GenomeNet

Database: UniProt
Entry: Q8IRW8
LinkDB: Q8IRW8
Original site: Q8IRW8 
ID   TRR_DROME               Reviewed;        2431 AA.
AC   Q8IRW8; O46083; Q8MYR5; Q8T9I7; Q9W548;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   13-FEB-2019, entry version 143.
DE   RecName: Full=Histone-lysine N-methyltransferase trr;
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine N-methyltransferase 2C;
DE   AltName: Full=Trithorax-related protein;
GN   Name=trr; Synonyms=KMT2C; ORFNames=CG3848;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
RA   Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
RA   Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
RA   Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
RA   Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
RA   Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
RA   Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
RA   Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1409-2431.
RC   STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10354481; DOI=10.1016/S0925-4773(98)00246-9;
RA   Sedkov Y., Benes J.J., Berger J.R., Riker K.M., Tillib S., Jones R.S.,
RA   Mazo A.;
RT   "Molecular genetic analysis of the Drosophila trithorax-related gene
RT   which encodes a novel SET domain protein.";
RL   Mech. Dev. 82:171-179(1999).
RN   [6]
RP   FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   ECR.
RX   PubMed=14603321; DOI=10.1038/nature02080;
RA   Sedkov Y., Cho E., Petruk S., Cherbas L., Smith S.T., Jones R.S.,
RA   Cherbas P., Canaani E., Jaynes J.B., Mazo A.;
RT   "Methylation at lysine 4 of histone H3 in ecdysone-dependent
RT   development of Drosophila.";
RL   Nature 426:78-83(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1486; SER-1488 AND
RP   SER-1490, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [8]
RP   IDENTIFICATION IN THE MLL3/4 COMPLEX.
RX   PubMed=21875999; DOI=10.1128/MCB.06092-11;
RA   Mohan M., Herz H.M., Smith E.R., Zhang Y., Jackson J., Washburn M.P.,
RA   Florens L., Eissenberg J.C., Shilatifard A.;
RT   "The COMPASS family of H3K4 methylases in Drosophila.";
RL   Mol. Cell. Biol. 31:4310-4318(2011).
RN   [9]
RP   FUNCTION, INTERACTION WITH ASH2, AND DISRUPTION PHENOTYPE.
RX   PubMed=23197473; DOI=10.1091/mbc.E12-04-0267;
RA   Carbonell A., Mazo A., Serras F., Corominas M.;
RT   "Ash2 acts as an ecdysone receptor coactivator by stabilizing the
RT   histone methyltransferase Trr.";
RL   Mol. Biol. Cell 24:361-372(2013).
CC   -!- FUNCTION: Histone methyltransferase that acts as a coactivator for
CC       the ecdysone receptor during development. Specifically
CC       trimethylates 'Lys-4' of histone H3, a specific tag for epigenetic
CC       transcriptional activation. Recruited by EcR in an ecdysone-
CC       dependent manner causing H3 'Lys-4' trimethylation at ecdysone-
CC       inducible promoters, leading to activate expression. Plays a
CC       central role in the developing compound eye, during the
CC       progression of the morphogenetic furrow and in post-furrow
CC       differentiation of the retinal epithelium, notably by activating
CC       expression of hh. Also required for wing and abdominal
CC       development. {ECO:0000269|PubMed:14603321,
CC       ECO:0000269|PubMed:23197473}.
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         Evidence={ECO:0000269|PubMed:14603321};
CC   -!- SUBUNIT: Component of the MLL3/4 complex composed at least of the
CC       catalytic subunit trr, ash2, Rbbp5, Dpy-30L1, wds, hcf, ptip, Pa1,
CC       Utx, Lpt and Ncoa6. Interacts with nuclear receptor EcR in an
CC       ecdysone-dependent manner. Interacts with ash2; the interaction
CC       stabilizes trr. {ECO:0000269|PubMed:14603321,
CC       ECO:0000269|PubMed:21875999, ECO:0000269|PubMed:23197473}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14603321}.
CC       Chromosome {ECO:0000305|PubMed:14603321}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IRW8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IRW8-2; Sequence=VSP_021439;
CC         Note=Produced by alternative promoter usage. No experimental
CC         confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:10354481}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Abundantly expressed in 1-7 than in 7-20 hours old embryos.
CC       Expressed uniformly at the preblastoderm stage, prior to the onset
CC       of zygotic transcription. In ovaries, it is not expressed in
CC       ovarian stem cells, oogonia or early cysts and is first detectable
CC       at stage 8 in nurse cells. At stage 10, it is expressed in the
CC       anterior end of the oocyte, and is uniformly distributed later on.
CC       Expressed almost uniformly in embryos from precellular blastoderm
CC       stage to the germband extended stage. At the germband extended
CC       stage, it is enriched in the mesoderm. During germband retraction,
CC       it is strongly expressed in the anterior and posterior midgut. At
CC       the germband retracted stage, it becomes less abundant and is
CC       mainly localized to the ventral nerve cord and the brain. In third
CC       instar larvae, it is strongly and almost ubiquitously expressed in
CC       all imaginal disks. Also weakly expressed expression in salivary
CC       glands. Not expressed in larval brain and gut tissues.
CC       {ECO:0000269|PubMed:10354481}.
CC   -!- DOMAIN: Contains 3 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL motif
CC       2 is essential for the association with nuclear receptor EcR.
CC   -!- DISRUPTION PHENOTYPE: Defects in mechanosensory bristle spacing
CC       and differentiation in wings and lack of chaetes and macrochaetes
CC       in abdominal a4 and a5 segments. {ECO:0000269|PubMed:23197473}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAL39418.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAM29656.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=CAA15944.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AE014298; AAF45684.2; -; Genomic_DNA.
DR   EMBL; AE014298; AAN09063.2; -; Genomic_DNA.
DR   EMBL; AL021106; CAA15944.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY069273; AAL39418.1; ALT_INIT; mRNA.
DR   EMBL; AY113651; AAM29656.1; ALT_INIT; mRNA.
DR   PIR; T12687; T12687.
DR   RefSeq; NP_525040.2; NM_080301.3. [Q8IRW8-2]
DR   RefSeq; NP_726773.2; NM_166911.4. [Q8IRW8-1]
DR   ProteinModelPortal; Q8IRW8; -.
DR   SMR; Q8IRW8; -.
DR   BioGrid; 57695; 18.
DR   ELM; Q8IRW8; -.
DR   IntAct; Q8IRW8; 2.
DR   STRING; 7227.FBpp0070347; -.
DR   iPTMnet; Q8IRW8; -.
DR   PaxDb; Q8IRW8; -.
DR   PRIDE; Q8IRW8; -.
DR   EnsemblMetazoa; FBtr0070362; FBpp0070346; FBgn0023518. [Q8IRW8-2]
DR   EnsemblMetazoa; FBtr0070363; FBpp0070347; FBgn0023518. [Q8IRW8-1]
DR   GeneID; 31149; -.
DR   KEGG; dme:Dmel_CG3848; -.
DR   UCSC; CG3848-RC; d. melanogaster. [Q8IRW8-1]
DR   CTD; 7870; -.
DR   FlyBase; FBgn0023518; trr.
DR   eggNOG; KOG4443; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000168851; -.
DR   InParanoid; Q8IRW8; -.
DR   KO; K09188; -.
DR   OMA; FKPGEAQ; -.
DR   PhylomeDB; Q8IRW8; -.
DR   Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   GenomeRNAi; 31149; -.
DR   PRO; PR:Q8IRW8; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0023518; Expressed in 32 organ(s), highest expression level in embryo.
DR   Genevisible; Q8IRW8; DM.
DR   GO; GO:0044666; C:MLL3/4 complex; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0005703; C:polytene chromosome puff; IDA:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:FlyBase.
DR   GO; GO:0003713; F:transcription coactivator activity; IGI:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IDA:FlyBase.
DR   GO; GO:0016571; P:histone methylation; IDA:FlyBase.
DR   GO; GO:1900114; P:positive regulation of histone H3-K9 trimethylation; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:FlyBase.
DR   GO; GO:0007458; P:progression of morphogenetic furrow involved in compound eye morphogenesis; IMP:FlyBase.
DR   GO; GO:0035075; P:response to ecdysone; IDA:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR037877; KMT2C.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22884:SF373; PTHR22884:SF373; 1.
DR   Pfam; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
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.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Chromatin regulator; Chromosome;
KW   Complete proteome; Developmental protein; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   2431       Histone-lysine N-methyltransferase trr.
FT                                /FTId=PRO_0000259524.
FT   DOMAIN     2061   2121       FYR N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00875}.
FT   DOMAIN     2122   2209       FYR C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00876}.
FT   DOMAIN     2291   2407       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     2415   2431       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING    1895   1935       C2HC pre-PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   ZN_FING    1956   2003       PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   MOTIF       801    805       LXXLL motif 1.
FT   MOTIF      1652   1656       LXXLL motif 2.
FT   MOTIF      2060   2064       LXXLL motif 3.
FT   COMPBIAS    172    225       Ser-rich.
FT   COMPBIAS    226    288       Thr-rich.
FT   COMPBIAS    430    448       Gln-rich.
FT   COMPBIAS    926    976       Gln-rich.
FT   COMPBIAS   1169   1240       Gln-rich.
FT   MOD_RES    1486   1486       Phosphothreonine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1488   1488       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1490   1490       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   VAR_SEQ     140    161       SEYRISTPRNSQSNPLLHRNTA -> T (in isoform
FT                                2). {ECO:0000305}.
FT                                /FTId=VSP_021439.
FT   CONFLICT    219    219       S -> A (in Ref. 3; CAA15944).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2431 AA;  259828 MW;  F444825B956A87AA CRC64;
     MNIPKVTTSL GAAEKAKPER VASVAAAAFN AVSLQKRSGD DTATPAEDPT RKKAKTELLL
     GTGTAAPSLP AKASSTAPQQ LLYQRSGQQA KAQVKAASEP QDVETADGVW DARDQQIIVC
     NFGSGTEMGA IKAEDADKQS EYRISTPRNS QSNPLLHRNT AFTSFTKKEG ASSSASSSSS
     TASVISIEPS GSGQDHAENS GKSEDLDYVL MPASGADSST SVGNSTGTGT PAGTPIGATT
     STIILNANNG TAGVSGAGTT TILTQKSGHT NYNIFNTTAT GSQTPTTTLL NRVNLHPKMK
     TQLMVNAKKL SEVTQTTAKV SIGNKTISVP LLKPLMSASG AATAGGATIV ESKQLLQPGG
     QVTTVMSAAQ QSGGQQVHPH VHSHAHHNFT KLIKRGPKNS GTIVSFSGLQ IKPANTKIVA
     TKVVSKKMLQ LQQHQQQIQQ QQQLQQLQVT SGGGLAPPTG SIVTITTTNP SQTYAMVQDS
     ATVGPAAHSE DDAPAPRKIT AYSENLQKIL NKSKSQESTG GPEEFTNINS VVIKPLDKNT
     LNCPPSFNIF KQQQHSQAAQ SQSISAVGSG AGTPVTFTMA SGNASDLATT STVSVSAGTI
     CINSPMMGTR PIISIQNKNI SLVLSKTTMA QQKPKMITTT TLSSQAALQM HHALIQDSSA
     DKAGSSANSG SATSGASMQL KLTTANTPTK LSVSLAPDVV KLEEVGSESK AKLLVKQEAV
     VKDSTGTPTS EERAEEIGTP EKRLNANATM TAINQVQNQS ANQIQMATST STASNPSTPN
     PTVNATPMNN QRSAAEDNAL LKQLLQNNSS SHSLNQISIT SAHVGSASAS APLSARKVIN
     VRAPSMGKVR SLEDQLARPV IPPVPTATQA AGSSSSSGSV ATSTTTTTVA SGGSSQQVAT
     ASATALPVSA VAITTPGVGG EAKLEQKSDQ PAAIMQNQSQ NQAPPPPPPP QQQQQQQLHQ
     PQQLQPSPHQ VKQTVQIVSK ETSFISGPVA AKTLVTEATS KPAELLPPPP YEMATAPISN
     VTISISTKQA APKELQMKPK AVAMSLPMEQ GDESLPEQAE PPLHSEQGAT AAGVAPHSGG
     PLVSAQWTNN HLEGGVATTK IPFKPGEPQK RKLPMHPQLD EKQIQQQAEI PISTSLPTTP
     TGQGTPDKVQ LISAIATYVK KSGVPNEAQP IQNQSQGQVQ MQAQMQATMQ GHLSGQMSGQ
     ISGHAAGQIP AQMHLQVQHQ LHMAVHPQQQ QQQLHQNQPQ NATIPLPVTG QGAVPIPVPT
     MESKAGDQRK RRKREVQKPR RTNLNAGQAG GALKDLTGPL PAGAMVQLAG MPPGTQYIQG
     AASGTGHVIT STGQGVTLGG VGASTGASSS PMLKKRVRKF SKVEEDHDAF TEKLLTHIRQ
     MQPLQVLEPH LNRNFHFLIG SNETSGGGSP ASMSSAASAG SSSAGGGKLK GGSRGWPLSR
     HLEGLEDCDG TVLGRYGRVN LPGIPSLYDS ERFGGSRGLV GGSARTRSPS PAESPGAEKM
     LPMSSIQNDF YDQEFSTHME RNPRERLVRH IGAVKDCNLE TVDLVESEGV AAWATLPRLT
     RYPGLILLNG NSRCHGRMSP VALPEDPLTM RFPVSPLLRS CGEELRKTQQ MELGMGPLGN
     NNNNNYQQKN QNVILALPAS ASENIAGVLR DLANLLHLAP ALTCKIIEDK IGNKLEDQFM
     NQDDEKHVDF KRPLSQVSHG HLRKILNGRR KLCRSCGNVV HATGLRVPRH SVPALEEQLP
     RLAQLMDMLP RKSVPPPFVY FCDRACFARF KWNGKDGQAE AASLLLQPAG GSAVKSSNGD
     SPGSFCASST APAEMVVKQE PEDEDEKTPS VPGNPTNIPA QRKCIVKCFS ADCFTTDSAP
     SGLELDGTAG AGTGAGPVNN TVWETETSGL QLEDTRQCVF CNQRGDGQAD GPSRLLNFDV
     DKWVHLNCAL WSNGVYETVS GALMNFQTAL QAGLSQACSA CHQPGATIKC FKSRCNSLYH
     LPCAIREECV FYKNKSVHCS VHGHAHAGIT MGAGAGATTG AGLGGSVADN ELSSLVVHRR
     VFVDRDENRQ VATVMHYSEL SNLLRVGNMT FLNVGQLLPH QLEAFHTPHY IYPIGYKVSR
     YYWCVRRPNR RCRYICSIAE AGCKPEFRIQ VQDAGDKEPE REFRGSSPSA VWQQILQPIT
     RLRKVHKWLQ LFPQHISGED LFGLTEPAIV RILESLPGIE TLTDYRFKYG RNPLLEFPLA
     INPSGAARTE PKQRQLLVWR KPHTQRTAGS CSTQRMANSA AIAGEVACPY SKQFVHSKSS
     QYKKMKQEWR NNVYLARSKI QGLGLYAARD IEKHTMIIEY IGEVIRTEVS EIREKQYESK
     NRGIYMFRLD EDRVVDATLS GGLARYINHS CNPNCVTEIV EVDRDVRIII FAKRKIYRGE
     ELSYDYKFDI EDESHKIPCA CGAPNCRKWM N
//
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