLVS LPMEESPLSP LPEELRLCPQ
     PEEPYLSPQP EEPRLCPQPE ELPLSPQSEE PCLSPVLVEP GPSSQPEEPH LSPVPQEPHL
     SPQPEEPHLS PQPQQLHLSP HSEEPCLSPM PEEPCLSPQP EELNGPPQPA EPPEEPSQSS
     APKELSLFSP SGEPPLPPML GEPALSEPGE PPLSPLPEEL PLSLSGEPVL SPQLMPPDPL
     PPPLSPIIPA AAPPALSPLG ELEYPFGAKG DSDPESPLAA PILETPISPP PEANCTDPEP
     VPPMILPPSP GSPLGPASPI LMERLPPPCS PLLPHSLPPP TPPPSHCSPP ALPLSVPSPL
     SPVQKAVDVS DEAELHEMET DKGPEPECPA LEPRATSPLP SPLGDLSCPA PSPAPALDDF
     SGLGEDTAPL DGTGQMSGSL AGELKGSPVL LDPEELTPVT PMEVYGPECK QAGQGSPCEE
     QEEPGAPMAP MPPTLIKSDI VNEISNLSQG DASASFPGSE PLLGSPDPEG GGSLSMELGV
     STDVSPARDE GSLRLCTDSL PETDDSLLCD TGTATSGGKA EGDKGRRRSS PARSRIKQGR
     SSSFPGRRRP RGGAAHGGRG RGRARLKSTT SSVETLVADI DSSPSKEEEE EDDDTMQNTV
     VLFSNTDKFV LMQDMCVVCG SFGRGAEGHL LACSQCSQCY HPYCVNSKIT KVMLLKGWRC
     VECIVCEVCG QASDPSRLLL CDDCDISYHT YCLDPPLLTV PKGGWKCKWC VSCMQCGAAS
     PGFHCEWQNS YTHCGPCASL VTCPVCHAPY VEEDLLIQCR HCERWMHAGC ESLFTEDEVE
     QAADEGFDCV SCQPYVVKPV VPVAPPELVP VKVKEPEPQF FRFEGVWLTE TGMAVLRNLT
     MSPLHKRRQR RGRLGLPGEA GLEGSEPSDA LGPDDKKDGD LDTDDLLKGE GGVEQMECEI
     KLEGPASPDV ELGKEETEES KKRKRKPYRP GIGGFMVRQR KSHTRVKRGP AAQAEVLSGD
     GQPDEVMPAD LPAEGSVEQS LAEGDEKKKQ QRRARKKSKL EDMFPAYLQA AFFGKDLLDL
     SRKALFAVGV GRPGFGLGAS KPRADGGSDR KELMTAMHKG DDGPDVADEE SHGPEGTADL
     PGLEDGGVKA SPVPSDPEKP GTPGEGVLSS DLDRIPTEEL PKMESKDLQQ LFKDVLGSER
     EQHLGCGTPG LEGGRTSLQR PFLQGGLALG SLPSSSPMDS YPGLCQSPFL DSRERGGFFS
     PEPGEPDSPW TGSGGTTPST PTTPTTEGEG DGLSYNQRSL QRWEKDEELG QLSTISPVLY
     ANINFPNLKQ DYPDWSSRCK QIMKLWRKVP AADKAPYLQK AKDNRAAHRI SKVQKQAESQ
     ISKQAKMGDI ARKTDRPALH LRIPSQPGAL GSPPPAAAPT IFLGSPTTPA GLSTSADGFL
     KPPAGTVPGP DSPGELFLKL PPQVPAQVPS QDPFGLAPAY APEPRFSAAP PTYPPYPSPT
     GAPAQPPMLG TTTRPGTGQP GEFHTTPPGT PRHQPSTPDP FLKPRCPSLD NLAVPESPGV
     AGGKASEPLL SPPPFGESRK SLEVKKEELG ASSPGYGPPN LGCVDSPSAG PHLGGLELKA
     PDVFKAPLTP RASQVEPQSP GLGLRAQEPP PAQALAPSPP SHPDVFRSGP YPDPYAQPPL
     TPRPQPPPPE SCCAPPPRSL PSDPFSRVPA SPQSQSSSQS PLTPRPLSAE AFCPSPVTPR
     FQSPDPYSRP PSRPQSRDPF APLHKPPRPQ PPEVAFKAGP LAHTPLGAGG FPAALPSGPA
     GELHAKVPSG QPTNFARSPG TGTFVGTPSP MRFTFPQGVG EPSLKPPVPQ PGLPSPHGIN
     SHFGPGPTLG KPQSTNYAVA TGNFHPSGSP LGPNSGPTGE GYGLSPLRPA SVLPPPAPDG
     SLPYLTHGAS QRVGITSPVE KREDPGATMS SSSLATPELS SAQDAGISSL SQTELEKQRQ
     RQRLRELLIR QQIQRNTLRQ EKETAAAAAG AVGPPGNWGA EPSSPAFEQL SRGQTPFTGS
     QDRSSIVGLP ASKLGGPTLG PGAFSSDDRL ARPLPPATPS SMDMNSRQLV GGSQAFYQRT
     PYPGSLPLQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQLWQ QQQQQQQQQQ QQAAAAAAAT
     SMRLAMSARF PSTPGPELGR QALGSPLAGI PTRLPGPAEP VPGPAGPAQF IELRHNVQKG
     LGPGVSPFPG QGPPQRPRFY PVSEELHRLA PEGLRGLAVP GLPSQKPSAL PAPELNNSLH
     QTPHAKGPAL ASGLELVSRP PSNTELSRPP LALEAGKLPC EDPELDDDFD AHKALEDDEE
     LAHLGLGVDV AKGDDELGTL ENLETNDPHL DDLLNGDEFD LLAYTDPELD TGDKKDIFNE
     HLRLVESANE KAEREALLRG VEPVSLGPEE RPPPAPDNSE PRLTSVLPEV KPKVEEGGRH
     PSPCQFTINT PKVEPAPPAT SLSLGLKPGQ TVMGTRDTRG GVGTGSFPSS GHTAEKGPFG
     ATGGTPAHLL NPSSLSGPAA SSLLEKFELE SGALTLPSGH AAAGDELDKM ESSLVASELP
     LLIEDLLEHE KKELQKKQQL SAQTVLPAQQ QQQQQQQQQQ QQQQHTLLPT PGPAQALPLP
     HEPGPPQQLA LGIGSTRQPG LGQSMVPIQP PAHALQQRLA PSVAMVSNQG HMLSGQQAGQ
     TGLVPQQSSQ PVLAQKPMSA MPASMCMKPQ QLAMQQQQLA NSFFPDTDLD KFAAEDIIDP
     IAKAKMVALK GIKKVMAQGS IGVAPGMNRQ QVSLLAQRLS GGSGSDLQNH VAPGSGQERN
     AGDPAQPRPN PPTFAQGVIN EADQRQYEEW LFHTQQLLQM QLKVLEEQIG VHRKSRKALC
     AKQRTAKKAG REFPEADAEK LKLVTEQQSK IQKQLDQVRK QQKEHTNLMA EYRNKQQQQQ
     QQQQQQQQQQ HSAVLAVSPS QNPRVLTKLP GQLLPAHGLQ PPQAPPGGQA GGLRLPPGGM
     VLPGQSGGPF LNTTLAQQQQ QQHSGVAGSL TGPPGSFFPG NLALRSLGPD SRLLQERQLQ
     LQQQRMQLAQ KLQQQQQQQQ QQQQQQHLLG QVAIQQQQGP GVQNQALGPK PQGLLPPSNH
     QGLLVQQLSP QQSQGSQGLL GPAQVTVLQQ QQQQQQHSGA LGPQGPHRQV LMTQSRVLSS
     PQLAQQGHSL MGHRLLTAQQ QQQQQQQQQQ QQQQQQQQQQ QQQGSMTGLS QLQQGMMSHG
     GQPKMSAQAL GSLQQQQQQL QQQQMLQQQQ LQQQQQQLQQ QQQQQQLQQQ QQQQLQLQQQ
     QQQQQQHLQH QQQQQQQLQQ QQQLQQQQQQ QLHLQQQLHQ QQQLQLQQQQ MGLLNQNRTL
     LSPQQQQQQQ QQQQQQQQQQ QQQQQQQQQV TLGPGLPVKP LQHFSSSGAL GPTLLLTGKE
     QNNAETALPS EVTEGPSTHQ GGPPAVGTAP EPMSVEPGEV KPSISGDSQL LLVQSQAQSQ
     ATSVQLQPPL RLPGQPQPQV NLLHTAGGGS HGQQLGSGSS SESPAVPHLL AQPSVSLGEQ
     PGPMAQNLLG SQQPLGLDRP IQNNTGSQPP KSGPAPQSGQ GPPGAGVMPT VGQLRAQLQG
     VLAKNPQLRH LSPQQQQQLQ ALLMQRQLQQ SQAVRQTPPF QEPGTQPSPL QGLLGCQPQP
     GGFSVSQTGP LQELGAGSRP QGPPRLPVPQ GALSTGPVLG PAHPTPPPSS PQEPKRPSQL
     PSPSAQLTPT HPGTPKPQGP ALELPPGRVS PAAAQLADTF FGKGLGPWDP SDNLTEAQKP
     EQSSLVPGHL DQVNGQVVHE PSQLSIKQEP REEPCALGAQ TVKREANGEP AGAPGTSNHL
     LLAGSRSEAG HLLLQKLLRA KNVQLGAGRG PEGLRAEING HIDSKLSGLE QKLQGTSSNK
     EDAATRKPLP AKPKRVQKTS DRLPSSRKKL RKEDGVRANE ALLKQLKQEL SQLPLTEPTI
     TANFSLFAPF GSGCLVSGQS QLRGAFGSGA LHTGPDYYSQ LLTKNNLSNP PTPPSSLPPT
     PPPSVQQKMV NGVTPSDELG ERPKDTASAQ DSEGALRDAA EVKSLDLLAA LPTPPHNQTE
     DVRMESDEDS DSPDSIVPAS SPESILGEEA PRFPQLGSGR WEQDNRALSP VIPIIPRTGI
     PVFPDTKPYG VLDLEVPGKL PATAWEKGKG SEVSVMLTVS AAAAKNLNGV MVAVAELLSM
     KIPNSYEVLF PDGPARAGLE PKKGEAEGPG GKEKGLSGKG PDTGPDWLKQ FDAVLPGYTL
     KSQLDILSLL KQESPAPEPS IQHSYTYNVS NLDVRQLSAP PPEEPSPPPS PLAPSPASPP
     AEPMVELQAE RPAEPPIPSP LPLASSPESA RPKPRARPPE ESEDSRPPRL KKWKGVRWKR
     LRLLLTIQKG SGHQEDEREV AEFMEQFGTA LRPSKVPRDN RRCCFCHEEG DGATDGPARL
     LNLDLDLWVH LNCALWSTEV YETQGGALMN VEVALHRGLL TKCSLCQRTG ATSSCNRMRC
     PNVYHFACAI RAKCMFFKDK TMLCPVHKIK GPCEQELSSF AVFRRVYIER DEVKQIASII
     QRGERLHMFR VGGLVFHAIG QLLPHQMADF HSATALYPVG YEATRIYWSL RTNNRRCCYR
     CSISENNGRP EFVIKVIEQG LEDLVFTDAS PQAVWNRIIE PVAAMRKEAD MLRLFPEYLK
     GEELFGLTVH AVLRIAESLP GVESCQNYLF RYGRHPLMEL PLMINPTGCA RSEPKILTHY
     KRPHTLNSTS MSKAYQSTFT GETNTPYSKQ FVHSKSSQYR RLRTEWKNNV YLARSRIQGL
     GLYAAKDLEK HTMVIEYIGT IIRNEVANRR EKIYEEQNRG IYMFRINNEH VIDATLTGGP
     ARYINHSCAP NCVAEVVTFD KEDKIIIISS RRIPKGEELT YDYQFDFEDD QHKIPCHCGA
     WNCRKWMN
//
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