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Database: UniProt
Entry: Q6EVK6
LinkDB: Q6EVK6
Original site: Q6EVK6 
ID   BRM_ARATH               Reviewed;        2193 AA.
AC   Q6EVK6; O82366; O82780;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   16-OCT-2019, entry version 128.
DE   RecName: Full=ATP-dependent helicase BRM {ECO:0000303|PubMed:15371304};
DE            EC=3.6.4.12;
DE   AltName: Full=Protein BRAHMA {ECO:0000303|PubMed:15371304};
DE            Short=AtBRM {ECO:0000303|PubMed:15371304};
DE   AltName: Full=Protein CHROMATIN REMODELING 2 {ECO:0000303|PubMed:16547115};
DE            Short=AtCHR2 {ECO:0000303|PubMed:16547115};
GN   Name=BRM {ECO:0000303|PubMed:15371304};
GN   Synonyms=CHR2 {ECO:0000303|PubMed:16547115};
GN   OrderedLocusNames=At2g46020 {ECO:0000312|Araport:AT2G46020};
GN   ORFNames=F4I18, T3F17.33 {ECO:0000312|EMBL:AAC62901.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SWI3C AND
RP   BSH, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=15371304; DOI=10.1242/dev.01363;
RA   Farrona S., Hurtado L., Bowman J.L., Reyes J.C.;
RT   "The Arabidopsis thaliana SNF2 homolog AtBRM controls shoot
RT   development and flowering.";
RL   Development 131:4965-4975(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
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   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16547115; DOI=10.1534/genetics.105.051664;
RA   Shaked H., Avivi-Ragolsky N., Levy A.A.;
RT   "Involvement of the Arabidopsis SWI2/SNF2 chromatin remodeling gene
RT   family in DNA damage response and recombination.";
RL   Genetics 173:985-994(2006).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH SWI3A; SWI3B AND SWI3D.
RX   PubMed=16845477; DOI=10.1007/s11103-006-9021-2;
RA   Hurtado L., Farrona S., Reyes J.C.;
RT   "The putative SWI/SNF complex subunit BRAHMA activates flower homeotic
RT   genes in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 62:291-304(2006).
RN   [6]
RP   INTERACTION WITH HISTONES H3 AND H4.
RX   PubMed=17825834; DOI=10.1016/j.jmb.2007.07.012;
RA   Farrona S., Hurtado L., Reyes J.C.;
RT   "A nucleosome interaction module is required for normal function of
RT   Arabidopsis thaliana BRAHMA.";
RL   J. Mol. Biol. 373:240-250(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=17293567; DOI=10.1105/tpc.106.048272;
RA   Bezhani S., Winter C., Hershman S., Wagner J.D., Kennedy J.F.,
RA   Kwon C.S., Pfluger J., Su Y., Wagner D.;
RT   "Unique, shared, and redundant roles for the Arabidopsis SWI/SNF
RT   chromatin remodeling ATPases BRAHMA and SPLAYED.";
RL   Plant Cell 19:403-416(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1641, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Root;
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
RA   Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
RA   Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by
RT   mass spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF GLY-1138.
RX   PubMed=18508955; DOI=10.1104/pp.108.121996;
RA   Tang X., Hou A., Babu M., Nguyen V., Hurtado L., Lu Q., Reyes J.C.,
RA   Wang A., Keller W.A., Harada J.J., Tsang E.W.T., Cui Y.;
RT   "The Arabidopsis BRAHMA chromatin-remodeling ATPase is involved in
RT   repression of seed maturation genes in leaves.";
RL   Plant Physiol. 147:1143-1157(2008).
RN   [10]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP   SER-2137, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
RA   Andreasson E., Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from
RT   Arabidopsis thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1641, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [13]
RP   INTERACTION WITH LFY.
RX   PubMed=22323601; DOI=10.1073/pnas.1113409109;
RA   Wu M.F., Sang Y., Bezhani S., Yamaguchi N., Han S.K., Li Z., Su Y.,
RA   Slewinski T.L., Wagner D.;
RT   "SWI2/SNF2 chromatin remodeling ATPases overcome polycomb repression
RT   and control floral organ identity with the LEAFY and SEPALLATA3
RT   transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:3576-3581(2012).
RN   [14]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
RN   [15]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH FGT1.
RC   STRAIN=cv. Columbia;
RX   PubMed=27680998; DOI=10.7554/elife.17061;
RA   Brzezinka K., Altmann S., Czesnick H., Nicolas P., Gorka M., Benke E.,
RA   Kabelitz T., Jaehne F., Graf A., Kappel C., Baeurle I.;
RT   "Arabidopsis FORGETTER1 mediates stress-induced chromatin memory
RT   through nucleosome remodeling.";
RL   Elife 5:0-0(2016).
RN   [16]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH REF6.
RX   PubMed=27111034; DOI=10.1038/ng.3555;
RA   Li C., Gu L., Gao L., Chen C., Wei C.Q., Qiu Q., Chien C.W., Wang S.,
RA   Jiang L., Ai L.F., Chen C.Y., Yang S., Nguyen V., Qi Y., Snyder M.P.,
RA   Burlingame A.L., Kohalmi S.E., Huang S., Cao X., Wang Z.Y., Wu K.,
RA   Chen X., Cui Y.;
RT   "Concerted genomic targeting of H3K27 demethylase REF6 and chromatin-
RT   remodeling ATPase BRM in Arabidopsis.";
RL   Nat. Genet. 48:687-693(2016).
CC   -!- FUNCTION: ATPase subunit of a multiprotein complex equivalent of
CC       the SWI/SNF complex that acts by remodeling the chromatin by
CC       catalyzing an ATP-dependent alteration in the structure of
CC       nucleosomal DNA. Represses embryonic genes in leaves and controls
CC       shoot development and flowering. Activates flower homeotic genes.
CC       The association of BRM with its target genes requires REF6
CC       (PubMed:27111034). Necessary to acquire heat stress (HS) memory,
CC       by globally binding to HS memory genes (PubMed:27680998).
CC       {ECO:0000269|PubMed:16845477, ECO:0000269|PubMed:17293567,
CC       ECO:0000269|PubMed:18508955, ECO:0000269|PubMed:27111034,
CC       ECO:0000269|PubMed:27680998}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Interacts with SWI3B, SWI3C, H3 and H4, but not with
CC       SWI3A, SWI3D or BSH (PubMed:15371304, PubMed:16845477,
CC       PubMed:17825834). Interacts with LFY (PubMed:22323601). Interacts
CC       with REF6 (PubMed:27111034). Binds to FGT1 (PubMed:27680998).
CC       {ECO:0000269|PubMed:15371304, ECO:0000269|PubMed:16845477,
CC       ECO:0000269|PubMed:17825834, ECO:0000269|PubMed:22323601,
CC       ECO:0000269|PubMed:27111034, ECO:0000269|PubMed:27680998}.
CC   -!- INTERACTION:
CC       Q00958:LFY; NbExp=3; IntAct=EBI-2025535, EBI-1644366;
CC       Q9ZVD0:SE; NbExp=6; IntAct=EBI-2025535, EBI-6553299;
CC       O22456:SEP3; NbExp=2; IntAct=EBI-2025535, EBI-592020;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00768, ECO:0000269|PubMed:15371304,
CC       ECO:0000269|PubMed:19245862, ECO:0000269|PubMed:27111034}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6EVK6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6EVK6-2; Sequence=VSP_034709;
CC         Note=Derived from EST data. No experimental confirmation
CC         available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in inflorescences and leaves.
CC       Low expression in siliques, roots and seedlings. Detected in shoot
CC       apical meristem, root meristem, vascular tissue of developing
CC       leaves, petals, stamens filaments, anthers and carpels.
CC       {ECO:0000269|PubMed:15371304}.
CC   -!- DOMAIN: The bromodomain binds histones.
CC   -!- DOMAIN: The AT-hook region (1568-1919) contains at least 3 DNA-
CC       binding sites with different characteristics.
CC   -!- DISRUPTION PHENOTYPE: Sterility. Reduced heat stress (HS) memory
CC       associated with a premature decline of expression of HSA32,
CC       HSP18.2, HSP21, HSP22 and HSP101 after HS. The double mutant brm-1
CC       fgt1-1 exhibits retarted seedling development resulting in reduced
CC       development and delayed leaf initiation, as well as delayed
CC       flowering time. {ECO:0000269|PubMed:27680998}.
CC   -!- MISCELLANEOUS: Was previously split between At2g46010 and
CC       At2g46020.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC62900.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAC62901.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAM14971.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AJ703891; CAG28313.1; -; mRNA.
DR   EMBL; AC004665; AAM14971.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC005397; AAC62900.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC005397; AAC62901.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC10632.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10633.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61549.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61550.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61551.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61552.1; -; Genomic_DNA.
DR   PIR; G84897; G84897.
DR   RefSeq; NP_001318432.1; NM_001337166.1. [Q6EVK6-2]
DR   RefSeq; NP_001323760.1; NM_001337168.1. [Q6EVK6-1]
DR   RefSeq; NP_001323761.1; NM_001337169.1. [Q6EVK6-2]
DR   RefSeq; NP_001323762.1; NM_001337167.1. [Q6EVK6-1]
DR   RefSeq; NP_182126.2; NM_130165.3. [Q6EVK6-2]
DR   RefSeq; NP_973695.1; NM_201966.2. [Q6EVK6-1]
DR   SMR; Q6EVK6; -.
DR   BioGrid; 4545; 170.
DR   DIP; DIP-46526N; -.
DR   IntAct; Q6EVK6; 7.
DR   STRING; 3702.AT2G46020.2; -.
DR   iPTMnet; Q6EVK6; -.
DR   PaxDb; Q6EVK6; -.
DR   PRIDE; Q6EVK6; -.
DR   EnsemblPlants; AT2G46020.1; AT2G46020.1; AT2G46020. [Q6EVK6-2]
DR   EnsemblPlants; AT2G46020.2; AT2G46020.2; AT2G46020. [Q6EVK6-1]
DR   EnsemblPlants; AT2G46020.3; AT2G46020.3; AT2G46020. [Q6EVK6-1]
DR   EnsemblPlants; AT2G46020.4; AT2G46020.4; AT2G46020. [Q6EVK6-1]
DR   EnsemblPlants; AT2G46020.5; AT2G46020.5; AT2G46020. [Q6EVK6-2]
DR   EnsemblPlants; AT2G46020.6; AT2G46020.6; AT2G46020. [Q6EVK6-2]
DR   GeneID; 819210; -.
DR   Gramene; AT2G46020.1; AT2G46020.1; AT2G46020. [Q6EVK6-2]
DR   Gramene; AT2G46020.2; AT2G46020.2; AT2G46020. [Q6EVK6-1]
DR   Gramene; AT2G46020.3; AT2G46020.3; AT2G46020. [Q6EVK6-1]
DR   Gramene; AT2G46020.4; AT2G46020.4; AT2G46020. [Q6EVK6-1]
DR   Gramene; AT2G46020.5; AT2G46020.5; AT2G46020. [Q6EVK6-2]
DR   Gramene; AT2G46020.6; AT2G46020.6; AT2G46020. [Q6EVK6-2]
DR   KEGG; ath:AT2G46020; -.
DR   Araport; AT2G46020; -.
DR   TAIR; locus:2062999; AT2G46020.
DR   eggNOG; KOG0386; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   HOGENOM; HOG000029719; -.
DR   InParanoid; Q6EVK6; -.
DR   KO; K11647; -.
DR   OMA; KPLRNMA; -.
DR   OrthoDB; 685477at2759; -.
DR   PhylomeDB; Q6EVK6; -.
DR   PRO; PR:Q6EVK6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q6EVK6; baseline and differential.
DR   Genevisible; Q6EVK6; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0010199; P:organ boundary specification between lateral organs and the meristem; IGI:TAIR.
DR   GO; GO:1900036; P:positive regulation of cellular response to heat; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR.
DR   GO; GO:1903798; P:regulation of production of miRNAs involved in gene silencing by miRNA; IDA:TAIR.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR031056; BRM.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF978; PTHR10799:SF978; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00951; QLQ; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51666; QLQ; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; ATP-binding;
KW   Bromodomain; Chromatin regulator; Coiled coil; Complete proteome;
KW   Developmental protein; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   2193       ATP-dependent helicase BRM.
FT                                /FTId=PRO_0000343902.
FT   DOMAIN      463    499       QLQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01001}.
FT   DOMAIN      993   1158       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1312   1489       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     1918   1988       Bromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00035}.
FT   NP_BIND    1006   1013       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED       38     58       {ECO:0000255}.
FT   COILED      726    795       {ECO:0000255}.
FT   COILED     1109   1129       {ECO:0000255}.
FT   COILED     1618   1638       {ECO:0000255}.
FT   MOTIF       705    712       Nuclear localization signal 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00768}.
FT   MOTIF      1901   1908       Nuclear localization signal 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00768}.
FT   COMPBIAS     30     37       Poly-Ser. {ECO:0000255}.
FT   COMPBIAS     39    262       Gln-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00006}.
FT   COMPBIAS    302    356       Ser-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00016}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:22223895}.
FT   MOD_RES    1641   1641       Phosphoserine.
FT                                {ECO:0000244|PubMed:18433157,
FT                                ECO:0000244|PubMed:19376835}.
FT   MOD_RES    2137   2137       Phosphoserine.
FT                                {ECO:0000244|PubMed:19245862}.
FT   VAR_SEQ    1075   1079       EVCAM -> VKFE (in isoform 2).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_034709.
FT   MUTAGEN    1138   1138       G->R: In brm-5/essp3; ectopic expression
FT                                of seed storage proteins in leaves.
FT                                {ECO:0000269|PubMed:18508955}.
SQ   SEQUENCE   2193 AA;  245469 MW;  ECC557B079A91301 CRC64;
     MQSGGSGGGP ARNPAMGPAG RTASTSSAAS PSSSSSSVQQ QQQQQQQQQQ QQQLASRQQQ
     QQHRNSDTNE NMFAYQPGGV QGMMGGGNFA SSPGSMQMPQ QSRNFFESPQ QQQQQQQQGS
     STQEGQQNFN PMQQAYIQFA MQAQHQKAQQ QARMGMVGSS SVGKDQDARM GMLNMQDLNP
     SSQPQASSSK PSGDQFARGE RQTESSSQQR NETKSHPQQQ VGTGQLMPGN MIRPMQAPQA
     QQLVNNMGNN QLAFAQQWQA MQAWARERNI DLSHPANASQ MAHILQARMA AQQKAGEGNV
     ASQSPSIPIS SQPASSSVVP GENSPHANSA SDISGQSGSA KARHALSTGS FASTSSPRMV
     NPAMNPFSGQ GRENPMYPRH LVQPTNGMPS GNPLQTSANE TPVLDQNAST KKSLGPAEHL
     QMQQPRQLNT PTPNLVAPSD TGPLSNSSLQ SGQGTQQAQQ RSGFTKQQLH VLKAQILAFR
     RLKKGEGSLP PELLQAISPP PLELQTQRQI SPAIGKVQDR SSDKTGEDQA RSLECGKESQ
     AAASSNGPIF SKEEDNVGDT EVALTTGHSQ LFQNLGKEAT STDVATKEEQ QTDVFPVKSD
     QGADSSTQKN PRSDSTADKG KAVASDGSQS KVPPQANSPQ PPKDTASARK YYGPLFDFPF
     FTRKLDSYGS ATANANNNLT LAYDIKDLIC EEGAEFLSKK RTDSLKKING LLAKNLERKR
     IRPDLVLRLQ IEEKKLRLSD LQSRVREEVD RQQQEIMSMP DRPYRKFVRL CERQRLEMNR
     QVLANQKAVR EKQLKTIFQW RKKLLEAHWA IRDARTARNR GVAKYHEKML REFSKRKDDG
     RNKRMEALKN NDVERYREML LEQQTNMPGD AAERYAVLSS FLTQTEDYLH KLGGKITATK
     NQQEVEEAAN AAAVAARLQG LSEEEVRAAA TCAREEVVIR NRFTEMNAPK ENSSVNKYYT
     LAHAVNEVVV RQPSMLQAGT LRDYQLVGLQ WMLSLYNNKL NGILADEMGL GKTVQVMALI
     AYLMEFKGNY GPHLIIVPNA VLVNWKSELH TWLPSVSCIY YVGTKDQRSK LFSQEVCAMK
     FNVLVTTYEF IMYDRSKLSK VDWKYIIIDE AQRMKDRESV LARDLDRYRC QRRLLLTGTP
     LQNDLKELWS LLNLLLPDVF DNRKAFHDWF AQPFQKEGPA HNIEDDWLET EKKVIVIHRL
     HQILEPFMLR RRVEDVEGSL PAKVSVVLRC RMSAIQSAVY DWIKATGTLR VDPDDEKLRA
     QKNPIYQAKI YRTLNNRCME LRKACNHPLL NYPYFNDFSK DFLVRSCGKL WILDRILIKL
     QRTGHRVLLF STMTKLLDIL EEYLQWRRLV YRRIDGTTSL EDRESAIVDF NDPDTDCFIF
     LLSIRAAGRG LNLQTADTVV IYDPDPNPKN EEQAVARAHR IGQTREVKVI YMEAVVEKLS
     SHQKEDELRS GGSVDLEDDM AGKDRYIGSI EGLIRNNIQQ YKIDMADEVI NAGRFDQRTT
     HEERRMTLET LLHDEERYQE TVHDVPSLHE VNRMIARSEE EVELFDQMDE EFDWTEEMTN
     HEQVPKWLRA STREVNATVA DLSKKPSKNM LSSSNLIVQP GGPGGERKRG RPKSKKINYK
     EIEDDIAGYS EESSEERNID SGNEEEGDIR QFDDDELTGA LGDHQTNKGE FDGENPVCGY
     DYPPGSGSYK KNPPRDDAGS SGSSPESHRS KEMASPVSSQ KFGSLSALDT RPGSVSKRLL
     DDLEEGEIAA SGDSHIDLQR SGSWAHDRDE GDEEQVLQPT IKRKRSIRLR PRQTAERVDG
     SEMPAAQPLQ VDRSYRSKLR TVVDSHSSRQ DQSDSSSRLR SVPAKKVAST SKLHVSSPKS
     GRLNATQLTV EDNAEASRET WDGTSPISSS NAGARMSHII QKRCKIVISK LQRRIDKEGQ
     QIVPMLTNLW KRIQNGYAAG GVNNLLELRE IDHRVERLEY AGVMELASDV QLMLRGAMQF
     YGFSHEVRSE AKKVHNLFFD LLKMSFPDTD FREARNALSF SGSAPTLVST PTPRGAGISQ
     GKRQKLVNEP ETEPSSPQRS QQRENSRIRV QIPQKETKLG GTTSHTDESP ILAHPGELVI
     CKKKRKDREK SGPKTRTGGS SSPVSPPPAM IGRGLRSPVS GGVPRETRLA QQQRWPNQPT
     HPNNSGAAGD SVGWANPVKR LRTDSGKRRP SHL
//
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