DAR2_ARATH
ID DAR2_ARATH Reviewed; 528 AA.
AC Q0WSN2; O22291;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Protein DA1-related 2 {ECO:0000303|PubMed:18483219};
DE AltName: Full=Protein LATERAL ROOT DEVELOPMENT 3 {ECO:0000303|PubMed:21749503};
GN Name=DAR2 {ECO:0000303|PubMed:18483219};
GN Synonyms=LRD3 {ECO:0000303|PubMed:21749503}; OrderedLocusNames=At2g39830;
GN ORFNames=T5I7.13;
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 [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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18483219; DOI=10.1101/gad.463608;
RA Li Y., Zheng L., Corke F., Smith C., Bevan M.W.;
RT "Control of final seed and organ size by the DA1 gene family in Arabidopsis
RT thaliana.";
RL Genes Dev. 22:1331-1336(2008).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21749503; DOI=10.1111/j.1365-313x.2011.04700.x;
RA Ingram P., Dettmer J., Helariutta Y., Malamy J.E.;
RT "Arabidopsis Lateral Root Development 3 is essential for early phloem
RT development and function, and hence for normal root system development.";
RL Plant J. 68:455-467(2011).
RN [6]
RP FUNCTION.
RX PubMed=23296689; DOI=10.1104/pp.112.210237;
RA Peng Y., Ma W., Chen L., Yang L., Li S., Zhao H., Zhao Y., Jin W., Li N.,
RA Bevan M.W., Li X., Tong Y., Li Y.;
RT "Control of root meristem size by DA1-RELATED PROTEIN2 in Arabidopsis.";
RL Plant Physiol. 161:1542-1556(2013).
RN [7]
RP FUNCTION, INTERACTION WITH UBIQUITIN; TCP14 AND TCP15, DEVELOPMENTAL STAGE,
RP AND DOMAIN.
RX PubMed=25757472; DOI=10.1105/tpc.114.132274;
RA Peng Y., Chen L., Lu Y., Wu Y., Dumenil J., Zhu Z., Bevan M.W., Li Y.;
RT "The ubiquitin receptors DA1, DAR1, and DAR2 redundantly regulate
RT endoreduplication by modulating the stability of TCP14/15 in Arabidopsis.";
RL Plant Cell 27:649-662(2015).
RN [8]
RP UBIQUITINATION.
RX PubMed=28167503; DOI=10.1101/gad.292235.116;
RA Dong H., Dumenil J., Lu F.H., Na L., Vanhaeren H., Naumann C., Klecker M.,
RA Prior R., Smith C., McKenzie N., Saalbach G., Chen L., Xia T., Gonzalez N.,
RA Seguela M., Inze D., Dissmeyer N., Li Y., Bevan M.W.;
RT "Ubiquitylation activates a peptidase that promotes cleavage and
RT destabilization of its activating E3 ligases and diverse growth regulatory
RT proteins to limit cell proliferation in Arabidopsis.";
RL Genes Dev. 31:197-208(2017).
CC -!- FUNCTION: Acts redundantly with DA1 and DAR1 to regulate
CC endoreduplication during leaf development. Together with DA1 and DAR1,
CC modulates the protein stability of the transcription factors TCP14 and
CC TCP15, which repress endoreduplication by directly regulating the
CC expression of cell-cycle genes (PubMed:25757472). Involved in root
CC phloem development. Is an essential component of early phloem
CC development, long-distance delivery of phloem content, and proper
CC maintenance of root system architecture (PubMed:21749503). Involved in
CC the control of root meristem size. Functions genetically downstream of
CC cytokinin and IAA3 to maintain normal auxin distribution by influencing
CC polar auxin transport. Acts through the PLETHORA pathway, upstream of
CC PLT1 and PLT2 to influence root stem cell niche activity and thus
CC control root meristem size (PubMed:23296689).
CC {ECO:0000269|PubMed:21749503, ECO:0000269|PubMed:23296689,
CC ECO:0000269|PubMed:25757472}.
CC -!- SUBUNIT: Interacts with ubiquitin, TCP14 and TCP15.
CC {ECO:0000269|PubMed:25757472}.
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature of leaves,
CC inflorescence stems, flowers, hypocotyls, and primary and lateral
CC roots. In roots, expressed in phloem companion cells.
CC {ECO:0000269|PubMed:21749503}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during early stages leaf
CC development, and expression decreases at the later stages of leaf
CC development. {ECO:0000269|PubMed:25757472}.
CC -!- DOMAIN: The UIM domains bind molecules modified by monoubiquitin or
CC ubiquitin chains and promote coupled monoubiquitination.
CC {ECO:0000305|PubMed:25757472}.
CC -!- PTM: Polyubiquitinated by DA2. {ECO:0000269|PubMed:28167503}.
CC -!- DISRUPTION PHENOTYPE: Reduced primary root growth, increased lateral
CC root formation, and altered root system architecture, due to altered
CC early phloem development. {ECO:0000269|PubMed:21749503}.
CC -!- MISCELLANEOUS: Exogenous treatment with auxin rescues the phloem
CC defects of the lrd3 knockout mutant. {ECO:0000269|PubMed:21749503}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB87132.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003000; AAB87132.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09736.1; -; Genomic_DNA.
DR EMBL; AK227895; BAE99866.1; -; mRNA.
DR PIR; T01013; T01013.
DR RefSeq; NP_181513.3; NM_129542.5.
DR AlphaFoldDB; Q0WSN2; -.
DR BioGRID; 3908; 5.
DR IntAct; Q0WSN2; 2.
DR STRING; 3702.AT2G39830.1; -.
DR iPTMnet; Q0WSN2; -.
DR PaxDb; Q0WSN2; -.
DR PRIDE; Q0WSN2; -.
DR ProteomicsDB; 224676; -.
DR EnsemblPlants; AT2G39830.1; AT2G39830.1; AT2G39830.
DR GeneID; 818570; -.
DR Gramene; AT2G39830.1; AT2G39830.1; AT2G39830.
DR KEGG; ath:AT2G39830; -.
DR Araport; AT2G39830; -.
DR TAIR; locus:2063932; AT2G39830.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_015906_4_0_1; -.
DR InParanoid; Q0WSN2; -.
DR PhylomeDB; Q0WSN2; -.
DR PRO; PR:Q0WSN2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q0WSN2; baseline and differential.
DR Genevisible; Q0WSN2; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IDA:TAIR.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0010088; P:phloem development; IMP:TAIR.
DR GO; GO:0032875; P:regulation of DNA endoreduplication; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR InterPro; IPR045218; DA1-like.
DR InterPro; IPR022087; DA1-like_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24209; PTHR24209; 1.
DR Pfam; PF12315; DA1-like; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW LIM domain; Metal-binding; Reference proteome; Repeat; Ubl conjugation;
KW Zinc.
FT CHAIN 1..528
FT /note="Protein DA1-related 2"
FT /id="PRO_0000396937"
FT DOMAIN 99..118
FT /note="UIM 1"
FT /evidence="ECO:0000305"
FT DOMAIN 127..148
FT /note="UIM 2; degenerate"
FT /evidence="ECO:0000305"
FT DOMAIN 160..220
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 60..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 59426 MW; A17599D7815012D6 CRC64;
MDSSSSSSSS SPSSSYGVAR VSHISNPCIF GEVGSSSSST YRDKKWKLMK WVSKLFKSGS
NGGGSGAHTN HHPPQFQEDE NMVFPLPPSS LDDRSRGARD KEELDRSISL SLADNTKRPH
GYGWSMDNNR DFPRPFHGGL NPSSFIPPYE PSYQYRRRQR ICGGCNSDIG SGNYLGCMGT
FFHPECFRCH SCGYAITEHE FSLSGTKPYH KLCFKELTHP KCEVCHHFIP TNDAGLIEYR
CHPFWNQKYC PSHEYDKTAR CCSCERLESW DVRYYTLEDG RSLCLECMET AITDTGECQP
LYHAIRDYYE GMYMKLDQQI PMLLVQREAL NDAIVGEKNG YHHMPETRGL CLSEEQTVTS
VLRRPRLGAH RLVGMRTQPQ RLTRKCEVTA ILVLYGLPRL LTGAILAHEL MHGWLRLNGF
RNLNPEVEEG ICQVLSYMWL ESEVLSDPST RNLPSTSSVA TSSSSSFSNK KGGKSNVEKK
LGEFFKHQIA HDASPAYGGG FRAANAAACK YGLRRTLDHI RLTGTFPL
