DRMH1_ARATH
ID DRMH1_ARATH Reviewed; 108 AA.
AC P93017; Q8RYC4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Dormancy-associated protein homolog 1 {ECO:0000303|PubMed:15908603};
DE AltName: Full=Auxin-repressed protein 1 {ECO:0000303|PubMed:23065269};
DE Short=AtARP1 {ECO:0000303|PubMed:23065269};
DE AltName: Full=DRM1 homolog 1 {ECO:0000303|PubMed:15908603};
DE AltName: Full=Dormancy-associated protein 2 {ECO:0000303|PubMed:24442277};
DE Short=AtDRM2 {ECO:0000303|PubMed:24442277};
GN Name=DRMH1 {ECO:0000305};
GN Synonyms=ARP1 {ECO:0000303|PubMed:23065269},
GN DRM2 {ECO:0000303|PubMed:24442277};
GN OrderedLocusNames=At2g33830 {ECO:0000312|Araport:AT2G33830};
GN ORFNames=T1B8.13 {ECO:0000312|EMBL:AAK32858.1};
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 {ECO:0000312|EMBL:BAB17679.1};
RN [1]
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., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND THR-50, AND
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 [8]
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 [9]
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).
RN [10]
RP ALTERNATIVE SPLICING, TISSUE 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).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P93017-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P93017-2; Sequence=VSP_058256;
CC -!- TISSUE SPECIFICITY: Expressed mainly in the low bolt.
CC {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 heat (PubMed:24442277). Up-
CC regulated by salt, cold and dark growth conditions (PubMed:24442277).
CC {ECO:0000269|PubMed:15908603, ECO:0000269|PubMed:23616605,
CC 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 -!- SIMILARITY: Belongs to the DRM1/ARP family. {ECO:0000305}.
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DR EMBL; U78721; AAC69134.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08891.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08892.1; -; Genomic_DNA.
DR EMBL; AB050786; BAB17679.1; -; mRNA.
DR EMBL; AF361846; AAK32858.1; -; mRNA.
DR EMBL; AY066049; AAL47416.1; -; mRNA.
DR EMBL; AY085689; AAM62908.1; -; mRNA.
DR PIR; B84750; B84750.
DR RefSeq; NP_001318345.1; NM_001336474.1. [P93017-2]
DR RefSeq; NP_850220.1; NM_179889.3. [P93017-1]
DR AlphaFoldDB; P93017; -.
DR IntAct; P93017; 1.
DR STRING; 3702.AT2G33830.2; -.
DR iPTMnet; P93017; -.
DR PaxDb; P93017; -.
DR PRIDE; P93017; -.
DR ProteomicsDB; 224355; -. [P93017-1]
DR EnsemblPlants; AT2G33830.1; AT2G33830.1; AT2G33830. [P93017-2]
DR EnsemblPlants; AT2G33830.2; AT2G33830.2; AT2G33830. [P93017-1]
DR GeneID; 817950; -.
DR Gramene; AT2G33830.1; AT2G33830.1; AT2G33830. [P93017-2]
DR Gramene; AT2G33830.2; AT2G33830.2; AT2G33830. [P93017-1]
DR KEGG; ath:AT2G33830; -.
DR Araport; AT2G33830; -.
DR TAIR; locus:2057584; AT2G33830.
DR eggNOG; ENOG502S158; Eukaryota.
DR InParanoid; P93017; -.
DR OMA; TAQPIDM; -.
DR PhylomeDB; P93017; -.
DR PRO; PR:P93017; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P93017; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0009617; P:response to bacterium; IDA: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..108
FT /note="Dormancy-associated protein homolog 1"
FT /id="PRO_0000436080"
FT REGION 28..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 31..32
FT /note="Missing (in isoform 2)"
FT /id="VSP_058256"
SQ SEQUENCE 108 AA; 11656 MW; 0F71F4EE24872D7A CRC64;
MWDETVAGPK PEHGLGRLRN KITTQPLDIK GVGEGSSSKT VAAVAGSPGT PTTPGSARKE
NVWRSVFHPG SNIATRGMGT NLFDKPSHPN SPTVYDWLYS DDTRSKHR
