GenomeNet

Database: UniProt/SWISS-PROT
Entry: ASHH2_ARATH
LinkDB: ASHH2_ARATH
Original site: ASHH2_ARATH 
ID   ASHH2_ARATH             Reviewed;        1759 AA.
AC   Q2LAE1; A9QA57; O80663; Q56WW4;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   23-MAY-2018, entry version 101.
DE   RecName: Full=Histone-lysine N-methyltransferase ASHH2;
DE            EC=2.1.1.43;
DE   AltName: Full=ASH1 homolog 2 {ECO:0000303|PubMed:19915673};
DE   AltName: Full=H3-K4-HMTase;
DE   AltName: Full=Histone H3-K36 methyltransferase 8;
DE            Short=H3-K36-HMTase 8;
DE   AltName: Full=Protein EARLY FLOWERING IN SHORT DAYS;
DE   AltName: Full=Protein LAZARUS 2 {ECO:0000303|PubMed:20949080};
DE   AltName: Full=Protein SET DOMAIN GROUP 8;
GN   Name=ASHH2 {ECO:0000303|PubMed:19915673};
GN   Synonyms=EFS, LAZ2 {ECO:0000303|PubMed:20949080}, SDG8, SET8;
GN   OrderedLocusNames=At1g77300; ORFNames=T14N5.15;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16299497; DOI=10.1038/ncb1329;
RA   Zhao Z., Yu Y., Meyer D., Wu C., Shen W.-H.;
RT   "Prevention of early flowering by expression of FLOWERING LOCUS C
RT   requires methylation of histone H3 K36.";
RL   Nat. Cell Biol. 7:1256-1260(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1299-1759 (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NOMENCLATURE.
RX   PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA   Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA   Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT   "The Arabidopsis thaliana genome contains at least 29 active genes
RT   encoding SET domain proteins that can be assigned to four
RT   evolutionarily conserved classes.";
RL   Nucleic Acids Res. 29:4319-4333(2001).
RN   [6]
RP   FUNCTION.
RX   PubMed=10518493;
RA   Soppe W.J.J., Bentsink L., Koornneef M.;
RT   "The early-flowering mutant efs is involved in the autonomous
RT   promotion pathway of Arabidopsis thaliana.";
RL   Development 126:4763-4770(1999).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16258034; DOI=10.1105/tpc.105.034645;
RA   Kim S.Y., He Y., Jacob Y., Noh Y.-S., Michaels S., Amasino R.;
RT   "Establishment of the vernalization-responsive, winter-annual habit in
RT   Arabidopsis requires a putative histone H3 methyl transferase.";
RL   Plant Cell 17:3301-3310(2005).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18070919; DOI=10.1128/MCB.01607-07;
RA   Xu L., Zhao Z., Dong A., Soubigou-Taconnat L., Renou J.P.,
RA   Steinmetz A., Shen W.H.;
RT   "Di- and tri- but not monomethylation on histone H3 lysine 36 marks
RT   active transcription of genes involved in flowering time regulation
RT   and other processes in Arabidopsis thaliana.";
RL   Mol. Cell. Biol. 28:1348-1360(2008).
RN   [9]
RP   INDUCTION BY VERNALIZATION, AND TISSUE SPECIFICITY.
RX   PubMed=19121105; DOI=10.1111/j.1365-313X.2008.03776.x;
RA   Choi J., Hyun Y., Kang M.J., In Yun H., Yun J.Y., Lister C., Dean C.,
RA   Amasino R.M., Noh B., Noh Y.S., Choi Y.;
RT   "Resetting and regulation of Flowering Locus C expression during
RT   Arabidopsis reproductive development.";
RL   Plant J. 57:918-931(2009).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=19915673; DOI=10.1371/journal.pone.0007817;
RA   Grini P.E., Thorstensen T., Alm V., Vizcay-Barrena G., Windju S.S.,
RA   Jorstad T.S., Wilson Z.A., Aalen R.B.;
RT   "The ASH1 HOMOLOG 2 (ASHH2) histone H3 methyltransferase is required
RT   for ovule and anther development in Arabidopsis.";
RL   PLoS ONE 4:E7817-E7817(2009).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH FRI AND SUF4.
RX   PubMed=20711170; DOI=10.1038/emboj.2010.198;
RA   Ko J.H., Mitina I., Tamada Y., Hyun Y., Choi Y., Amasino R.M., Noh B.,
RA   Noh Y.S.;
RT   "Growth habit determination by the balance of histone methylation
RT   activities in Arabidopsis.";
RL   EMBO J. 29:3208-3215(2010).
RN   [12]
RP   FUNCTION.
RX   PubMed=20949080; DOI=10.1371/journal.ppat.1001137;
RA   Palma K., Thorgrimsen S., Malinovsky F.G., Fiil B.K., Nielsen H.B.,
RA   Brodersen P., Hofius D., Petersen M., Mundy J.;
RT   "Autoimmunity in Arabidopsis acd11 is mediated by epigenetic
RT   regulation of an immune receptor.";
RL   PLoS Pathog. 6:E1001137-E1001137(2010).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH THE FRI-C
RP   COMPLEX AND SWC6.
RX   PubMed=21282526; DOI=10.1105/tpc.110.075911;
RA   Choi K., Kim J., Hwang H.J., Kim S., Park C., Kim S.Y., Lee I.;
RT   "The FRIGIDA complex activates transcription of FLC, a strong
RT   flowering repressor in Arabidopsis, by recruiting chromatin
RT   modification factors.";
RL   Plant Cell 23:289-303(2011).
RN   [14]
RP   FUNCTION, INTERACTION WITH BZR2/BES1 AND IWS1, SUBCELLULAR LOCATION,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=24838002; DOI=10.1093/mp/ssu056;
RA   Wang X., Chen J., Xie Z., Liu S., Nolan T., Ye H., Zhang M., Guo H.,
RA   Schnable P.S., Li Z., Yin Y.;
RT   "Histone lysine methyltransferase SDG8 is involved in brassinosteroid-
RT   regulated gene expression in Arabidopsis thaliana.";
RL   Mol. Plant 7:1303-1315(2014).
RN   [15]
RP   STRUCTURE BY NMR OF 849-937 IN COMPLEX WITH ZINC AND METHYLATED H3K4
RP   PEPTIDE, AND MUTAGENESIS OF TRP-865; TRP-874; TRP-891; GLN-908 AND
RP   GLU-909.
RX   PubMed=21522130; DOI=10.1038/emboj.2011.108;
RA   Hoppmann V., Thorstensen T., Kristiansen P.E., Veiseth S.V.,
RA   Rahman M.A., Finne K., Aalen R.B., Aasland R.;
RT   "The CW domain, a new histone recognition module in chromatin
RT   proteins.";
RL   EMBO J. 30:1939-1952(2011).
CC   -!- FUNCTION: Histone methyltransferase involved in di and tri-
CC       methylation of 'Lys-36' of histone H3 (H3K36me2 and H3K36me3).
CC       Binds to H3 already mono- or di-methylated on 'Lys-4'(H3K4me1 or
CC       H3K4me2), but not to H3K4me3. H3K4me and H3K36me represent
CC       specific tags for epigenetic transcriptional activation. Regulates
CC       positively FLC transcription to prevent early flowering
CC       transition. Required for flowering transition in response to
CC       vernalization and for the maintenance of FLC expression in late
CC       embryos, but dispensable for the initial reactivation in early
CC       embryos during reprogramming. Seems also to modulate several
CC       traits including floral organ size, root size and dormancy.
CC       Promotes apical dominance (PubMed:16299497, PubMed:10518493,
CC       PubMed:16258034, PubMed:18070919, PubMed:19915673,
CC       PubMed:20711170). Directly involved in the tri-methylation of
CC       'Lys-36' of histone H3 (H3K36me3) at LAZ5 chromatin to maintain a
CC       transcriptionally active state of LAZ5, a TIR-NB-LRR protein
CC       involved in innate immunity (PubMed:20949080). Required for
CC       brassinosteroid (BR)-induced gene expression and histone H3
CC       trimethylation on 'Lys-36' (H3K36me3) in BR-regulated genes
CC       (PubMed:24838002). {ECO:0000269|PubMed:10518493,
CC       ECO:0000269|PubMed:16258034, ECO:0000269|PubMed:16299497,
CC       ECO:0000269|PubMed:18070919, ECO:0000269|PubMed:19915673,
CC       ECO:0000269|PubMed:20711170, ECO:0000269|PubMed:20949080,
CC       ECO:0000269|PubMed:24838002}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBUNIT: Interacts with FRI and SUF4, two components of the
CC       transcription activator complex FRI-C, and with SWC6, a component
CC       of the SWR1 chromatin-remodeling complex (PubMed:20711170,
CC       PubMed:21282526, PubMed:21522130). Interacts with BZR2/BES1 and
CC       IWS1 (PubMed:24838002). {ECO:0000269|PubMed:20711170,
CC       ECO:0000269|PubMed:21282526, ECO:0000269|PubMed:21522130,
CC       ECO:0000269|PubMed:24838002}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18070919,
CC       ECO:0000269|PubMed:24838002}. Chromosome, centromere
CC       {ECO:0000305|PubMed:18070919}. Note=Associates with centromeric
CC       constitutive heterochromatin. {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q2LAE1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2LAE1-2; Sequence=VSP_018133;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in young
CC       tissues, including shoot and root apex. Expressed in ovules,
CC       tapetum layer and microspores. {ECO:0000269|PubMed:16258034,
CC       ECO:0000269|PubMed:16299497, ECO:0000269|PubMed:19121105,
CC       ECO:0000269|PubMed:19915673}.
CC   -!- INDUCTION: Not regulated by vernalization.
CC       {ECO:0000269|PubMed:19121105}.
CC   -!- DISRUPTION PHENOTYPE: Early flowering. Pleiotropic developmental
CC       effects including dwarf and bushy phenotype, reduced seed setting
CC       and defects in ovule and embryo sac development (PubMed:18070919,
CC       PubMed:19915673, PubMed:24838002). Altered responses to
CC       brassinosteroid (BR) (PubMed:24838002).
CC       {ECO:0000269|PubMed:18070919, ECO:0000269|PubMed:19915673,
CC       ECO:0000269|PubMed:24838002}.
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=AAC34358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAD94318.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
DR   EMBL; DQ340869; ABC69038.1; -; mRNA.
DR   EMBL; EU014690; ABV68921.1; -; mRNA.
DR   EMBL; AC004260; AAC34358.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35960.1; -; Genomic_DNA.
DR   EMBL; AK221916; BAD94318.1; ALT_INIT; mRNA.
DR   PIR; T00458; T00458.
DR   RefSeq; NP_177854.6; NM_106379.9. [Q2LAE1-2]
DR   UniGene; At.34505; -.
DR   PDB; 2L7P; NMR; -; A=849-937.
DR   PDB; 5YVX; X-ray; 1.59 A; A=862-921.
DR   PDBsum; 2L7P; -.
DR   PDBsum; 5YVX; -.
DR   ProteinModelPortal; Q2LAE1; -.
DR   SMR; Q2LAE1; -.
DR   BioGrid; 29285; 15.
DR   IntAct; Q2LAE1; 2.
DR   MINT; Q2LAE1; -.
DR   STRING; 3702.AT1G77300.1; -.
DR   iPTMnet; Q2LAE1; -.
DR   PaxDb; Q2LAE1; -.
DR   PRIDE; Q2LAE1; -.
DR   EnsemblPlants; AT1G77300.1; AT1G77300.1; AT1G77300. [Q2LAE1-2]
DR   GeneID; 844066; -.
DR   Gramene; AT1G77300.1; AT1G77300.1; AT1G77300. [Q2LAE1-2]
DR   KEGG; ath:AT1G77300; -.
DR   Araport; AT1G77300; -.
DR   TAIR; locus:2196000; AT1G77300.
DR   eggNOG; KOG4442; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000029212; -.
DR   InParanoid; Q2LAE1; -.
DR   OMA; MEANSPI; -.
DR   OrthoDB; EOG0936006B; -.
DR   PhylomeDB; Q2LAE1; -.
DR   Reactome; R-ATH-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-ATH-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   PRO; PR:Q2LAE1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q2LAE1; baseline and differential.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048653; P:anther development; IMP:TAIR.
DR   GO; GO:0016116; P:carotenoid metabolic process; IMP:TAIR.
DR   GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR   GO; GO:0010452; P:histone H3-K36 methylation; IDA:TAIR.
DR   GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR   GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR   GO; GO:0009555; P:pollen development; IMP:TAIR.
DR   GO; GO:0031062; P:positive regulation of histone methylation; IDA:TAIR.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR.
DR   GO; GO:0010363; P:regulation of plant-type hypersensitive response; IMP:TAIR.
DR   GO; GO:0043067; P:regulation of programmed cell death; IGI:TAIR.
DR   GO; GO:0010223; P:secondary shoot formation; IMP:TAIR.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR011124; Znf_CW.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF07496; zf-CW; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51050; ZF_CW; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Centromere; Chromatin regulator;
KW   Chromosome; Complete proteome; Metal-binding; Methyltransferase;
KW   Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1759       Histone-lysine N-methyltransferase ASHH2.
FT                                /FTId=PRO_0000233371.
FT   DOMAIN      974   1024       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN     1026   1143       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1151   1167       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING     859    912       CW-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00454}.
FT   COMPBIAS   1400   1405       Poly-Leu.
FT   METAL       868    868       Zinc. {ECO:0000269|PubMed:21522130}.
FT   METAL       871    871       Zinc. {ECO:0000269|PubMed:21522130}.
FT   METAL       893    893       Zinc. {ECO:0000269|PubMed:21522130}.
FT   METAL       904    904       Zinc. {ECO:0000269|PubMed:21522130}.
FT   BINDING    1142   1142       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   VAR_SEQ    1447   1447       G -> GLQMLHNIMKQYRGDFKRIPIIRKLLKVLEYLATRK
FT                                ILALEHIIRRP (in isoform 2).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_018133.
FT   MUTAGEN     865    865       W->A: Loss of histone tail binding.
FT                                {ECO:0000269|PubMed:21522130}.
FT   MUTAGEN     874    874       W->A: Loss of histone tail binding.
FT                                {ECO:0000269|PubMed:21522130}.
FT   MUTAGEN     891    891       W->A: Loss of histone tail binding.
FT                                {ECO:0000269|PubMed:21522130}.
FT   MUTAGEN     908    908       Q->A: Loss of histone tail binding.
FT                                {ECO:0000269|PubMed:21522130}.
FT   MUTAGEN     909    909       E->A: Loss of histone tail binding.
FT                                {ECO:0000269|PubMed:21522130}.
FT   CONFLICT   1426   1426       I -> T (in Ref. 4; BAD94318).
FT                                {ECO:0000305}.
FT   STRAND      863    867       {ECO:0000244|PDB:5YVX}.
FT   TURN        869    871       {ECO:0000244|PDB:5YVX}.
FT   STRAND      874    878       {ECO:0000244|PDB:5YVX}.
FT   HELIX       879    882       {ECO:0000244|PDB:5YVX}.
FT   HELIX       893    895       {ECO:0000244|PDB:5YVX}.
FT   STRAND      899    901       {ECO:0000244|PDB:2L7P}.
FT   HELIX       912    919       {ECO:0000244|PDB:5YVX}.
SQ   SEQUENCE   1759 AA;  193228 MW;  5616BE25ECEF2155 CRC64;
     MDCKENGVGD ASGCNIDANS LASNLAMNTN EDFYEKLSSR GQNLDSVSSL EIPQTASSVN
     HTIEGQRKCF TEIEQMGYGN SNSQEDAGNT DDDLYVCYNA DDTQEQGVVS GELEQSQELI
     CDTDLLVNCN KLDDGKESQD TNVSLVSIFS GSMQEKEAPQ AKEDEGYGGT TLPIGGSGID
     TESTFVNDAP EQFESLETTK HIKPDEVESD GISYRFDDGG KEGRNGPSSD LDTGSSDDIS
     LSQSFSFPDS LLDSSVFGCS ATESYLEDAI DIEGNGTIVV SPSLAITEML NNDDGGLCSH
     DLNKITVTET INPDLKLVRE DRLDTDLSVM NEKMLKNHVG DSSSESAVAA LSMNNGMAAD
     LRAENFSQSS PIDEKTLDME ANSPITDSSL IWNFPLNFGS GGIEVCNPEN AVEPLRIVDD
     NGRIGGEVAS ASGSDFCEAG MSSSRRKARD GKQCKVVQTK TSARHLRKSS RKKQSERDIE
     SIFKCSKQKR SSLLKTSRSS EWGLPSKTTE IFLQSNNIPY DGPPHHEPQR SQGNLNNGEH
     NRSSHNGNVE GSNRNIQASS GSCLRLKVKF GKSGGQNPLN ITVSKVSGNS LPGNGIVKAG
     TCLELPGSAH FGEDKMQTVE TKEDLVEKSN PVEKVSYLQS SDSMRDKKYN QDAGGLCRKV
     GGDVLDDDPH LSSIRMVEEC ERATGTQSLD AETSPDSEVI NSVPDSIVNI EHKEGLHHGF
     FSTPEDVVKK NRVLEKEDEL RASKSPSENG SHLIPNAKKA KHPKSKSNGT KKGKSKFSES
     AKDGRKNESH EGVEQRKSLN TSMGRDDSDY PEVGRIESHK TTGALLDADI GKTSATYGTI
     SSDVTHGEMV VDVTIEDSYS TESAWVRCDD CFKWRRIPAS VVGSIDESSR WICMNNSDKR
     FADCSKSQEM SNEEINEELG IGQDEADAYD CDAAKRGKEK EQKSKRLTGK QKACFKAIKT
     NQFLHRNRKS QTIDEIMVCH CKPSPDGRLG CGEECLNRML NIECLQGTCP AGDLCSNQQF
     QKRKYVKFER FQSGKKGYGL RLLEDVREGQ FLIEYVGEVL DMQSYETRQK EYAFKGQKHF
     YFMTLNGNEV IDAGAKGNLG RFINHSCEPN CRTEKWMVNG EICVGIFSMQ DLKKGQELTF
     DYNYVRVFGA AAKKCYCGSS HCRGYIGGDP LNGDVIIQSD SDEEYPELVI LDDDESGEGI
     LGATSRTFTD DADEQMPQSF EKVNGYKDLA PDNTQTQSSV SVKLPEREIP PPLLQPTEVL
     KELSSGISIT AVQQEVPAEK KTKSTSPTSS SLSRMSPGGT NSDKTTKHGS GEDKKILPRP
     RPRMKTSRSS ESSKRDKGGI YPGVNKAQVI PVNKLQQQPI KSKGSEKVSP SIETFEGKLN
     ELLDAVGGIS KRRDSAKGYL KLLLLTAASR GTDEEGIYSN RDLSMILDAL LKTKSKSVLV
     DIINKNGPFA GMESFKDSVL SFTEHDDYTV HNIARSFRDR WIPKHFRKPW RINREERSES
     MRSPINRRFR ASQEPRYDHQ SPRPAEPAAS VTSSKAATPE TASVSEGYSE PNSGLPETNG
     RKRKSRWDQP SKTKEQRIMT ILSQQTDETN GNQDVQDDLP PGFSSPCTDV PDAITAQPQQ
     KFLSRLPVSY GIPLSIVHQF GSPGKEDPTT WSVAPGMPFY PFPPLPPVSH GEFFAKRNVR
     ACSSSMGNLT YSNEILPATP VTDSTAPTRK RELFSSDIGT TYFRQQKQSV PPWLRNNGGE
     KTANSPIPGN LTLEKKLNS
//
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