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Database: UniProt
Entry: O08550
LinkDB: O08550
Original site: O08550 
ID   KMT2B_MOUSE             Reviewed;        2713 AA.
AC   O08550; E9QKF4; Q5NU09;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   13-FEB-2019, entry version 151.
DE   RecName: Full=Histone-lysine N-methyltransferase 2B;
DE            Short=Lysine N-methyltransferase 2B;
DE            EC=2.1.1.43;
DE   AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 4 homolog;
DE   AltName: Full=Trithorax homolog 2;
DE   AltName: Full=WW domain-binding protein 7;
DE            Short=WBP-7;
GN   Name=Kmt2b; Synonyms=Mll2, Trx2, Wbp7;
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].
RA   Yoshida K.;
RT   "Murine MLL2 gene and its expression.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 [MRNA] OF 379-657.
RX   PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
RA   Bedford M.T., Chan D.C., Leder P.;
RT   "FBP WW domains and the Abl SH3 domain bind to a specific class of
RT   proline-rich ligands.";
RL   EMBO J. 16:2376-2383(1997).
RN   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-114; SER-118;
RP   SER-1037; SER-1040; SER-1098; SER-1101; THR-2064 AND SER-2346, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, 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   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20808952; DOI=10.1371/journal.pbio.1000453;
RA   Andreu-Vieyra C.V., Chen R., Agno J.E., Glaser S., Anastassiadis K.,
RA   Stewart A.F., Matzuk M.M.;
RT   "MLL2 is required in oocytes for bulk histone 3 lysine 4
RT   trimethylation and transcriptional silencing.";
RL   PLoS Biol. 8:1657-1680(2010).
CC   -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone
CC       H3. H3 'Lys-4' methylation represents a specific tag for
CC       epigenetic transcriptional activation. Plays a central role in
CC       beta-globin locus transcription regulation by being recruited by
CC       NFE2 (By similarity). Plays an important role in controlling bulk
CC       H3K4me during oocyte growth and preimplantation development.
CC       Required during the transcriptionally active period of oocyte
CC       growth for the establishment and/or maintenance of bulk H3K4
CC       trimethylation (H3K4me3), global transcriptional silencing that
CC       preceeds resumption of meiosis, oocyte survival and normal zygotic
CC       genome activation. {ECO:0000250, ECO:0000269|PubMed:20808952}.
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: Component of the menin-associated histone
CC       methyltransferase complex, at least composed of KMT2B/MLL4, ASH2L,
CC       RBBP5, WDR5, DPY30, MEN1; the complex interacts with POLR2A and
CC       POLR2B via MEN1. Interacts with NFE2. Interacts with KDM6B.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Females are infertile due to anovulation and
CC       follicle loss. Oocytes show reduced H3K4me3 but not H3K4me1,
CC       abnormal expression of pro-apoptotic genes and Iap elements (which
CC       may contribute to oocyte death and, ultimately, follicle loss) and
CC       fail to establish transcriptional repression.
CC       {ECO:0000269|PubMed:20808952}.
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: The human ortholog, KMT2B/MLL4, was first named MLL2 (see
CC       AC Q9UMN6). Thus, mouse Kmt2b/Mll4 is also often referred to as
CC       Mll2 and vice versa in the literature. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC53192.1; Type=Miscellaneous discrepancy; Note=Possible contaminating sequence. The N-terminal 3 residues and C-terminal 8 residues do not match the underlying genomic sequence.; Evidence={ECO:0000305};
DR   EMBL; AB182318; BAD81031.1; -; mRNA.
DR   EMBL; AC167970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U92455; AAC53192.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS21101.1; -.
DR   RefSeq; NP_083550.2; NM_029274.2.
DR   UniGene; Mm.168688; -.
DR   ProteinModelPortal; O08550; -.
DR   SMR; O08550; -.
DR   BioGrid; 217461; 3.
DR   CORUM; O08550; -.
DR   IntAct; O08550; 1.
DR   MINT; O08550; -.
DR   STRING; 10090.ENSMUSP00000103789; -.
DR   iPTMnet; O08550; -.
DR   PhosphoSitePlus; O08550; -.
DR   EPD; O08550; -.
DR   jPOST; O08550; -.
DR   MaxQB; O08550; -.
DR   PaxDb; O08550; -.
DR   PRIDE; O08550; -.
DR   Ensembl; ENSMUST00000108154; ENSMUSP00000103789; ENSMUSG00000006307.
DR   GeneID; 75410; -.
DR   KEGG; mmu:75410; -.
DR   UCSC; uc009gfg.1; mouse.
DR   CTD; 9757; -.
DR   MGI; MGI:109565; Kmt2b.
DR   eggNOG; KOG1084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000161496; -.
DR   HOGENOM; HOG000015326; -.
DR   HOVERGEN; HBG100043; -.
DR   InParanoid; O08550; -.
DR   KO; K14959; -.
DR   OrthoDB; 738155at2759; -.
DR   TreeFam; TF319820; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   PRO; PR:O08550; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000006307; Expressed in 245 organ(s), highest expression level in secondary oocyte.
DR   ExpressionAtlas; O08550; baseline and differential.
DR   Genevisible; O08550; MM.
DR   GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016458; P:gene silencing; IMP:MGI.
DR   GO; GO:0051568; P:histone H3-K4 methylation; ISO:MGI.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:MGI.
DR   GO; GO:0034968; P:histone lysine methylation; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0009994; P:oocyte differentiation; IMP:MGI.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR   GO; GO:0030728; P:ovulation; IMP:MGI.
DR   GO; GO:0051569; P:regulation of histone H3-K4 methylation; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 3.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR016569; MeTrfase_trithorax.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR002857; Znf_CXXC.
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; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00249; PHD; 4.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; SSF57903; 2.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51543; FYRC; 1.
DR   PROSITE; PS51542; FYRN; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 3.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Complete proteome; DNA-binding;
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   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q9UMN6}.
FT   CHAIN         2   2713       Histone-lysine N-methyltransferase 2B.
FT                                /FTId=PRO_0000124882.
FT   DOMAIN     1733   1789       FYR N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00875}.
FT   DOMAIN     2409   2490       FYR C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00876}.
FT   DOMAIN     2573   2689       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     2697   2713       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DNA_BIND     37     44       A.T hook 1.
FT   DNA_BIND    110    117       A.T hook 2.
FT   DNA_BIND    357    365       A.T hook 3.
FT   ZN_FING     964   1011       CXXC-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00509}.
FT   ZN_FING    1207   1258       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1255   1309       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1341   1402       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1584   1624       C2HC pre-PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   ZN_FING    1645   1692       PHD-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   REGION     2650   2651       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COMPBIAS      6    106       Gly-rich.
FT   COMPBIAS    272    300       Gly-rich.
FT   COMPBIAS    347    410       Glu-rich.
FT   COMPBIAS    414    776       Pro-rich.
FT   COMPBIAS   1814   2296       Pro-rich.
FT   METAL      2653   2653       Zinc. {ECO:0000250}.
FT   METAL      2701   2701       Zinc. {ECO:0000250}.
FT   METAL      2703   2703       Zinc. {ECO:0000250}.
FT   METAL      2708   2708       Zinc. {ECO:0000250}.
FT   BINDING    2583   2583       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    2585   2585       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    2627   2627       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    2702   2702       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   MOD_RES     113    113       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     114    114       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     118    118       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     826    826       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   MOD_RES     849    849       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   MOD_RES     866    866       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   MOD_RES     941    941       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   MOD_RES    1037   1037       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1040   1040       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1098   1098       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1101   1101       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1926   1926       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   MOD_RES    1932   1932       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   MOD_RES    2064   2064       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    2079   2079       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   MOD_RES    2286   2286       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   MOD_RES    2346   2346       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CROSSLNK    810    810       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   CROSSLNK   1142   1142       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9UMN6}.
FT   CONFLICT     18     18       G -> V (in Ref. 1; BAD81031).
FT                                {ECO:0000305}.
FT   CONFLICT     25     27       RGS -> LGC (in Ref. 1; BAD81031).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2713 AA;  294821 MW;  2AD4343C5C081933 CRC64;
     MAAAAGGGSC PGPGSARGRF PGRPRGSGGG GGRGGRGNGA ERVRVALRRG GGAAGPGGAE
     PGEDTALLRL LGLRRGLRRL RRLWAGARVQ RGRGRGRGRG WGPNRGCMPE EESSDGESEE
     EEFQGFHSDE DVAPSSLRSA LRSQRGRAPR GRGRKHKTTP LPPRLADVTP VPPKAPTRKR
     GEEGTERMVQ ALTELLRRSQ APQPPRSRAR AREPSTPRRS RGRPPGRPAG PCRKKQQAVV
     LAEAAVTIPK PEPPPPVVPV KNKAGSWKCK EGPGPGPGTP KRGGQPGRGG RGGRGRGRGG
     LPLMIKFVSK AKKVKMGQLS QELESGQGHG QRGESWQDAP QRKDGDEPER GSCRKKQEQK
     LEEEEEEEEK EGEEKEEKDD NEDNNKQEEE EETERAVAEE EAMLAKEKEE AKLPSPPLTP
     PVPSPPPPLP PPSTSPPPPA SPLPPPVSPP PPLSPPPYPA PEKQEESPPL VPATCSRKRG
     RPPLTPSQRA EREAARSGPE GTLSPTPNPS TTTGSPLEDS PTVVPKSTTF LKNIRQFIMP
     VVSARSSRVI KTPRRFMDED PPKPPKVEAS IVRPPVATSP PAPQEPVPVS SPPRVPTPPS
     TPVPLPEKRR SILREPTFRW TSLTRELPPP PPAPPPAPSP PPAPATPSRR PLLLRAPQFT
     PSEAHLKIYE SVLTPPPLGA LETPEPELPP ADDSPAEPEP RAVGRTNHLS LPRFVPVVTS
     PVKVEVPPHG APALSEGQQL QLQQPPQALQ TQLLPQALPP QQPQAQPPPS PQHTPPLEKA
     RVASLGSLPL SGVEEKMFSL LKRAKVQLFK IDQQQQQKVA ASMPLSPAVQ TEEAVGTVKQ
     TPDRGCVRSE DESMEAKRDR ASGPESPLQG PRIKHVCRHA AVALGQARAM VPEDVPRLSA
     LPLRDRQDLA TEDTSSASET ESVPSRSQRE KVESAGPGGD SEPTGSTGAL AHTPRRSLPS
     HHGKKMRMAR CGHCRGCLRV QDCGSCVNCL DKPKFGGPNT KKQCCVYRKC DKIEARKMER
     LAKKGRTIVK TLLPWDSDES PEASPGPPGP RRGAGAGGSR EEVGATPGPE EQDSLLLQRK
     SARRCVKQRP SYDVFEDSDD SEPGGPPAPR RRTPREHELP VLEPEEQSRP RKPTLQPVLQ
     LKARRRLDKD ALAPGPFASF PNGWTGKQKS PDGVHRVRVD FKEDCDLENV WLMGGLSVLT
     SVPGGPPMVC LLCASKGLHE LVFCQVCCDP FHPFCLEEAE RPSPQHRDTW CCRRCKFCHV
     CGRKGRGSKH LLECERCRHA YHPACLGPSY PTRATRRRRH WICSACVRCK SCGATPGKNW
     DVEWSGDYSL CPRCTELYEK GNYCPICTRC YEDNDYESKM MQCAQCDHWV HAKCEGLSDE
     DYEILSGLPD SVLYTCGPCA GATQPRWREA LSGALQGGLR QVLQGLLSSK VAGPLLLCTQ
     CGQDGKQLHP GPCDLQAVGK RFEEGLYKSV HSFMEDVVAI LMRHSEEGET PERRAGSQMK
     GLLLKLLESA FCWFDAHDPK YWRRSTRLPN GVLPNAVLPP SLDHVYAQWR QQESETPESG
     QPPGDPSAAF QSKDPAAFSH LDDPRQCALC LKYGDADSKE AGRLLYIGQN EWTHVNCAIW
     SAEVFEENDG SLKNVHAAVA RGRQMRCELC LKPGATVGCC LSSCLSNFHF MCARASYCIF
     QDDKKVFCQK HTDLLDGKEI VTPDGFDVLR RVYVDFEGIN FKRKFLTGLE PDVINVLIGS
     IRINSLGTLS DLSDCEGRLF PIGYQCSRLY WSTVDARRRC WYRCRILEYR PWGPREEPVH
     LEAAEENQTI VHSPTPSSDT DSLIPGDPVH HSPIQNLDPP LRTDSSNGPP PTPRSFSGAR
     IKVPNYSPSR RPLGGVSFGP LPSPGSPSSL THHIPTVGDS DFPAPPRRSR RPSPLATRPP
     PSRRTSSPLR TSPQLRVPLS TSVTALTPTS GELAPPDLAP SPLPPSEDLG PDFEDMEVVS
     GLSAADLDFA ASLLGTEPFQ EEIVAAGAVG SSQGGPGDSS EEEASPTTHY VHFPVTVVSG
     PALAPSSLAG APRIEQLDGV DDGTDSEAEA VQQPRGQGTP PSGPGVGRGG VLGAAGDRAQ
     PPEDLPSEIV DFVLKNLGGP GEGAAGPRED SLPSAPPLAN GSQPPQSLST SPADPTRTFA
     WLPGAPGVRV LSLGPAPEPP KPATSKIILV NKLGQVFVKM AGEGEPVAPP VKQPPLPPII
     PPTAPTSWTL PPGPLLSVLP VVGVGVVRPA PPPPPPPLTL VFSSGPPSPP RQAIRVKRVS
     TFSGRSPPVP PPNKTPRLDE DGESLEDAHH VPGISGSGFS RVRMKTPTVR GVLDLNNPGE
     QPEEESPGRP QDRCPLLPLA EAPSQALDGS SDLLFESQWH HYSAGEASSS EEEPPSPEDK
     ENQVPKRVGP HLRFEISSDD GFSVEAESLE VAWRTLIEKV QEARGHARLR HLSFSGMSGA
     RLLGIHHDAV IFLAEQLPGA QRCQHYKFRY HQQGEGQEEP PLNPHGAARA EVYLRKCTFD
     MFNFLASQHR VLPEGATCDE EEDEVQLRST RRATSLELPM AMRFRHLKKT SKEAVGVYRS
     AIHGRGLFCK RNIDAGEMVI EYSGIVIRSV LTDKREKFYD GKGIGCYMFR MDDFDVVDAT
     MHGNAARFIN HSCEPNCFSR VIHVEGQKHI VIFALRRILR GEELTYDYKF PIEDASNKLP
     CNCGAKRCRR FLN
//
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