GenomeNet

Database: UniProt
Entry: P20659
LinkDB: P20659
Original site: P20659 
ID   TRX_DROME               Reviewed;        3726 AA.
AC   P20659; A4V2V9; A4V2W0; Q27255; Q27327; Q8INF9; Q960R2; Q9VFL1;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 4.
DT   16-JAN-2019, entry version 202.
DE   RecName: Full=Histone-lysine N-methyltransferase trithorax;
DE            EC=2.1.1.43 {ECO:0000269|PubMed:12408863};
DE   AltName: Full=Lysine N-methyltransferase 2A;
GN   Name=trx; Synonyms=KMT2A; ORFNames=CG8651;
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 [MRNA] (ISOFORM A), AND FUNCTION.
RX   PubMed=2107543; DOI=10.1073/pnas.87.6.2112;
RA   Mazo A.M., Huang D.-H., Mozer B.A., Dawid I.B.;
RT   "The trithorax gene, a trans-acting regulator of the bithorax complex
RT   in Drosophila, encodes a protein with zinc-binding domains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:2112-2116(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, FUNCTION,
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=7924996;
RA   Sedkov Y., Tillib S., Mizrokhi L., Mazo A.;
RT   "The bithorax complex is regulated by trithorax earlier during
RT   Drosophila embryogenesis than is the Antennapedia complex, correlating
RT   with a bithorax-like expression pattern of distinct early trithorax
RT   transcripts.";
RL   Development 120:1907-1917(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Oregon-R; TISSUE=Embryo;
RX   PubMed=8555104; DOI=10.1016/0925-4773(95)00429-7;
RA   Tillib S., Sedkov Y., Mizrokhi L., Mazo A.;
RT   "Conservation of structure and expression of the trithorax gene
RT   between Drosophila virilis and Drosophila melanogaster.";
RL   Mech. Dev. 53:113-122(1995).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2970-3726 (ISOFORMS A/B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
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   [7]
RP   INTERACTION WITH ASH1.
RX   PubMed=10454589; DOI=10.1128/MCB.19.9.6441;
RA   Rozovskaia T., Tillib S., Smith S., Sedkov Y., Rozenblatt-Rosen O.,
RA   Petruk S., Yano T., Nakamura T., Ben-Simchon L., Gildea J.,
RA   Croce C.M., Shearn A., Canaani E., Mazo A.;
RT   "Trithorax and ASH1 interact directly and associate with the trithorax
RT   group-responsive bxd region of the Ultrabithorax promoter.";
RL   Mol. Cell. Biol. 19:6441-6447(1999).
RN   [8]
RP   INTERACTION WITH ASH1.
RX   PubMed=10656681; DOI=10.1038/sj.onc.1203307;
RA   Rozovskaia T., Rozenblatt-Rosen O., Sedkov Y., Burakov D., Yano T.,
RA   Nakamura T., Petruck S., Ben-Simchon L., Croce C.M., Mazo A.,
RA   Canaani E.;
RT   "Self-association of the SET domains of human ALL-1 and of Drosophila
RT   TRITHORAX and ASH1 proteins.";
RL   Oncogene 19:351-357(2000).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7958911; DOI=10.1101/gad.8.20.2478;
RA   Kuzin B., Tillib S., Sedkov Y., Mizrokhi L., Mazo A.;
RT   "The Drosophila trithorax gene encodes a chromosomal protein and
RT   directly regulates the region-specific homeotic gene fork head.";
RL   Genes Dev. 8:2478-2490(1994).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12408863; DOI=10.1016/S0092-8674(02)00975-3;
RA   Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
RT   "Drosophila Enhancer of zeste/ESC complexes have a histone H3
RT   methyltransferase activity that marks chromosomal Polycomb sites.";
RL   Cell 111:185-196(2002).
RN   [11]
RP   FUNCTION, INTERACTION WITH NUP98, AND DISRUPTION PHENOTYPE.
RX   PubMed=25310983; DOI=10.1016/j.celrep.2014.09.002;
RA   Pascual-Garcia P., Jeong J., Capelson M.;
RT   "Nucleoporin Nup98 associates with Trx/MLL and NSL histone-modifying
RT   complexes and regulates Hox gene expression.";
RL   Cell Rep. 9:433-442(2014).
CC   -!- FUNCTION: Histone methyltransferase that methylates 'Lys-4' of
CC       histone H3. H3 'Lys-4' methylation represents a specific tag for
CC       epigenetic transcriptional activation (PubMed:12408863). Functions
CC       in segment determination through interaction with genes of
CC       bithorax (BX-C) and antennapedia (ANT-C) complexes
CC       (PubMed:2107543, PubMed:7958911). Acts as an activator of BX-C
CC       (PubMed:7924996). Involved in the very early regulation of
CC       homeotic genes expressed only in the posterior region of the
CC       embryo (PubMed:7924996, PubMed:25310983).
CC       {ECO:0000269|PubMed:12408863, ECO:0000269|PubMed:2107543,
CC       ECO:0000269|PubMed:25310983, ECO:0000269|PubMed:7924996,
CC       ECO:0000269|PubMed:7958911}.
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:12408863};
CC   -!- SUBUNIT: Interacts (via SET domain) with ash1 (via SET domain)
CC       (PubMed:10454589, PubMed:10656681). Interacts with Nup98
CC       (PubMed:25310983). {ECO:0000269|PubMed:10454589,
CC       ECO:0000269|PubMed:10656681, ECO:0000269|PubMed:25310983}.
CC   -!- INTERACTION:
CC       Self; NbExp=7; IntAct=EBI-591327, EBI-591327;
CC       Q9V3G3:cyp33; NbExp=2; IntAct=EBI-591327, EBI-128445;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00407, ECO:0000269|PubMed:7958911}. Chromosome
CC       {ECO:0000269|PubMed:7958911}. Note=Binds to 16 discrete sites on
CC       larval salivary gland polytene chromosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A; Synonyms=D;
CC         IsoId=P20659-1; Sequence=Displayed;
CC       Name=B; Synonyms=C, E;
CC         IsoId=P20659-2; Sequence=VSP_006665;
CC   -!- TISSUE SPECIFICITY: Maternal isoforms are expressed in syncytial
CC       blastoderm, confined to the ventral region fated to become
CC       mesoderm. An additional broad domain of expression arises during
CC       cellularization and is quickly resolved into four pair-rule-like
CC       stripes in the posterior half of the embryo.
CC       {ECO:0000269|PubMed:7924996}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:7924996}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down in the larva
CC       results in decreased expression of Hox genes such as Ubx and Antp.
CC       {ECO:0000269|PubMed:25310983}.
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=AAK93328.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; M31617; AAA29025.1; -; mRNA.
DR   EMBL; Z50152; CAA90514.1; -; Genomic_DNA.
DR   EMBL; Z50152; CAA90513.1; -; Genomic_DNA.
DR   EMBL; Z31725; CAA83516.1; -; Genomic_DNA.
DR   EMBL; Z31725; CAA83515.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55041.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13599.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13600.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13601.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAX52951.1; -; Genomic_DNA.
DR   EMBL; AY051904; AAK93328.1; ALT_INIT; mRNA.
DR   PIR; A35085; A35085.
DR   RefSeq; NP_001014621.1; NM_001014621.2. [P20659-2]
DR   RefSeq; NP_476769.1; NM_057421.3. [P20659-1]
DR   RefSeq; NP_476770.1; NM_057422.3. [P20659-2]
DR   RefSeq; NP_599108.1; NM_134281.2. [P20659-2]
DR   RefSeq; NP_599109.1; NM_134282.2. [P20659-1]
DR   UniGene; Dm.6437; -.
DR   ProteinModelPortal; P20659; -.
DR   SMR; P20659; -.
DR   BioGrid; 66813; 45.
DR   ELM; P20659; -.
DR   IntAct; P20659; 14.
DR   MINT; P20659; -.
DR   STRING; 7227.FBpp0082406; -.
DR   PaxDb; P20659; -.
DR   PRIDE; P20659; -.
DR   EnsemblMetazoa; FBtr0082947; FBpp0082406; FBgn0003862. [P20659-1]
DR   EnsemblMetazoa; FBtr0082948; FBpp0082407; FBgn0003862. [P20659-2]
DR   EnsemblMetazoa; FBtr0082949; FBpp0082408; FBgn0003862. [P20659-2]
DR   EnsemblMetazoa; FBtr0082950; FBpp0082409; FBgn0003862. [P20659-1]
DR   EnsemblMetazoa; FBtr0100277; FBpp0099668; FBgn0003862. [P20659-2]
DR   GeneID; 41737; -.
DR   KEGG; dme:Dmel_CG8651; -.
DR   UCSC; CG8651-RC; d. melanogaster.
DR   UCSC; CG8651-RD; d. melanogaster.
DR   CTD; 41737; -.
DR   FlyBase; FBgn0003862; trx.
DR   eggNOG; KOG1084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000163756; -.
DR   InParanoid; P20659; -.
DR   KO; K09186; -.
DR   OMA; GVMYFEQ; -.
DR   PhylomeDB; P20659; -.
DR   Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   SignaLink; P20659; -.
DR   ChiTaRS; trx; fly.
DR   GenomeRNAi; 41737; -.
DR   PRO; PR:P20659; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0003862; Expressed in 49 organ(s), highest expression level in eye disc (Drosophila).
DR   Genevisible; P20659; DM.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IDA:FlyBase.
DR   GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR   GO; GO:0044665; C:MLL1/2 complex; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005700; C:polytene chromosome; IDA:UniProtKB.
DR   GO; GO:0008023; C:transcription elongation factor complex; IPI:FlyBase.
DR   GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:FlyBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IPI:FlyBase.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR   GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR   GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR   GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR   GO; GO:0007482; P:haltere development; IGI:UniProtKB.
DR   GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
DR   GO; GO:0043966; P:histone H3 acetylation; 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:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:FlyBase.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 2.
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; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00856; SET; 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; 2.
DR   SMART; SM00184; RING; 4.
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; PS51030; NUCLEAR_REC_DBD_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 4.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Chromatin regulator; Chromosome;
KW   Complete proteome; Developmental protein; DNA-binding; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   3726       Histone-lysine N-methyltransferase
FT                                trithorax.
FT                                /FTId=PRO_0000124874.
FT   DOMAIN     1884   1941       FYR N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00875}.
FT   DOMAIN     3386   3470       FYR C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00876}.
FT   DOMAIN     3588   3704       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     3710   3726       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DNA_BIND    759    884       Nuclear receptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING    1266   1347       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1348   1393       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1421   1482       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1734   1774       C2HC pre-PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   ZN_FING    1795   1842       PHD-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   REGION     3665   3666       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COMPBIAS    512    516       Poly-Ser.
FT   COMPBIAS    565    570       Poly-Asp.
FT   COMPBIAS    661    664       Poly-Ser.
FT   COMPBIAS    905    910       Poly-Ser.
FT   COMPBIAS   1576   1582       Poly-Gln.
FT   COMPBIAS   2298   3027       Gln-rich.
FT   COMPBIAS   3032   3040       Poly-Ser.
FT   COMPBIAS   3181   3184       Poly-Gln.
FT   COMPBIAS   3220   3225       Poly-Glu.
FT   METAL      3668   3668       Zinc. {ECO:0000250}.
FT   METAL      3714   3714       Zinc. {ECO:0000250}.
FT   METAL      3716   3716       Zinc. {ECO:0000250}.
FT   METAL      3721   3721       Zinc. {ECO:0000250}.
FT   BINDING    3598   3598       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    3600   3600       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING    3642   3642       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   VAR_SEQ       1    368       Missing (in isoform B). {ECO:0000305}.
FT                                /FTId=VSP_006665.
FT   CONFLICT    239    249       GTTSEATTSGL -> LEQLVKQQPLV (in Ref. 1;
FT                                AAA29025, 2; CAA90513 and 3; CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT    303    303       N -> K (in Ref. 1; AAA29025, 2; CAA90513
FT                                and 3; CAA83516). {ECO:0000305}.
FT   CONFLICT    337    337       A -> L (in Ref. 1; AAA29025, 2; CAA90513
FT                                and 3; CAA83516). {ECO:0000305}.
FT   CONFLICT    521    521       G -> R (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT    578    578       E -> Q (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT    587    587       V -> A (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT    700    700       N -> I (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT    720    720       T -> A (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT   1073   1073       K -> P (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT   1529   1530       KL -> NV (in Ref. 1; AAA29025, 2;
FT                                CAA90513/CAA90514 and 3; CAA83515/
FT                                CAA83516). {ECO:0000305}.
FT   CONFLICT   1594   1594       S -> P (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT   1627   1627       A -> E (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT   1690   1690       T -> A (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT   2010   2010       E -> Q (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT   2025   2025       P -> PWLTSPLKFLGLSTHGGLLLWLLLGVVVRLKQGG
FT                                (in Ref. 1; AAA29025). {ECO:0000305}.
FT   CONFLICT   2341   2341       S -> R (in Ref. 2; CAA90513/CAA90514 and
FT                                3; CAA83515/CAA83516). {ECO:0000305}.
FT   CONFLICT   2365   2365       S -> N (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT   2392   2392       S -> G (in Ref. 2; CAA90513/CAA90514 and
FT                                3; CAA83515/CAA83516). {ECO:0000305}.
FT   CONFLICT   3157   3157       E -> Q (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT   3234   3234       A -> R (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
FT   CONFLICT   3690   3690       L -> V (in Ref. 1; AAA29025, 2; CAA90513/
FT                                CAA90514 and 3; CAA83515/CAA83516).
FT                                {ECO:0000305}.
SQ   SEQUENCE   3726 AA;  400098 MW;  E3DDB8F062BD7796 CRC64;
     MGRSKFPGKP SKSINRKRIS VLQLEDDAAN PAEPQQPAPE SQQPSGSGSG SSAAREKGNN
     CDNDEDDNAP GGASISGNTA SSSAGSGNSG NGSSSGSSTG SGSSGSGSTN GGSVNGGTHH
     KSAANLDKEA VTKDQNGDGD KTRGNVSSAP SGKLSAAASG KALSKSSRTF SASTSVTSSG
     RSSGSSPDGN SGASSDGASS GISCGKSTAK STEASSGKLA KTTGAGTCSS AKSSKASSGT
     TSEATTSGLS GACLKALFVA TPATSTGLAC ALVSPGGSSQ GGTFPISAAL LRARKNSNKK
     FKNLNLARGE VMLPSTSKLK QLNSPVVDNP SPSPPIASGS TPSVEGGIGV GGVVSPGEDA
     ALKRVLTEMP NEVARDPSPS SCTAAANGAA SGKGSASNGP PAMASSGDGS SPKSGADTGP
     STSSTTAKQK KTVTFRNVLE TSDDKSVVKR FYNPDIRIPI VSIMKKDSLN RPLNYSRGGE
     CIVRPSILSK ILNKNSNIDK LNSLKFRSAG ASSSSSNQES GSSSNVFGLS RAFGAPMDED
     DEGGVTFRRN DSPEDQNNAE DDEMDDDDDD EEAEEDDENE DDNDEAVSEK SAETEKSAGA
     DERDPDEKQL VMDSHFVLPK RSTRSSRIIK PNKRLLEEGA ISTKKPLSLG DSKGKNVFGT
     SSSSAGSTAS TFSASTNLKL GKETFFNFGT LKPNSSAAGN FVLRQPRLQF QADNQQATFT
     APKACPTSPS AIPKPANSLA TSSFGSLAST NSSTVTPTPS ACSICSAVVS SKEVTQARKY
     GVVACDVCRK FFSKMTKKSI SANSSTANTS SGSQQYLQCK GNEGSPCSIH SAKSQLKNFK
     KFYKDRCTAC WLKKCMISFQ LPAAHRSRLS AILPPGMRGE AAAREEKSAE LLSPTGSLRF
     TSTASSSSPS VVASTSVKWK SSGDSTSALT SIKPNPLAEN NVTFGSTPLL RPAILENPLF
     LKISNAADQK LAAAEAISPS LTKKNSKQEK EKVKESEQSE KLLSPTQAGT KKSGAAEAQV
     EEVQPQKEEA PQTSTTTQPS ASNGASHGVP QAELAGETNA TGDTLKRQRI DLKGPRVKHV
     CRSASIVLGQ PLATFGEDQQ PEDAADMQQE IAAPVPSAIM EPSPEKPTHI VTDENDNCAS
     CKTSPVGDES KPSKSSGSAQ AEVKKATALG KEGTASAAGG SSAKVTTRNA AVASNLIVAA
     SKKQRNGDIA TSSSVTQSSN QTQGRKTKEH RQQRTLISID FWENYDPAEV CQTGFGLIVT
     ETVAQRALCF LCGSTGLDPL IFCACCCEPY HQYCVQDEYN LKHGSFEDTT LMGSLLETTV
     NASTGPSSSL NQLTQRLNWL CPRCTVCYTC NMSSGSKVKC QKCQKNYHST CLGTSKRLLG
     ADRPLICVNC LKCKSCSTTK VSKFVGNLPM CTGCFKLRKK GNFCPICQRC YDDNDFDLKM
     MECGDCGQWV HSKCEGLSDE QYNLLSTLPE SIEFICKKCA RRNESSKIKA EEWRQAVMEE
     FKASLYSVLK LLSKSRQACA LLKLSPRKKL RCTCGASSNQ GKLQPKALQF SSGSDNGLGS
     DGESQNSDDV YEFKDQQQQQ QQRNANMNKP RVKSLPCSCQ QHISHSQSFS LVDIKQKIAG
     NSYVSLAEFN YDMSQVIQQS NCDELDIAYK ELLSEQFPWF QNETKACTDA LEEDMFESCS
     GGNYEDLQDT GGVSASVYNE HSTSQAESRS GVLDIPLEEV DDFGSCGIKM RLDTRMCLFC
     RKSGEGLSGE EARLLYCGHD CWVHTNCAMW SAEVFEEIDG SLQNVHSAVA RGRMIKCTVC
     GNRGATVGCN VRSCGEHYHY PCARSIDCAF LTDKSMYCPA HAKNGNALKA NGSPSVTYES
     NFEVSRPVYV ELDRKRKKLI EPARVQFHIG SLEVRQLGAI VPRFSDSYEA VVPINFLCSR
     LYWSSKEPWK IVEYTVRTTI QNSSSTLTAL DVGRNYTVDH TNPNSKEVQL GMAQIARWHT
     SLARSEFLEN GGTDWSGEFP NPNSCVPPDE NTEEEPQQQA DLLPPELKDA IFEDLPHELL
     DGISMLDIFL YDDKTDLFAI SEQSKDGTQA MTSNQAQNQN QQAGGANSVS ICDEDTRNSN
     TSLGNGWPAS NPVEDAMLSA ARNSSQVQML KTLAWPKLDG NSAMATAIKR RKLSKNLAEG
     VFLTLSSQQR NKKEMATVAG VSRRQSISET SVEGVATTSG SVRSKSFTWS AAKRYFEKSE
     GREEAAKMRI MQMDGVDDSI TEFRIISGDG NLSTAQFSGQ VKCDRCQCTY RNYDAFQRHL
     PSCSPTMSSN ETESDVSGQG MTNNATQISA ESLNELQKQL LANAGGLNYL QSATSFPQVQ
     SLGSLGQFGL QGLQQLQLQP QSLGSGFFLS QPNPATQANT DDLQIYANSL QSLAANLGGG
     FTLAQPTVTA PAQPQLIAVS TNPDGTQQFI QIPQTMQATT TPTATYQTLQ ATNTDKKIML
     PLTAAGKPLK TVATKAAQQA AVKQRQLKSG HQVKPIQAKL QPHPQQHQQQ QQTQVQQPIT
     VMGQNLLQPQ LLFQSSTQTQ APQIILPQAQ PQNIISFVTG DGSQGQPLQY ISIPTAGEYK
     PQPQPTATPT FLTTAPGAGA TYLQTDASGN LVLTTTPSNS GLQMLTAQSL QAQPQVIGTL
     IQPQTIQLGG GADGNQPGSN QQPLILGGTG GGSSGLEFAT TSPQVILATQ PMYYGLETIV
     QNTVMSSQQF VSTAMPGMLS QNASFSATTT QVFQASKIEP IVDLPAGYVV LNNTGDASSA
     GTFLNAASVL QQQTQDDTTT QILQNANFQF QSVPTSSGAS TSMDYTSPVM VTAKIPPVTQ
     IKRTNAQAKA AGISGVGKVP PQPQVVNKVL PTSIVTQQSQ VQVKNSNLKQ SQVKGKAASG
     TGTTCGAPPS IASKPLQKKT NMIRPIHKLE VKPKVMKPTP KVQNQNHSLL QQQQQQQPQL
     QQQIPAVVVN QVPKVTISQQ RIPAQTQQQQ LQQAQMIHIP QQQQPLQQQQ VQVQPSMPII
     TLAEAPVVQS QFVMEPQALE QQELANRVQH FSTSSSSSSS NCSLPTNVVN PMQQQAPSTT
     SSSTTRPTNR VLPMQQRQEP APLSNECPVV SSPTPPKPVE QPIIHQMTSA SVSKCYAQKS
     TLPSPVYEAE LKVSSVLESI VPDVTMDAIL EEQPVTESIY TEGLYEKNSP GESKTEQLLL
     QQQQREQLNQ QLVNNGYLLD KHTFQVEPMD TDVYREEDLE EEEDEDDDFS LKMATSACND
     HEMSDSEEPA VKDKISKILD NLTNDDCADS IATATTMEVD ASAGYQQMVE DVLATTAAQS
     APTEEFEGAL ETAAVEAAAT YINEMADAHV LDLKQLQNGV ELELRRRKEE QRTVSQEQEQ
     SKAAIVPTAA APEPPQPIQE PKKMTGPHLL YEIQSEDGFT YKSSSITEIW EKVFEAVQVA
     RRAHGLTPLP EGPLADMGGI QMIGLKTNAL KYLIEQLPGV EKCSKYTPKY HKRNGNVSTA
     ANGAHGGNLG GSSASAALSV SGGDSHGLLD YGSDQDELEE NAYDCARCEP YSNRSEYDMF
     SWLASRHRKQ PIQVFVQPSD NELVPRRGTG SNLPMAMKYR TLKETYKDYV GVFRSHIHGR
     GLYCTKDIEA GEMVIEYAGE LIRSTLTDKR ERYYDSRGIG CYMFKIDDNL VVDATMRGNA
     ARFINHCCEP NCYSKVVDIL GHKHIIIFAL RRIVQGEELT YDYKFPFEDE KIPCSCGSKR
     CRKYLN
//
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