TRR_DROME
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 03-AUG-2022, entry version 163.
DE RecName: Full=Histone-lysine N-methyltransferase trr;
DE EC=2.1.1.354 {ECO:0000269|PubMed:14603321};
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; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC 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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., 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., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., 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., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA 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., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT 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., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., 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., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA 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 which
RT encodes a novel SET domain protein.";
RL Mech. Dev. 82:171-179(1999).
RN [6]
RP FUNCTION, CATALYTIC 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 development of
RT Drosophila.";
RL Nature 426:78-83(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1486; SER-1488 AND SER-1490,
RP 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 histone
RT methyltransferase Trr.";
RL Mol. Biol. Cell 24:361-372(2013).
CC -!- FUNCTION: Histone methyltransferase that acts as a coactivator for the
CC ecdysone receptor during development. Specifically trimethylates 'Lys-
CC 4' of histone H3, a specific tag for epigenetic transcriptional
CC activation. Recruited by EcR in an ecdysone-dependent manner causing H3
CC 'Lys-4' trimethylation at ecdysone-inducible promoters, leading to
CC activate expression. Plays a central role in the developing compound
CC eye, during the progression of the morphogenetic furrow and in post-
CC furrow differentiation of the retinal epithelium, notably by activating
CC expression of hh. Also required for wing and abdominal development.
CC {ECO:0000269|PubMed:14603321, ECO:0000269|PubMed:23197473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
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, Utx,
CC Lpt and Ncoa6. Interacts with nuclear receptor EcR in an ecdysone-
CC dependent manner. Interacts with ash2; the interaction stabilizes trr.
CC {ECO:0000269|PubMed:14603321, ECO:0000269|PubMed:21875999,
CC ECO:0000269|PubMed:23197473}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14603321}. Chromosome
CC {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 -!- TISSUE SPECIFICITY: Widely expressed. {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. Expressed
CC uniformly at the preblastoderm stage, prior to the onset of zygotic
CC transcription. In ovaries, it is not expressed in ovarian stem cells,
CC oogonia or early cysts and is first detectable at stage 8 in nurse
CC cells. At stage 10, it is expressed in the anterior end of the oocyte,
CC and is uniformly distributed later on. Expressed almost uniformly in
CC embryos from precellular blastoderm stage to the germband extended
CC stage. At the germband extended stage, it is enriched in the mesoderm.
CC During germband retraction, it is strongly expressed in the anterior
CC and posterior midgut. At the germband retracted stage, it becomes less
CC abundant and is mainly localized to the ventral nerve cord and the
CC brain. In third instar larvae, it is strongly and almost ubiquitously
CC expressed in all imaginal disks. Also weakly expressed expression in
CC salivary 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 2 is
CC essential for the association with nuclear receptor EcR.
CC -!- DISRUPTION PHENOTYPE: Defects in mechanosensory bristle spacing and
CC differentiation in wings and lack of chaetes and macrochaetes in
CC abdominal a4 and a5 segments. {ECO:0000269|PubMed:23197473}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39418.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM29656.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA15944.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q8IRW8; -.
DR SMR; Q8IRW8; -.
DR BioGRID; 57695; 30.
DR ELM; Q8IRW8; -.
DR IntAct; Q8IRW8; 11.
DR STRING; 7227.FBpp0070347; -.
DR iPTMnet; Q8IRW8; -.
DR PaxDb; 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; 31149; -.
DR FlyBase; FBgn0023518; trr.
DR VEuPathDB; VectorBase:FBgn0023518; -.
DR eggNOG; KOG4443; Eukaryota.
DR GeneTree; ENSGT00940000168851; -.
DR InParanoid; Q8IRW8; -.
DR OMA; RDIVICT; -.
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 BioGRID-ORCS; 31149; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31149; -.
DR PRO; PR:Q8IRW8; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0023518; Expressed in egg cell and 29 other tissues.
DR ExpressionAtlas; Q8IRW8; baseline and differential.
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:0001046; F:core promoter sequence-specific DNA binding; IDA:FlyBase.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:FlyBase.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; IMP: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; IDA:FlyBase.
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; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 SUPFAM; SSF82199; SSF82199; 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 Developmental protein; Metal-binding; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2431
FT /note="Histone-lysine N-methyltransferase trr"
FT /id="PRO_0000259524"
FT DOMAIN 2061..2121
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 2122..2209
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT DOMAIN 2291..2407
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 2415..2431
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 1895..1935
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 1956..2003
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 34..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1478..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1790..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 801..805
FT /note="LXXLL motif 1"
FT MOTIF 1652..1656
FT /note="LXXLL motif 2"
FT MOTIF 2060..2064
FT /note="LXXLL motif 3"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1486
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1488
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1490
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 140..161
FT /note="SEYRISTPRNSQSNPLLHRNTA -> T (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021439"
FT CONFLICT 219
FT /note="S -> A (in Ref. 3; CAA15944)"
FT /evidence="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
