DSE1_ARATH
ID DSE1_ARATH Reviewed; 386 AA.
AC Q3MV14; Q8GW99; Q9SZQ7;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein DECREASED SIZE EXCLUSION LIMIT 1 {ECO:0000303|PubMed:22411811};
DE Short=AtDSE1 {ECO:0000303|PubMed:22411811};
DE AltName: Full=Protein ALUMINUM TOLERANT 2 {ECO:0000303|PubMed:22345493};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2757 {ECO:0000303|PubMed:15266054};
DE AltName: Full=Protein TANMEI {ECO:0000303|PubMed:16113228};
GN Name=DSE1 {ECO:0000303|PubMed:22411811};
GN Synonyms=ALT2 {ECO:0000303|PubMed:22345493},
GN EMB2757 {ECO:0000303|PubMed:15266054}, TAN {ECO:0000303|PubMed:16113228};
GN OrderedLocusNames=At4g29860 {ECO:0000312|Araport:AT4G29860};
GN ORFNames=F27B13.100 {ECO:0000312|EMBL:CAB43661.1};
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:BAE44475.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=16113228; DOI=10.1104/pp.105.060467;
RA Yamagishi K., Nagata N., Yee K.M., Braybrook S.A., Pelletier J.,
RA Fujioka S., Yoshida S., Fischer R.L., Goldberg R.B., Harada J.J.;
RT "TANMEI/EMB2757 encodes a WD repeat protein required for embryo development
RT in Arabidopsis.";
RL Plant Physiol. 139:163-173(2005).
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=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 [5]
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-213 AND GLY-340, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22345493; DOI=10.1105/tpc.112.095596;
RA Nezames C.D., Sjogren C.A., Barajas J.F., Larsen P.B.;
RT "The Arabidopsis cell cycle checkpoint regulators TANMEI/ALT2 and ATR
RT mediate the active process of aluminum-dependent root growth inhibition.";
RL Plant Cell 24:608-621(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22411811; DOI=10.1073/pnas.1202919109;
RA Xu M., Cho E., Burch-Smith T.M., Zambryski P.C.;
RT "Plasmodesmata formation and cell-to-cell transport are reduced in
RT decreased size exclusion limit 1 during embryogenesis in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5098-5103(2012).
CC -!- FUNCTION: Involved in the formation of X-, Y-shaped and twinned
CC plasmodesmata (PD), thus modelating PD size exclusion limit and
CC regulating cell-to-cell transport (PubMed:22411811). Cell cycle
CC checkpoint regulator that monitors and responds to DNA damage such as
CC DNA cross-links, and triggers the halt of the cell cycle progression in
CC the presence of DNA cross-linking agents. Mediates the active process
CC of aluminum- (Al) dependent root growth inhibition and thus is required
CC for response to Al toxicity (PubMed:22345493). Required for both early
CC and late phases of embryo development as well as during seedling growth
CC (PubMed:16113228, PubMed:15266054). Essential for signal transduction
CC and development of both male and female organs (PubMed:22411811).
CC {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:16113228,
CC ECO:0000269|PubMed:22345493, ECO:0000269|PubMed:22411811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22345493,
CC ECO:0000269|PubMed:22411811}. Nucleus {ECO:0000269|PubMed:22345493,
CC ECO:0000269|PubMed:22411811}. Note=Translocates from the cytoplasm to
CC the nucleus in response to DNA damage mediated by treatment with
CC AlCl(3), mitomycin C (MMC), or cisplatin (CDDP).
CC {ECO:0000269|PubMed:22345493}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in floral buds, leaves,
CC stems, roots, and siliques, highest levels being in siliques that
CC contain developing seeds. {ECO:0000269|PubMed:16113228,
CC ECO:0000269|PubMed:22345493, ECO:0000269|PubMed:22411811}.
CC -!- DEVELOPMENTAL STAGE: Accumulates throughout the embryo and in endosperm
CC (PubMed:16113228). Expressed throughout the plant life cycle, from
CC embryogenesis to seed set. Accumulates in the shoot apex. In roots,
CC confined to the vascular system. In anthers, observed when the
CC filaments start to elongate, and remain expressed in later stages.
CC Constitutively expressed in gynoecia (PubMed:22411811).
CC {ECO:0000269|PubMed:16113228, ECO:0000269|PubMed:22411811}.
CC -!- DISRUPTION PHENOTYPE: Defects in both embryo and seedling development,
CC and pale yellow seeds. Die as embryos, probably because of intolerance
CC to desiccation and abnormal protein and lipid body accumulation in
CC mature seeds, but immature mutant seeds can be germinated in culture
CC and lead to short life seedlings defective in shoot and root
CC development, with reduced hypocotyls elongation in the dark
CC (PubMed:16113228, PubMed:15266054). Seedlings accumulate less
CC anthocyanin, are intolerant to desiccation, form trichomes on
CC cotyledons, and have reduced accumulation of storage proteins and
CC lipids (PubMed:16113228). Suppressor of the aluminum- (Al)
CC hypersensitive mutant als3-1 that fails to halt root growth after Al
CC exposure, does not accumulate CyclinB1;1 in the root tip, and fails to
CC force differentiation of the quiescent center and is thus highly
CC tolerant to high Al levels (PubMed:22345493). In dse1, reduced
CC plasmodesmata (PD) formation and cell-to-cell transport during
CC embryogenesis, due to reduced PD size exclusion limit. Dse1 embryos are
CC developmentally retarded and accumulate anthocyanin at the junction
CC between the cotyledons and hypocotyls, corresponding to the shoot
CC apical meristem (SAM). Reduced apical dominance leading to the
CC production of small abnormal flowers, often with altered organ numbers.
CC Infertility due in part to the abnormal development of stamen with
CC under-extended anther filaments that don't release pollen, and due in
CC part to abnormal ovules lacking pollen attractiveness
CC (PubMed:22411811). {ECO:0000269|PubMed:15266054,
CC ECO:0000269|PubMed:16113228, ECO:0000269|PubMed:22345493,
CC ECO:0000269|PubMed:22411811}.
CC -!- MISCELLANEOUS: 'Tanmei' means short life in Japanese.
CC {ECO:0000303|PubMed:16113228}.
CC -!- SIMILARITY: Belongs to the plant DSE1 protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43565.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC43565.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD44334.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD44334.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB43661.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79744.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB191306; BAE44475.1; -; mRNA.
DR EMBL; AL050352; CAB43661.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161575; CAB79744.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85686.1; -; Genomic_DNA.
DR EMBL; AK118989; BAC43565.1; ALT_SEQ; mRNA.
DR EMBL; AK176571; BAD44334.1; ALT_SEQ; mRNA.
DR PIR; T08547; T08547.
DR RefSeq; NP_194715.2; NM_119132.3.
DR AlphaFoldDB; Q3MV14; -.
DR SMR; Q3MV14; -.
DR STRING; 3702.AT4G29860.1; -.
DR iPTMnet; Q3MV14; -.
DR PaxDb; Q3MV14; -.
DR PRIDE; Q3MV14; -.
DR ProteomicsDB; 224280; -.
DR EnsemblPlants; AT4G29860.1; AT4G29860.1; AT4G29860.
DR GeneID; 829108; -.
DR Gramene; AT4G29860.1; AT4G29860.1; AT4G29860.
DR KEGG; ath:AT4G29860; -.
DR Araport; AT4G29860; -.
DR TAIR; locus:2123869; AT4G29860.
DR eggNOG; KOG0322; Eukaryota.
DR HOGENOM; CLU_041940_1_0_1; -.
DR InParanoid; Q3MV14; -.
DR OMA; NSLCFQE; -.
DR OrthoDB; 1543596at2759; -.
DR PhylomeDB; Q3MV14; -.
DR PRO; PR:Q3MV14; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q3MV14; baseline and differential.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048700; P:acquisition of desiccation tolerance in seed; IMP:TAIR.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0031570; P:DNA integrity checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0048481; P:plant ovule development; IMP:UniProtKB.
DR GO; GO:0009663; P:plasmodesma organization; IMP:UniProtKB.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0010044; P:response to aluminum ion; IMP:UniProtKB.
DR GO; GO:0072718; P:response to cisplatin; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Developmental protein; DNA damage; Nucleus;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..386
FT /note="Protein DECREASED SIZE EXCLUSION LIMIT 1"
FT /id="PRO_0000432850"
FT REPEAT 15..54
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 62..100
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 157..197
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 213..256
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 260..299
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 306..347
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 348..386
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT MUTAGEN 213
FT /note="G->E: In alt2-2; severely sensitive to DNA cross-
FT linking agents, enhanced tolerance to aluminum (Al), but
FT impaired halting root growth in response to Al toxicity."
FT /evidence="ECO:0000269|PubMed:22345493"
FT MUTAGEN 340
FT /note="G->R: In alt2-1; severely sensitive to the
FT intrastrand DNA cross-linking agent cisplatin (CDDP) and to
FT the DNA cross-linking agent mitomycin C (MMC), enhanced
FT tolerance to aluminum (Al), but impaired halting root
FT growth in response to Al toxicity. Fails to halt cell cycle
FT progression in the presence of DNA cross-linking agents."
FT /evidence="ECO:0000269|PubMed:22345493"
SQ SEQUENCE 386 AA; 41986 MW; 7C40E89F5D41536E CRC64;
MSKRPPPDPV AVLRGHRHSV MDVSFHPSKS LLFTGSADGE LRIWDTIQHR AVSSAWAHSR
ANGVLAVAAS PWLGEDKIIS QGRDGTVKCW DIEDGGLSRD PLLILETCAY HFCKFSLVKK
PKNSLQEAES HSRGCDEQDG GDTCNVQIAD DSERSEEDSG LLQDKDHAEG TTFVAVVGEQ
PTEVEIWDLN TGDKIIQLPQ SSPDESPNAS TKGRGMCMAV QLFCPPESQG FLHVLAGYED
GSILLWDIRN AKIPLTSVKF HSEPVLSLSV ASSCDGGISG GADDKIVMYN LNHSTGSCTI
RKEITLERPG VSGTSIRVDG KIAATAGWDH RIRVYNYRKG NALAILKYHR ATCNAVSYSP
DCELMASASE DATVALWKLY PPHKSL
