DAR1_ARATH
ID DAR1_ARATH Reviewed; 553 AA.
AC Q8W4F0; O23197;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein DA1-related 1 {ECO:0000303|PubMed:18483219};
GN Name=DAR1 {ECO:0000303|PubMed:18483219}; OrderedLocusNames=At4g36860;
GN ORFNames=AP22.33, C7A10.500;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 DISRUPTION PHENOTYPE, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
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 DAR2 to regulate
CC endoreduplication during leaf development. Together with DA1 and DAR2,
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. {ECO:0000269|PubMed:25757472}.
CC -!- SUBUNIT: Interacts with ubiquitin, TCP14 and TCP15.
CC {ECO:0000269|PubMed:25757472}.
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: No visible phenotype.
CC {ECO:0000269|PubMed:18483219}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB16816.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB16816.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB80352.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80352.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z99708; CAB16816.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161590; CAB80352.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86710.1; -; Genomic_DNA.
DR EMBL; AY062599; AAL32677.1; -; mRNA.
DR EMBL; AY114659; AAM47978.1; -; mRNA.
DR PIR; C85435; C85435.
DR RefSeq; NP_195404.6; NM_119850.7.
DR AlphaFoldDB; Q8W4F0; -.
DR BioGRID; 15120; 7.
DR IntAct; Q8W4F0; 5.
DR STRING; 3702.AT4G36860.1; -.
DR iPTMnet; Q8W4F0; -.
DR PaxDb; Q8W4F0; -.
DR PRIDE; Q8W4F0; -.
DR EnsemblPlants; AT4G36860.1; AT4G36860.1; AT4G36860.
DR GeneID; 829839; -.
DR Gramene; AT4G36860.1; AT4G36860.1; AT4G36860.
DR KEGG; ath:AT4G36860; -.
DR Araport; AT4G36860; -.
DR TAIR; locus:2115290; AT4G36860.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_015906_4_0_1; -.
DR InParanoid; Q8W4F0; -.
DR OMA; HIRITGS; -.
DR PRO; PR:Q8W4F0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W4F0; baseline and differential.
DR Genevisible; Q8W4F0; 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; IDA:TAIR.
DR GO; GO:0032875; P:regulation of DNA endoreduplication; IMP:UniProtKB.
DR InterPro; IPR045218; DA1-like.
DR InterPro; IPR022087; DA1-like_dom.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24209; PTHR24209; 2.
DR Pfam; PF12315; DA1-like; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00726; UIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50330; UIM; 3.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; Zinc.
FT CHAIN 1..553
FT /note="Protein DA1-related 1"
FT /id="PRO_0000396936"
FT DOMAIN 42..61
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 87..106
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 122..141
FT /note="UIM 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 149..168
FT /note="UIM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 188..248
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 10..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT CONFLICT 505
FT /note="K -> E (in Ref. 4; AAL32677/AAM47978)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 63308 MW; 10A724F4867A1AB2 CRC64;
MGWLTKILKG SSHKFSDGQC NGRYREDRNL EGPRYSAEGS DFDKEEIECA IALSLSEQEH
VIPQDDKGKK IIEYKSETEE DDDDDEDEDE EYMRAQLEAA EEEERRVAQA QIEEEEKRRA
EAQLEETEKL LAKARLEEEE MRRSKAQLEE DELLAKALQE SMNVGSPPRY DPGNILQPYP
FLIPSSHRIC VGCQAEIGHG RFLSCMGGVW HPECFCCNAC DKPIIDYEFS MSGNRPYHKL
CYKEQHHPKC DVCHNFIPTN PAGLIEYRAH PFWMQKYCPS HERDGTPRCC SCERMEPKDT
KYLILDDGRK LCLECLDSAI MDTHECQPLY LEIREFYEGL HMKVEQQIPM LLVERSALNE
AMEGEKHGHH HLPETRGLCL SEEQTVTTVL RRPRIGAGYK LIDMITEPCR LIRRCEVTAI
LILYGLPRLL TGSILAHEMM HAWLRLNGYP NLRPEVEEGI CQVLAHMWLE SETYAGSTLV
DIASSSSSAV VSASSKKGER SDFEKKLGEF FKHQIESDSS SAYGDGFRQG NQAVLKHGLR
RTLDHIRLTG TFP
