EDE1_ARATH
ID EDE1_ARATH Reviewed; 474 AA.
AC O80588;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Protein ENDOSPERM DEFECTIVE 1;
DE AltName: Full=Protein EMBRYO DEFECTIVE 3116;
DE AltName: Full=QWRF motif-containing protein 5;
GN Name=EDE1; Synonyms=EMB3116, QWRF5; OrderedLocusNames=At2g44190;
GN ORFNames=F6E13.32;
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].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, MUTAGENESIS OF 304-ARG--GLN-321, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19151224; DOI=10.1105/tpc.108.061812;
RA Pignocchi C., Minns G.E., Nesi N., Koumproglou R., Kitsios G., Benning C.,
RA Lloyd C.W., Doonan J.H., Hills M.J.;
RT "ENDOSPERM DEFECTIVE1 is a novel microtubule-associated protein essential
RT for seed development in Arabidopsis.";
RL Plant Cell 21:90-105(2009).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=20978221; DOI=10.1105/tpc.110.074781;
RA Albrecht V., Simkova K., Carrie C., Delannoy E., Giraud E., Whelan J.,
RA Small I.D., Apel K., Badger M.R., Pogson B.J.;
RT "The cytoskeleton and the peroxisomal-targeted snowy cotyledon3 protein are
RT required for chloroplast development in Arabidopsis.";
RL Plant Cell 22:3423-3438(2010).
RN [6]
RP INTERACTION WITH GRF5, AND PHOSPHORYLATION.
RX PubMed=21558460; DOI=10.1093/aob/mcr050;
RA Pignocchi C., Doonan J.H.;
RT "Interaction of a 14-3-3 protein with the plant microtubule-associated
RT protein EDE1.";
RL Ann. Bot. 107:1103-1109(2011).
RN [7]
RP FUNCTION.
RX PubMed=22535409; DOI=10.1242/dev.077057;
RA Hehenberger E., Kradolfer D., Koehler C.;
RT "Endosperm cellularization defines an important developmental transition
RT for embryo development.";
RL Development 139:2031-2039(2012).
CC -!- FUNCTION: Microtubule-associated protein required for seed development
CC and for microtubule function in the endosperm. Associates with nuclear
CC microtubules during mitosis. Binds to microtubules of the spindle and
CC spindle-poles and to midzone microtubules out of which the phragmoplast
CC emerges. Not associated with cortical microtubules. Required for
CC endosperm cellularization. May be bound and sequestered by GRF5 in an
CC inactive soluble form during the early stages of mitosis.
CC {ECO:0000269|PubMed:19151224, ECO:0000269|PubMed:22535409}.
CC -!- SUBUNIT: Interacts with GRF5 in a phosphorylation-independent manner.
CC The binding to microtubules occurs independently of the interaction
CC with GRF5. {ECO:0000269|PubMed:21558460}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19151224}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19151224}.
CC Note=Microtubule-associated.
CC -!- TISSUE SPECIFICITY: Highly expressed in young siliques, seedlings,
CC flower buds and open flowers. Weak expression in roots, and not
CC detected in older siliques and mature leaves. Expressed in the embryo
CC sac in prefertilization ovules and in seeds following fertilization.
CC Detected in both embryo up to the heart stage and endosperm throughout
CC most of the syncytial phase of endosperm development. Not detected in
CC the cellularized endosperm, when cell division has ceased.
CC {ECO:0000269|PubMed:19151224}.
CC -!- INDUCTION: Cell cycle-dependent regulation. Up-regulated during the
CC G2/M phase. {ECO:0000269|PubMed:19151224}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:21558460}.
CC -!- DISRUPTION PHENOTYPE: Aborted seed development.
CC {ECO:0000269|PubMed:19151224}.
CC -!- SIMILARITY: Belongs to the QWRF family. {ECO:0000305}.
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DR EMBL; AC004005; AAC23423.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10387.1; -; Genomic_DNA.
DR EMBL; BT022041; AAY25453.1; -; mRNA.
DR PIR; T00699; T00699.
DR RefSeq; NP_181947.1; NM_129982.3.
DR AlphaFoldDB; O80588; -.
DR BioGRID; 4362; 4.
DR STRING; 3702.AT2G44190.1; -.
DR MEROPS; M41.018; -.
DR iPTMnet; O80588; -.
DR PaxDb; O80588; -.
DR PRIDE; O80588; -.
DR ProteomicsDB; 222059; -.
DR EnsemblPlants; AT2G44190.1; AT2G44190.1; AT2G44190.
DR GeneID; 819026; -.
DR Gramene; AT2G44190.1; AT2G44190.1; AT2G44190.
DR KEGG; ath:AT2G44190; -.
DR Araport; AT2G44190; -.
DR TAIR; locus:2051869; AT2G44190.
DR eggNOG; ENOG502R98H; Eukaryota.
DR HOGENOM; CLU_015955_0_0_1; -.
DR InParanoid; O80588; -.
DR OMA; LQMREYS; -.
DR OrthoDB; 1288185at2759; -.
DR PhylomeDB; O80588; -.
DR PRO; PR:O80588; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80588; baseline and differential.
DR Genevisible; O80588; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005880; C:nuclear microtubule; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0010342; P:endosperm cellularization; IMP:TAIR.
DR GO; GO:0009960; P:endosperm development; IMP:TAIR.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR InterPro; IPR007573; QWRF.
DR Pfam; PF04484; QWRF; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..474
FT /note="Protein ENDOSPERM DEFECTIVE 1"
FT /id="PRO_0000423622"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 283..286
FT /note="QWRF motif"
FT COMPBIAS 39..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine; by CDC2"
FT /evidence="ECO:0000255"
FT MUTAGEN 304..321
FT /note="Missing: In ede1-1; endosperm containing a few
FT enlarged nuclei lacking associated microtubule structures."
FT /evidence="ECO:0000269|PubMed:19151224"
SQ SEQUENCE 474 AA; 52593 MW; 3896704CDC65D3B5 CRC64;
MEARIGRSME HPSTPAINAP APVPPPSTRR PRVREVSSRF MSPISSSSSS SSSSSAGDLH
QLTSNSPRHH HQHQNQRSTS AQRMRRQLKM QEGDENRPSE TARSLDSPFP LQQVDGGKNP
KQHIRSKPLK ENGHRLDTPT TAMLPPPSRS RLNQQRLLTA SAATRLLRSS GISLSSSTDG
EEDNNNREIF KSNGPDLLPT IRTQAKAFNT PTASPLSRSL SSDDASMFRD VRASLSLKNG
VGLSLPPVAP NSKIQADTKK QKKALGQQAD VHSLKLLHNR YLQWRFANAN AEVKTQSQKA
QAERMFYSLG LKMSELSDSV QRKRIELQHL QRVKAVTEIV ESQTPSLEQW AVLEDEFSTS
LLETTEALLN ASLRLPLDSK IKVETKELAE ALVVASKSME GIVQNIGNLV PKTQEMETLM
SELARVSGIE KASVEDCRVA LLKTHSSQME ECYLRSQLIQ HQKKCHQQEC TTSV
