ELD1_ARATH
ID ELD1_ARATH Reviewed; 533 AA.
AC Q9C9Z9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Glycosyltransferase-like KOBITO 1 {ECO:0000303|PubMed:12215501, ECO:0000303|PubMed:22457425};
DE EC=2.4.1.- {ECO:0000305|PubMed:22457425};
DE AltName: Full=Protein ABA INSENSITIVE 8 {ECO:0000303|PubMed:14742875};
DE AltName: Full=Protein ELONGATION DEFECTIVE 1 {ECO:0000303|PubMed:10859181};
DE Flags: Precursor;
GN Name=ELD1 {ECO:0000303|PubMed:10859181};
GN Synonyms=ABI8 {ECO:0000303|PubMed:14742875},
GN KOB1 {ECO:0000303|PubMed:12215501};
GN OrderedLocusNames=At3g08550 {ECO:0000312|Araport:AT3G08550};
GN ORFNames=F17O14.2 {ECO:0000312|EMBL:AAG51348.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, TISSUE SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=15010620; DOI=10.1023/b:plan.0000019067.05185.d6;
RA Lertpiriyapong K., Sung Z.R.;
RT "The elongation defective1 mutant of Arabidopsis is impaired in the gene
RT encoding a serine-rich secreted protein.";
RL Plant Mol. Biol. 53:581-595(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=10859181; DOI=10.1104/pp.123.2.509;
RA Cheng J.C., Lertpiriyapong K., Wang S., Sung Z.R.;
RT "The role of the Arabidopsis ELD1 gene in cell development and
RT photomorphogenesis in darkness.";
RL Plant Physiol. 123:509-520(2000).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=12215501; DOI=10.1105/tpc.002873;
RA Pagant S., Bichet A., Sugimoto K., Lerouxel O., Desprez T., McCann M.,
RA Lerouge P., Vernhettes S., Hofte H.;
RT "KOBITO1 encodes a novel plasma membrane protein necessary for normal
RT synthesis of cellulose during cell expansion in Arabidopsis.";
RL Plant Cell 14:2001-2013(2002).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND GENE FAMILY.
RX PubMed=14742875; DOI=10.1105/tpc.018077;
RA Brocard-Gifford I., Lynch T.J., Garcia M.E., Malhotra B., Finkelstein R.R.;
RT "The Arabidopsis thaliana ABSCISIC ACID-INSENSITIVE8 encodes a novel
RT protein mediating abscisic acid and sugar responses essential for growth.";
RL Plant Cell 16:406-421(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-371.
RX PubMed=22457425; DOI=10.1104/pp.112.194563;
RA Kong D., Karve R., Willet A., Chen M.K., Oden J., Shpak E.D.;
RT "Regulation of plasmodesmatal permeability and stomatal patterning by the
RT glycosyltransferase-like protein KOBITO1.";
RL Plant Physiol. 159:156-168(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, REGULATION BY LIGHT, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=24995569; DOI=10.1111/pce.12395;
RA Wang X., Jing Y., Zhang B., Zhou Y., Lin R.;
RT "Glycosyltransferase-like protein ABI8/ELD1/KOB1 promotes Arabidopsis
RT hypocotyl elongation through regulating cellulose biosynthesis.";
RL Plant Cell Environ. 38:411-422(2015).
CC -!- FUNCTION: Involved in the coordination between cell elongation and
CC cellulose synthesis by promoting the expression of genes involved in
CC cell elongation and cellulose synthesis (PubMed:15010620,
CC PubMed:10859181, PubMed:12215501, PubMed:24995569). Acts as a regulator
CC of plasmodesmatal permeability (PubMed:22457425). Mediates abscisic
CC acid (ABA) and sugar responses essential for growth (e.g. seed
CC germination, stomatal regulation and ABA-regulated gene expression)
CC (PubMed:14742875). Required for normal organogenesis by promoting cell
CC elongation, regulating cell differentiation in vascular tissues and
CC maintaining root meristem identity (PubMed:15010620, PubMed:10859181).
CC Regulates crystalline cellulose microfibrils deposition and parallel
CC organization during the elongation phase of the cell (PubMed:12215501).
CC Maybe a glycosyltransferase (PubMed:22457425). Negative factor in light
CC inhibition of hypocotyl elongation through modulating cellulose
CC biosynthesis (PubMed:24995569). {ECO:0000269|PubMed:10859181,
CC ECO:0000269|PubMed:12215501, ECO:0000269|PubMed:14742875,
CC ECO:0000269|PubMed:15010620, ECO:0000269|PubMed:22457425,
CC ECO:0000269|PubMed:24995569}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:15010620}. Cytoplasm {ECO:0000269|PubMed:14742875}.
CC Cell membrane {ECO:0000269|PubMed:12215501}. Note=The cell membrane
CC subcellular localization first observed (PubMed:12215501) and the
CC punctate pattern within the cytoplasm (PubMed:14742875) could not be
CC confirmed (PubMed:15010620).
CC -!- TISSUE SPECIFICITY: Expressed at low levels in both light- and dark-
CC grown plants (PubMed:15010620, PubMed:12215501, PubMed:14742875).
CC Accumulates especially in the elongation zone of roots (at protein
CC level) (PubMed:14742875). Expressed in the roots regardless of the
CC light treatment, high levels in the uppermost regions of hypocotyls in
CC darkness, but low levels in light-grown hypocotyls (PubMed:24995569).
CC {ECO:0000269|PubMed:12215501, ECO:0000269|PubMed:14742875,
CC ECO:0000269|PubMed:15010620, ECO:0000269|PubMed:24995569}.
CC -!- INDUCTION: Down-regulated by light in a phytochrome A-dependent manner,
CC via protein destabilization and subsequent degradation by the 26S
CC proteasome (at protein level). Reduced transcription in light
CC conditions in a HY5-dependent manner. {ECO:0000269|PubMed:24995569}.
CC -!- DISRUPTION PHENOTYPE: Increased plasmodesmatal permeability leading to
CC an increase in intercellular protein trafficking (PubMed:22457425).
CC Growth-defective due to cellulose deficiency, impaired cell elongation
CC and altered cell division in root meristems, thus leading to stunted
CC plants (PubMed:15010620, PubMed:10859181, PubMed:12215501). When light-
CC grown, dwarf, with very short root and lateral organs (e.g. leaves)
CC extremely reduced in size, as well as abnormal vascular tissues,
CC characterized by twisted vascular bundle and the presence of
CC undifferentiated vascular cells (PubMed:15010620, PubMed:24995569).
CC Accumulation of ectopic lignin, especially in the mature part of the
CC root, of ectopic callose accumulation in hypocotyls, and of ectopic
CC suberin around the vascular bundles in roots and hypocotyls
CC (PubMed:15010620, PubMed:10859181, PubMed:12215501). Photomorphogenesis
CC in the dark, absence of etiolated phenotype, with extremely short
CC hypocotyls, shoot development, and inflorescences and flowers
CC production (PubMed:15010620, PubMed:24995569). Inability to grow in
CC soil (PubMed:15010620, PubMed:14742875). The cell wall is constituted
CC by abnormally randomized microfibrils occluded by a layer of pectins
CC probably due to a defect in the synthesis of crystalline cellulose
CC during the elongation phase of the cell (PubMed:15010620,
CC PubMed:24995569). Abscisic acid- (ABA-) resistant germination
CC associated with defective stomatal regulation, altered ABA-responsive
CC gene expression, delayed flowering, and male sterility
CC (PubMed:14742875). Glucose- (Glc-) dependent growth with impaired Glc
CC sensitivity that normaly induces seedling developmental arrest; Glc
CC reverses partially disruption phenotypes (PubMed:14742875).
CC {ECO:0000269|PubMed:10859181, ECO:0000269|PubMed:12215501,
CC ECO:0000269|PubMed:14742875, ECO:0000269|PubMed:15010620,
CC ECO:0000269|PubMed:22457425, ECO:0000269|PubMed:24995569}.
CC -!- MISCELLANEOUS: 'Kobito' means 'dwarf' in Japanese.
CC {ECO:0000303|PubMed:12215501}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 92 family.
CC {ECO:0000305|PubMed:22457425}.
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DR EMBL; AF543710; AAN33186.1; -; mRNA.
DR EMBL; AC012562; AAG51348.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74645.1; -; Genomic_DNA.
DR RefSeq; NP_187467.1; NM_111689.5.
DR AlphaFoldDB; Q9C9Z9; -.
DR STRING; 3702.AT3G08550.1; -.
DR iPTMnet; Q9C9Z9; -.
DR PaxDb; Q9C9Z9; -.
DR PRIDE; Q9C9Z9; -.
DR ProteomicsDB; 220658; -.
DR EnsemblPlants; AT3G08550.1; AT3G08550.1; AT3G08550.
DR GeneID; 820002; -.
DR Gramene; AT3G08550.1; AT3G08550.1; AT3G08550.
DR KEGG; ath:AT3G08550; -.
DR Araport; AT3G08550; -.
DR TAIR; locus:2077858; AT3G08550.
DR eggNOG; ENOG502QPZC; Eukaryota.
DR HOGENOM; CLU_032860_0_0_1; -.
DR InParanoid; Q9C9Z9; -.
DR OMA; RDARMEW; -.
DR OrthoDB; 431242at2759; -.
DR PhylomeDB; Q9C9Z9; -.
DR PRO; PR:Q9C9Z9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C9Z9; baseline and differential.
DR Genevisible; Q9C9Z9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IMP:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071482; P:cellular response to light stimulus; IEP:UniProtKB.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0010215; P:cellulose microfibril organization; IMP:UniProtKB.
DR GO; GO:0060560; P:developmental growth involved in morphogenesis; IMP:UniProtKB.
DR GO; GO:0010078; P:maintenance of root meristem identity; IMP:UniProtKB.
DR GO; GO:0009831; P:plant-type cell wall modification involved in multidimensional cell growth; IMP:TAIR.
DR GO; GO:0009663; P:plasmodesma organization; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:2001009; P:regulation of plant-type cell wall cellulose biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR InterPro; IPR008166; Glyco_transf_92.
DR InterPro; IPR044224; KOBITO1-like.
DR PANTHER; PTHR46701; PTHR46701; 1.
DR Pfam; PF01697; Glyco_transf_92; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Cell cycle; Cell division; Cell membrane;
KW Cell wall; Cell wall biogenesis/degradation; Cytoplasm;
KW Developmental protein; Differentiation; Glycoprotein; Glycosyltransferase;
KW Growth regulation; Membrane; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..533
FT /note="Glycosyltransferase-like KOBITO 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430755"
FT DOMAIN 137..377
FT /note="GT92"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 371
FT /note="S->L: In kob1-3; increased plasmodesmatal
FT permeability, dwarf plants and stomata clusters in the
FT erl1-2 erl2-1 background."
FT /evidence="ECO:0000269|PubMed:22457425"
SQ SEQUENCE 533 AA; 59889 MW; 06C33FE658F68764 CRC64;
MKSTHHHRAP LISASSSSSS SSQNHSFVSR LLLLLTLLPV SLACLAFILQ WRGGGLADPA
SASVRSSTSV PGGSDLNHEV FPGMETVSSV SPKSHQSSSD CSNLARSSSP SFPYYADWKF
GVDTSLKPKI CITTSTSAGL DQILPWMFYH KVLGVSTFFL FVEGKAATPS ISKVLESIPG
VKVIYRTKEL EEKQAKSRIW NETWLSSFFY KPCNYELFVK QSLNMEMAIV MARDAGMDWI
LHLDTDELIY PAGAREYSLR RLLLDVPPNV DMVIFPNYES SVERDDIKDP FTEVSMFKKN
YDHLPKDTYF GMYKEATRNN PNYFLTYGNG KSVARVQDHL RPNGAHRWHN YMKTPNEIKL
EEAAVLHYTY SKFSDLTSRR DRCGCKPTKE DVKRCFMLDF DRSAFIIAST ATDEEMLSWY
REHVVWGDKD VKTKLLRKGI LTRIYSPMVV IQALKESGVF SSVVSSASTN LSKKKFLSSI
HKSNSSRSTA SESLPSKESK SEGISARHLL EAESAIPPLS PPGMEQARFF TED
