DRP1E_ARATH
ID DRP1E_ARATH Reviewed; 624 AA.
AC Q9FNX5; Q9M1C4; Q9SE82;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Phragmoplastin DRP1E {ECO:0000305};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P42697};
DE AltName: Full=Dynamin-like protein 1E {ECO:0000303|PubMed:11351070, ECO:0000303|PubMed:12834397, ECO:0000303|PubMed:14750516};
DE AltName: Full=Dynamin-like protein 4 {ECO:0000303|PubMed:12671086, ECO:0000303|PubMed:14750516};
DE AltName: Full=Dynamin-like protein DLP2 {ECO:0000303|PubMed:14750516};
DE AltName: Full=Dynamin-related protein 1E {ECO:0000303|PubMed:14750516, ECO:0000303|PubMed:14750520};
DE Short=AtDRP1E {ECO:0000303|PubMed:14750516, ECO:0000303|PubMed:14750520};
GN Name=DRP1E {ECO:0000303|PubMed:14750516, ECO:0000303|PubMed:14750520};
GN Synonyms=ADL1E {ECO:0000303|PubMed:11351070, ECO:0000303|PubMed:12834397,
GN ECO:0000303|PubMed:14750516}, ADL4 {ECO:0000303|PubMed:12671086,
GN ECO:0000303|PubMed:14750516}, DLP2 {ECO:0000303|PubMed:14750516};
GN OrderedLocusNames=At3g60190 {ECO:0000312|Araport:AT3G60190};
GN ORFNames=T2O9.170 {ECO:0000312|EMBL:CAB75934.1};
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].
RX PubMed=11351070; DOI=10.1104/pp.126.1.47;
RA Kang B.-H., Busse J.S., Dickey C., Rancour D.M., Bednarek S.Y.;
RT "The Arabidopsis cell plate-associated dynamin-like protein, ADL1Ap, is
RT required for multiple stages of plant growth and development.";
RL Plant Physiol. 126:47-68(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kang Y.N., Kim S.H., Hwang I.;
RT "Presence of multiple isoforms of dynamin-like proteins in Arabidopsis and
RT their differential expression.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Jasper F., Menzel D.;
RT "Identification of a subgroup of closely related dynamin-like proteins in
RT Arabidopsis thaliana.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12671086; DOI=10.1105/tpc.009670;
RA Kang B.-H., Busse J.S., Bednarek S.Y.;
RT "Members of the Arabidopsis dynamin-like gene family, ADL1, are essential
RT for plant cytokinesis and polarized cell growth.";
RL Plant Cell 15:899-913(2003).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=12834397; DOI=10.1046/j.1365-313x.2003.01775.x;
RA Kang B.-H., Rancour D.M., Bednarek S.Y.;
RT "The dynamin-like protein ADL1C is essential for plasma membrane
RT maintenance during pollen maturation.";
RL Plant J. 35:1-15(2003).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14750516; DOI=10.1023/b:plan.0000007000.29697.81;
RA Hong Z., Bednarek S.Y., Blumwald E., Hwang I., Jurgens G., Menzel D.,
RA Osteryoung K.W., Raikhel N.V., Shinozaki K., Tsutsumi N., Verma D.P.S.;
RT "A unified nomenclature for Arabidopsis dynamin-related large GTPases based
RT on homology and possible functions.";
RL Plant Mol. Biol. 53:261-265(2003).
RN [10]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=14750520; DOI=10.1023/b:plan.0000006936.50532.3a;
RA Hong Z., Geisler-Lee C.J., Zhang Z., Verma D.P.S.;
RT "Phragmoplastin dynamics: multiple forms, microtubule association and their
RT roles in cell plate formation in plants.";
RL Plant Mol. Biol. 53:297-312(2003).
RN [11]
RP INTERACTION WITH PHIP1.
RX PubMed=18621982; DOI=10.1104/pp.108.120527;
RA Ma L., Xie B., Hong Z., Verma D.P.S., Zhang Z.;
RT "A novel RNA-binding protein associated with cell plate formation.";
RL Plant Physiol. 148:223-234(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Microtubule-associated force-producing protein that is
CC targeted to the tubulo-vesicular network of the forming cell plate
CC during cytokinesis. Also plays a major role in plasma membrane
CC maintenance and cell wall integrity with an implication in vesicular
CC trafficking, polar cell expansion, and other aspects of plant growth
CC and development. Has a GTPase activity (By similarity).
CC {ECO:0000250|UniProtKB:P42697, ECO:0000269|PubMed:12671086,
CC ECO:0000269|PubMed:14750520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P42697};
CC -!- SUBUNIT: Forms homodimer and may homooligomerize and heterooligomerize
CC to form the phragmoplastin complex (PubMed:14750520). Binds to PHIP1
CC (PubMed:18621982). {ECO:0000269|PubMed:14750520,
CC ECO:0000269|PubMed:18621982}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm,
CC cytoskeleton, phragmoplast. Note=Microtubule-associated and localized
CC in the forming cell plate during cytokinesis.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12834397}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF22292.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL88715.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB75934.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF488725; AAL88715.1; ALT_INIT; mRNA.
DR EMBL; AF180733; AAF22292.1; ALT_FRAME; mRNA.
DR EMBL; AJ304842; CAC19657.1; -; mRNA.
DR EMBL; AL138658; CAB75934.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE80022.1; -; Genomic_DNA.
DR EMBL; AF428332; AAL16262.1; -; mRNA.
DR PIR; T47843; T47843.
DR RefSeq; NP_567094.1; NM_115882.4.
DR AlphaFoldDB; Q9FNX5; -.
DR SMR; Q9FNX5; -.
DR BioGRID; 10503; 5.
DR IntAct; Q9FNX5; 3.
DR STRING; 3702.AT3G60190.1; -.
DR iPTMnet; Q9FNX5; -.
DR PaxDb; Q9FNX5; -.
DR PRIDE; Q9FNX5; -.
DR ProteomicsDB; 224363; -.
DR EnsemblPlants; AT3G60190.1; AT3G60190.1; AT3G60190.
DR GeneID; 825189; -.
DR Gramene; AT3G60190.1; AT3G60190.1; AT3G60190.
DR KEGG; ath:AT3G60190; -.
DR Araport; AT3G60190; -.
DR TAIR; locus:2101482; AT3G60190.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_3_1; -.
DR InParanoid; Q9FNX5; -.
DR OMA; VEKPNCV; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; Q9FNX5; -.
DR PRO; PR:Q9FNX5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FNX5; baseline and differential.
DR Genevisible; Q9FNX5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:TAIR.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW GTP-binding; Hydrolase; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..624
FT /note="Phragmoplastin DRP1E"
FT /id="PRO_0000206581"
FT DOMAIN 37..306
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 532..624
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 47..54
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 73..75
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 148..151
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 217..220
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 247..250
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 50..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT BINDING 218..223
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT BINDING 248..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 404..405
FT /note="PH -> LT (in Ref. 2; AAF22292)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="P -> L (in Ref. 2; AAF22292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 69804 MW; A4D33A8B114BCE62 CRC64;
MTTMESLIGL VNRIQRACTV LGDYGGGTGS NAFNSLWEAL PTVAVVGGQS SGKSSVLESI
VGRDFLPRGS GIVTRRPLVL QLHKTDDGTE EYAEFLHLPK KQFTDFALVR REIQDETDRI
TGKNKQISPV PIHLSIYSPN VVNLTLIDLP GLTKVAVEGQ PETIAEDIES MVRTYVDKPN
CIILAISPAN QDIATSDAIK LAKDVDPTGE RTFGVLTKLD LMDKGTNALE VLEGRSYRLQ
HPWVGIVNRS QADINKNVDM MLARRKEREY FDTSPDYGHL ASKMGSEYLA KLLSKHLESV
IRTRIPSILS LINKSIEELE RELDRMGRPV AVDAGAQLYT ILEMCRAFDK IFKEHLDGGR
PGGDRIYGVF DNQLPAALKK LPFDRHLSLQ SVKKIVSEAD GYQPHLIAPE QGYRRLIEGA
LGYFRGPAEA SVDAVHYVLK ELVRKSISET EELKRFPSLQ VELAAAANSS LEKFREESKK
SVIRLVDMES AYLTAEFFRK LPQEIERPVT NSKNQTASPS SATLDQYGDG HFRRIASNVS
AYVNMVSDTL RNTIPKACVY CQVRQAKLAL LNYFYSQISK REGKQLGQLL DEDPALMDRR
LECAKRLELY KKARDEIDAV AWVR
