DRM1_ARATH
ID DRM1_ARATH Reviewed; 132 AA.
AC B9DGG8; F4HWK7; F4HWK9; O65923;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Dormancy-associated protein 1 {ECO:0000303|Ref.1};
DE Short=AtDRM1 {ECO:0000303|Ref.1};
DE AltName: Full=Dormancy-associated protein-like 1 {ECO:0000303|PubMed:11130712};
DE Short=AtDYL1;
GN Name=DRM1 {ECO:0000303|Ref.1}; Synonyms=DYL1 {ECO:0000303|PubMed:11130712};
GN OrderedLocusNames=At1g28330 {ECO:0000312|Araport:AT1G28330};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RA Stafstrom J.P., Krueger M.T., Stoudt W.;
RT "Nucleotide sequence of Atdrm1-1 cDNA and genomic clones, an Arabidopsis
RT homolog of a dormant, bud-associated gene from pea.";
RL (er) Plant Gene Register PGR98-099(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, INDUCTION, AND TOPOLOGY.
RX PubMed=24442277; DOI=10.1007/s00438-013-0804-2;
RA Rae G.M., Uversky V.N., David K., Wood M.;
RT "DRM1 and DRM2 expression regulation: potential role of splice variants in
RT response to stress and environmental factors in Arabidopsis.";
RL Mol. Genet. Genomics 289:317-332(2014).
RN [3]
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., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., 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., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP INDUCTION BY DECAPITATION.
RX PubMed=15908603; DOI=10.1104/pp.104.057984;
RA Tatematsu K., Ward S., Leyser O., Kamiya Y., Nambara E.;
RT "Identification of cis-elements that regulate gene expression during
RT initiation of axillary bud outgrowth in Arabidopsis.";
RL Plant Physiol. 138:757-766(2005).
RN [8]
RP INDUCTION BY SUGARS.
RX PubMed=16463203; DOI=10.1007/s10265-005-0251-1;
RA Gonzali S., Loreti E., Solfanelli C., Novi G., Alpi A., Perata P.;
RT "Identification of sugar-modulated genes and evidence for in vivo sugar
RT sensing in Arabidopsis.";
RL J. Plant Res. 119:115-123(2006).
RN [9]
RP IDENTIFICATION 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 [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=23065269; DOI=10.1007/s11033-012-2050-9;
RA Lee J., Han C.T., Hur Y.;
RT "Molecular characterization of the Brassica rapa auxin-repressed,
RT superfamily genes, BrARP1 and BrDRM1.";
RL Mol. Biol. Rep. 40:197-209(2013).
RN [11]
RP INDUCTION BY ERF114.
RX PubMed=23616605; DOI=10.1104/pp.113.214049;
RA Mehrnia M., Balazadeh S., Zanor M.I., Mueller-Roeber B.;
RT "EBE, an AP2/ERF transcription factor highly expressed in proliferating
RT cells, affects shoot architecture in Arabidopsis.";
RL Plant Physiol. 162:842-857(2013).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=B9DGG8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B9DGG8-2; Sequence=VSP_058252;
CC Name=3;
CC IsoId=B9DGG8-3; Sequence=VSP_058255;
CC Name=4;
CC IsoId=B9DGG8-4; Sequence=VSP_058253;
CC Name=5;
CC IsoId=B9DGG8-5; Sequence=VSP_058254;
CC -!- TISSUE SPECIFICITY: Isoform 1: Expressed mainly in the low bolt.
CC Isoform 2: Expressed mainly in the low bolt. Detected in flowers.
CC Isoform 4: Expressed mainly in the low bolt. Isoform 5: Expressed
CC mainly in the 6 days old seedlings. Detected in 16 days old seedlings,
CC axil, low bolt and floral samples, but only barely in leaves and top
CC bolt. {ECO:0000269|PubMed:24442277}.
CC -!- INDUCTION: Circadian-regulation (PubMed:24442277). Down-regulated in
CC axillary buds within 24 hours after decapitation and then up-regulated
CC (PubMed:15908603). Down-regulated by the transcription factor ERF114
CC (PubMed:23616605). Down-regulated by cold (PubMed:24442277). Almost
CC complete down-regulation by sucrose, fructose and glucose, but not by
CC other sugars (PubMed:16463203). Up-regulated by heat and dark growth
CC conditions (PubMed:24442277). Isoform 2: Up-regulated by salt. Isoform
CC 4: Up-regulated by salt. Isoform 1: Not up-regulated by salt. Isoform
CC 5: Not up-regulated by salt (PubMed:24442277).
CC {ECO:0000269|PubMed:15908603, ECO:0000269|PubMed:16463203,
CC ECO:0000269|PubMed:23616605, ECO:0000269|PubMed:24442277}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Drm1 and drmh1 double
CC mutants have no visible phenotype. {ECO:0000269|PubMed:23065269}.
CC -!- MISCELLANEOUS: Predicted to be an intrinsically disordered protein.
CC {ECO:0000303|PubMed:24442277}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be artifactual or particularly rare.
CC {ECO:0000269|PubMed:24442277}.
CC -!- SIMILARITY: Belongs to the DRM1/ARP family. {ECO:0000305}.
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DR EMBL; AF053746; AAC26202.1; -; mRNA.
DR EMBL; AF053747; AAC26203.1; -; Genomic_DNA.
DR EMBL; AC021044; AAF98422.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30954.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30955.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30956.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30957.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30958.2; -; Genomic_DNA.
DR EMBL; CP002684; ANM58145.1; -; Genomic_DNA.
DR EMBL; AY037227; AAK59827.1; -; mRNA.
DR EMBL; AY074825; AAL69521.1; -; mRNA.
DR EMBL; AK317149; BAH19835.1; -; mRNA.
DR PIR; T52190; T52190.
DR RefSeq; NP_001154378.1; NM_001160906.1. [B9DGG8-4]
DR RefSeq; NP_001319096.1; NM_001332808.1. [B9DGG8-5]
DR RefSeq; NP_001320602.1; NM_001332809.1. [B9DGG8-5]
DR RefSeq; NP_564305.1; NM_102599.3. [B9DGG8-2]
DR RefSeq; NP_849720.1; NM_179389.4. [B9DGG8-1]
DR RefSeq; NP_849721.1; NM_179390.1. [B9DGG8-1]
DR AlphaFoldDB; B9DGG8; -.
DR STRING; 3702.AT1G28330.5; -.
DR iPTMnet; B9DGG8; -.
DR PaxDb; B9DGG8; -.
DR PRIDE; B9DGG8; -.
DR ProteomicsDB; 224352; -. [B9DGG8-1]
DR EnsemblPlants; AT1G28330.1; AT1G28330.1; AT1G28330. [B9DGG8-2]
DR EnsemblPlants; AT1G28330.2; AT1G28330.2; AT1G28330. [B9DGG8-1]
DR EnsemblPlants; AT1G28330.3; AT1G28330.3; AT1G28330. [B9DGG8-1]
DR EnsemblPlants; AT1G28330.4; AT1G28330.4; AT1G28330. [B9DGG8-4]
DR EnsemblPlants; AT1G28330.5; AT1G28330.5; AT1G28330. [B9DGG8-5]
DR EnsemblPlants; AT1G28330.6; AT1G28330.6; AT1G28330. [B9DGG8-5]
DR GeneID; 839729; -.
DR Gramene; AT1G28330.1; AT1G28330.1; AT1G28330. [B9DGG8-2]
DR Gramene; AT1G28330.2; AT1G28330.2; AT1G28330. [B9DGG8-1]
DR Gramene; AT1G28330.3; AT1G28330.3; AT1G28330. [B9DGG8-1]
DR Gramene; AT1G28330.4; AT1G28330.4; AT1G28330. [B9DGG8-4]
DR Gramene; AT1G28330.5; AT1G28330.5; AT1G28330. [B9DGG8-5]
DR Gramene; AT1G28330.6; AT1G28330.6; AT1G28330. [B9DGG8-5]
DR KEGG; ath:AT1G28330; -.
DR Araport; AT1G28330; -.
DR TAIR; locus:2032226; AT1G28330.
DR eggNOG; ENOG502S158; Eukaryota.
DR OMA; IFDKPAH; -.
DR PhylomeDB; B9DGG8; -.
DR PRO; PR:B9DGG8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; B9DGG8; baseline and differential.
DR GO; GO:0009750; P:response to fructose; IEP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR InterPro; IPR008406; DRM/ARP.
DR PANTHER; PTHR33565; PTHR33565; 1.
DR Pfam; PF05564; Auxin_repressed; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..132
FT /note="Dormancy-associated protein 1"
FT /id="PRO_0000436079"
FT REGION 53..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P93017"
FT VAR_SEQ 111..132
FT /note="CVDNEAQRKEHVALCLVGAWIK -> WLYSGDSRSQHR (in isoform
FT 2)"
FT /id="VSP_058252"
FT VAR_SEQ 111..132
FT /note="CVDNEAQRKEHVALCLVGAWIK -> WLYSGDSRSQHQWIK (in
FT isoform 4)"
FT /id="VSP_058253"
FT VAR_SEQ 111..132
FT /note="CVDNEAQRKEHVALCLVGAWIK -> W (in isoform 5)"
FT /id="VSP_058254"
FT VAR_SEQ 131..132
FT /note="IK -> IKSRVVGSLIDRTWGVCRLYSGDSRSQHR (in isoform 3)"
FT /id="VSP_058255"
SQ SEQUENCE 132 AA; 14397 MW; E7C36CB6C231B276 CRC64;
MVLLEKLWDD VVAGPQPDRG LGRLRKITTQ PINIRDIGEG SSSKVVMHRS LTMPAAVSPG
TPTTPTTPTT PRKDNVWRSV FNPGSNLATR AIGSNIFDKP THPNSPSVYD CVDNEAQRKE
HVALCLVGAW IK
