DRP1A_ARATH
ID DRP1A_ARATH Reviewed; 610 AA.
AC P42697; Q0WLG2; Q1EBU0; Q39118; Q8L9V5; Q8LPS7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Phragmoplastin DRP1A {ECO:0000305};
DE EC=3.6.5.- {ECO:0000269|PubMed:20171176};
DE AltName: Full=Dynamin-like protein 1 {ECO:0000303|PubMed:9342876};
DE AltName: Full=Dynamin-like protein 1A {ECO:0000303|PubMed:11351070, ECO:0000303|PubMed:12671086, ECO:0000303|PubMed:12834397, ECO:0000303|PubMed:18642946};
DE AltName: Full=Dynamin-related protein 1A {ECO:0000303|PubMed:14750516, ECO:0000303|PubMed:14750520, ECO:0000303|PubMed:15923323, ECO:0000303|PubMed:22107825};
DE Short=AtDRP1A {ECO:0000303|PubMed:14750516, ECO:0000303|PubMed:14750520, ECO:0000303|PubMed:15923323, ECO:0000303|PubMed:22107825};
DE AltName: Full=Protein RADIAL SWELLING 9 {ECO:0000303|PubMed:18256049};
GN Name=DRP1A {ECO:0000303|PubMed:14750516, ECO:0000303|PubMed:14750520,
GN ECO:0000303|PubMed:15923323, ECO:0000303|PubMed:22107825};
GN Synonyms=ADL1 {ECO:0000303|PubMed:9342876},
GN ADL1A {ECO:0000303|PubMed:11351070, ECO:0000303|PubMed:12671086,
GN ECO:0000303|PubMed:12834397, ECO:0000303|PubMed:18642946},
GN AG68 {ECO:0000303|PubMed:7548829}, RSW9 {ECO:0000303|PubMed:18256049};
GN OrderedLocusNames=At5g42080 {ECO:0000312|Araport:AT5G42080};
GN ORFNames=MJC20.19 {ECO:0000312|EMBL:BAB08441.1};
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7548829; DOI=10.1007/bf00032672;
RA Dombrowski J.E., Raikhel N.V.;
RT "Isolation of a cDNA encoding a novel GTP-binding protein of Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 28:1121-1126(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=9342876; DOI=10.1104/pp.115.2.763;
RA Park J.M., Kang S.G., Pih K.T., Jang H.J., Piao H.L., Yoon H.W., Cho M.J.,
RA Hwang I.;
RT "A dynamin-like protein, ADL1, is present in membranes as a high-molecular-
RT mass complex in Arabidopsis thaliana.";
RL Plant Physiol. 115:763-771(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-610 (ISOFORM 1).
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION.
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AGD3, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15923323; DOI=10.1104/pp.105.061689;
RA Sawa S., Koizumi K., Naramoto S., Demura T., Ueda T., Nakano A., Fukuda H.;
RT "DRP1A is responsible for vascular continuity synergistically working with
RT VAN3 in Arabidopsis.";
RL Plant Physiol. 138:819-826(2005).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=15815986; DOI=10.1002/pmic.200401062;
RA Giavalisco P., Nordhoff E., Kreitler T., Kloeppel K.-D., Lehrach H.,
RA Klose J., Gobom J.;
RT "Proteome analysis of Arabidopsis thaliana by two-dimensional gel
RT electrophoresis and matrix-assisted laser desorption/ionisation-time of
RT flight mass spectrometry.";
RL Proteomics 5:1902-1913(2005).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18256049; DOI=10.1093/jxb/erm324;
RA Collings D.A., Gebbie L.K., Howles P.A., Hurley U.A., Birch R.J.,
RA Cork A.H., Hocart C.H., Arioli T., Williamson R.E.;
RT "Arabidopsis dynamin-like protein DRP1A: a null mutant with widespread
RT defects in endocytosis, cellulose synthesis, cytokinesis, and cell
RT expansion.";
RL J. Exp. Bot. 59:361-376(2008).
RN [17]
RP INTERACTION WITH AHK2.
RX PubMed=18642946; DOI=10.1021/pr0703831;
RA Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT "Toward an interaction map of the two-component signaling pathway of
RT Arabidopsis thaliana.";
RL J. Proteome Res. 7:3649-3660(2008).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18612642; DOI=10.1007/s00299-008-0583-0;
RA Fujimoto M., Arimura S., Nakazono M., Tsutsumi N.;
RT "Arabidopsis dynamin-related protein DRP2B is co-localized with DRP1A on
RT the leading edge of the forming cell plate.";
RL Plant Cell Rep. 27:1581-1586(2008).
RN [19]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=18344418; DOI=10.1104/pp.108.116863;
RA Konopka C.A., Bednarek S.Y.;
RT "Comparison of the dynamics and functional redundancy of the Arabidopsis
RT dynamin-related isoforms DRP1A and DRP1C during plant development.";
RL Plant Physiol. 147:1590-1602(2008).
RN [20]
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 [21]
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20171176; DOI=10.1016/j.bbrc.2010.02.070;
RA Backues S.K., Bednarek S.Y.;
RT "Arabidopsis dynamin-related protein 1A polymers bind, but do not tubulate,
RT liposomes.";
RL Biochem. Biophys. Res. Commun. 393:734-739(2010).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DRP2B, AND HOMODIMER.
RC STRAIN=cv. Columbia;
RX PubMed=20231465; DOI=10.1073/pnas.0913562107;
RA Fujimoto M., Arimura S., Ueda T., Takanashi H., Hayashi Y., Nakano A.,
RA Tsutsumi N.;
RT "Arabidopsis dynamin-related proteins DRP2B and DRP1A participate together
RT in clathrin-coated vesicle formation during endocytosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6094-6099(2010).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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).
RN [24]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=25234576; DOI=10.1111/tpj.12674;
RA Frescatada-Rosa M., Stanislas T., Backues S.K., Reichardt I., Men S.,
RA Boutte Y., Juergens G., Moritz T., Bednarek S.Y., Grebe M.;
RT "High lipid order of Arabidopsis cell-plate membranes mediated by sterol
RT and DYNAMIN-RELATED PROTEIN1A function.";
RL Plant J. 80:745-757(2014).
RN [25]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27251533; DOI=10.1038/nplants.2015.162;
RA Stanislas T., Hueser A., Barbosa I.C.R., Kiefer C.S., Brackmann K.,
RA Pietra S., Gustavsson A., Zourelidou M., Schwechheimer C., Grebe M.;
RT "Arabidopsis D6PK is a lipid domain-dependent mediator of root epidermal
RT planar polarity.";
RL Nat. Plants 1:15162-15162(2015).
RN [26]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-47.
RC STRAIN=cv. Columbia;
RX PubMed=27449211; DOI=10.1093/pcp/pcw121;
RA Yoshinari A., Fujimoto M., Ueda T., Inada N., Naito S., Takano J.;
RT "DRP1-dependent endocytosis is essential for polar Localization and boron-
RT induced degradation of the borate transporter BOR1 in Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 57:1985-2000(2016).
RN [27]
RP FUNCTION, AND INTERACTION WITH SH3P2.
RC STRAIN=cv. Columbia, and cv. Wassilewskija-2;
RX PubMed=28584166; DOI=10.1105/tpc.17.00108;
RA Ahn G., Kim H., Kim D.H., Hanh H., Yoon Y., Singaram I., Wijesinghe K.J.,
RA Johnson K.A., Zhuang X., Liang Z., Stahelin R.V., Jiang L., Cho W.,
RA Kang B.-H., Hwang I.;
RT "SH3 domain-containing protein 2 plays a crucial role at the step of
RT membrane tubulation during cell plate formation.";
RL Plant Cell 29:1388-1405(2017).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-325 AND 579-606 IN COMPLEX WITH
RP GTP, FUNCTION, AND SUBUNIT.
RX PubMed=22107825; DOI=10.1093/jmcb/mjr032;
RA Yan L., Ma Y., Sun Y., Gao J., Chen X., Liu J., Wang C., Rao Z., Lou Z.;
RT "Structural basis for mechanochemical role of Arabidopsis thaliana dynamin-
RT related protein in membrane fission.";
RL J. Mol. Cell Biol. 3:378-381(2011).
CC -!- FUNCTION: Microtubule-associated force-producing protein that is
CC targeted to at the leading edges of the forming cell plate during
CC cytokinesis (PubMed:18612642). Also plays a major role in plasma
CC membrane maintenance and cell wall integrity with implications in
CC vesicular trafficking, polar cell expansion, vascular formation, and
CC other aspects of plant growth and development, including stigmatic
CC papillae expansion (PubMed:18256049, PubMed:18344418). Collaboratively
CC with DRP2B, participates in clathrin-coated vesicle formation during
CC endocytosis (PubMed:20231465). Necessary for BOR1 polar localization in
CC low-boron (B) conditions as well as for BOR1 endocytosis and subsequent
CC degradation under high-concentration of boron (PubMed:27449211). Has a
CC GTPase activity (PubMed:20171176). Required for the sterols-dependent
CC dynamic high lipid order observed at the cell plate of dividing cells
CC (PubMed:25234576). Together with SH3P2, converts the fused vesicles to
CC tubular structures at the cell plate and phragmoplasts during
CC cytokinesis (PubMed:28584166, PubMed:18256049). With DRP2B and PIP5K3,
CC required for the precise coordination of polar ARAC3/ROP6 and
CC ARAC4/ROP2 placement and subsequent root hair positioning during planar
CC polarity formation in root hair-forming cells, probably by mediating
CC the correct basal-to-planar polarity switching of D6PK into the polar,
CC lipid-enriched domain (PubMed:27251533). Involved in endocytosis
CC required for cellulose deposition during cell wall formation and
CC elongation (PubMed:18256049). Interacts with plasma membrane-mimetic
CC liposomes and induces their clustering (PubMed:20171176).
CC {ECO:0000269|PubMed:11351070, ECO:0000269|PubMed:12671086,
CC ECO:0000269|PubMed:14750520, ECO:0000269|PubMed:15923323,
CC ECO:0000269|PubMed:18256049, ECO:0000269|PubMed:18344418,
CC ECO:0000269|PubMed:18612642, ECO:0000269|PubMed:20171176,
CC ECO:0000269|PubMed:20231465, ECO:0000269|PubMed:22107825,
CC ECO:0000269|PubMed:25234576, ECO:0000269|PubMed:27251533,
CC ECO:0000269|PubMed:27449211, ECO:0000269|PubMed:28584166}.
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:0000269|PubMed:20171176};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=99 uM for GTP {ECO:0000269|PubMed:20171176};
CC Note=kcat is 28 min(-1) with GTP as substrate.
CC {ECO:0000269|PubMed:20171176};
CC -!- SUBUNIT: Forms homodimer and may homooligomerize and heterooligomerize
CC to form the phragmoplastin complex (PubMed:20171176, PubMed:20231465).
CC Interacts with AGD3/VAN3. May interact with CALS1. Binds to AHK2. Binds
CC to SH3P2 (PubMed:28584166). Forms a complex made of SH3P2 and DRP1A and
CC triggers its accumulation at the cell plate (PubMed:28584166).
CC Interacts with DRP2B at the plasma membrane and in forming clathrin-
CC coated vesicles (CCV) (PubMed:20231465). Binds to PHIP1
CC (PubMed:18621982). {ECO:0000269|PubMed:14750520,
CC ECO:0000269|PubMed:15923323, ECO:0000269|PubMed:18621982,
CC ECO:0000269|PubMed:18642946, ECO:0000269|PubMed:20171176,
CC ECO:0000269|PubMed:20231465, ECO:0000269|PubMed:22107825,
CC ECO:0000269|PubMed:28584166}.
CC -!- INTERACTION:
CC P42697; Q5W7F2: AGD3; NbExp=4; IntAct=EBI-994234, EBI-994222;
CC P42697; Q9C5U2: AHK2; NbExp=3; IntAct=EBI-994234, EBI-1100634;
CC P42697; Q9LQ55: DRP2B; NbExp=4; IntAct=EBI-994234, EBI-2355848;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12671086,
CC ECO:0000269|PubMed:18612642}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14750520, ECO:0000269|PubMed:15923323,
CC ECO:0000269|PubMed:18344418, ECO:0000269|PubMed:18612642,
CC ECO:0000269|PubMed:28584166}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:12671086, ECO:0000269|PubMed:14750520,
CC ECO:0000269|PubMed:18612642, ECO:0000269|PubMed:25234576,
CC ECO:0000269|PubMed:28584166}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:18344418}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:18344418, ECO:0000269|PubMed:20231465}.
CC Cell membrane {ECO:0000269|PubMed:20231465,
CC ECO:0000269|PubMed:27251533}. Note=Microtubule-associated and localized
CC in the forming cell plate, at the vicinity of sterols, during
CC cytokinesis, especially at the leading edges (PubMed:14750520,
CC PubMed:28584166, PubMed:18612642, PubMed:25234576). Accumulates in a
CC sterol-enriched, polar membrane domain during root hair initiation
CC (PubMed:27251533). Forms discreet dynamic foci in the epidermal cell
CC cortex, which colocalize with part of the clathrin endocytic machinery
CC (PubMed:18344418). Co-localizes with BOR1 in the cell plate and the
CC plasma membrane (PubMed:27449211). {ECO:0000269|PubMed:14750520,
CC ECO:0000269|PubMed:18344418, ECO:0000269|PubMed:18612642,
CC ECO:0000269|PubMed:25234576, ECO:0000269|PubMed:27251533,
CC ECO:0000269|PubMed:27449211, ECO:0000269|PubMed:28584166}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42697-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42697-2; Sequence=VSP_009187;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in leaves (at protein level).
CC {ECO:0000269|PubMed:12834397, ECO:0000269|PubMed:15815986,
CC ECO:0000269|PubMed:7548829, ECO:0000269|PubMed:9342876}.
CC -!- DISRUPTION PHENOTYPE: Vascular discontinuity (PubMed:15923323,
CC PubMed:18344418). Short and swollen roots and hypocotyls due to
CC cellulose-deficient walls associated with increased levels of
CC arabinose, xylose, and galactose in non-cellulosic polysaccharides
CC (PubMed:18256049). Infertility due to the inability of stigmatic
CC papillae to undergo rapid polar expansion prior to fertilization
CC (PubMed:18344418). The alteration of cell wall formation correlates
CC with abnormal phragmoplasts and division plates in dividing cells, as
CC well as reduced cell elongation and disturbed endocytosis
CC (PubMed:18256049). Hypersensitivity to trafficking inhibitors (e.g.
CC brefeldin A, monensin A and latrunculin B) (PubMed:18256049). Both
CC basal and apical shift of ARAC3/ROP6 and ARAC4/ROP2 positioning and
CC broad lateral localization of D6PK in root hair-forming cells leading
CC to basal and apical shift of root hair positions (PubMed:27251533).
CC {ECO:0000269|PubMed:15923323, ECO:0000269|PubMed:18256049,
CC ECO:0000269|PubMed:18344418, ECO:0000269|PubMed:27251533}.
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=AAB63528.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L38614; AAA84446.1; -; mRNA.
DR EMBL; L36939; AAB63528.1; ALT_FRAME; mRNA.
DR EMBL; AB017067; BAB08441.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94763.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94764.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69643.1; -; Genomic_DNA.
DR EMBL; AY094408; AAM19784.1; -; mRNA.
DR EMBL; BT001063; AAN46817.1; -; mRNA.
DR EMBL; BT025994; ABG25083.1; -; mRNA.
DR EMBL; AY088201; AAM65743.1; -; mRNA.
DR EMBL; AK230240; BAF02045.1; -; mRNA.
DR PIR; S59558; S59558.
DR RefSeq; NP_001331306.1; NM_001344434.1. [P42697-1]
DR RefSeq; NP_568602.3; NM_123573.3. [P42697-2]
DR RefSeq; NP_851120.1; NM_180789.3. [P42697-1]
DR PDB; 3T34; X-ray; 2.40 A; A/B=1-325, A/B=579-606.
DR PDB; 3T35; X-ray; 3.59 A; A/B/C/D=1-325, A/B/C/D=579-606.
DR PDBsum; 3T34; -.
DR PDBsum; 3T35; -.
DR AlphaFoldDB; P42697; -.
DR SMR; P42697; -.
DR BioGRID; 19463; 14.
DR DIP; DIP-37642N; -.
DR IntAct; P42697; 8.
DR MINT; P42697; -.
DR STRING; 3702.AT5G42080.1; -.
DR iPTMnet; P42697; -.
DR PaxDb; P42697; -.
DR PRIDE; P42697; -.
DR ProteomicsDB; 224359; -. [P42697-1]
DR EnsemblPlants; AT5G42080.1; AT5G42080.1; AT5G42080. [P42697-1]
DR EnsemblPlants; AT5G42080.2; AT5G42080.2; AT5G42080. [P42697-2]
DR EnsemblPlants; AT5G42080.4; AT5G42080.4; AT5G42080. [P42697-1]
DR GeneID; 834213; -.
DR Gramene; AT5G42080.1; AT5G42080.1; AT5G42080. [P42697-1]
DR Gramene; AT5G42080.2; AT5G42080.2; AT5G42080. [P42697-2]
DR Gramene; AT5G42080.4; AT5G42080.4; AT5G42080. [P42697-1]
DR KEGG; ath:AT5G42080; -.
DR Araport; AT5G42080; -.
DR TAIR; locus:2165805; AT5G42080.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; P42697; -.
DR OMA; VDAIHYV; -.
DR PhylomeDB; P42697; -.
DR BioCyc; ARA:AT5G42080-MON; -.
DR BRENDA; 3.6.5.5; 399.
DR PRO; PR:P42697; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42697; baseline and differential.
DR Genevisible; P42697; AT.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0009504; C:cell plate; IDA:UniProtKB.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0030276; F:clathrin binding; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR GO; GO:0009920; P:cell plate formation involved in plant-type cell wall biogenesis; IDA:UniProtKB.
DR GO; GO:0080029; P:cellular response to boron-containing substance levels; IMP:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:UniProtKB.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IGI:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:TAIR.
DR GO; GO:1905952; P:regulation of lipid localization; IDA:UniProtKB.
DR GO; GO:2000694; P:regulation of phragmoplast microtubule organization; IMP:UniProtKB.
DR GO; GO:0080157; P:regulation of plant-type cell wall organization or biogenesis; IMP:UniProtKB.
DR GO; GO:0010036; P:response to boron-containing substance; IMP:UniProtKB.
DR GO; GO:0048766; P:root hair initiation; IMP:TAIR.
DR GO; GO:0048480; P:stigma development; IMP:UniProtKB.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP: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 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; GTP-binding;
KW Hydrolase; Membrane; Microtubule; Motor protein; Nucleotide-binding;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..610
FT /note="Phragmoplastin DRP1A"
FT /id="PRO_0000206577"
FT DOMAIN 31..300
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 518..610
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 41..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 67..69
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 142..145
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 211..214
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 241..244
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 44..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22107825,
FT ECO:0007744|PDB:3T34, ECO:0007744|PDB:3T35"
FT BINDING 212..217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22107825,
FT ECO:0007744|PDB:3T34, ECO:0007744|PDB:3T35"
FT BINDING 242..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22107825,
FT ECO:0007744|PDB:3T34, ECO:0007744|PDB:3T35"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 430..610
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6, ECO:0000303|Ref.7"
FT /id="VSP_009187"
FT MUTAGEN 47
FT /note="K->A: Dominant-negative mutation leading to a
FT prolonged residence time of clathrin at the plasma membrane
FT and impaired endocytosis of membrane lipids. Disturbed BOR1
FT polar localization in low-boron (B) conditions and blocked
FT BOR1 endocytosis and subsequent degradation under high-
FT concentration of boron."
FT /evidence="ECO:0000269|PubMed:27449211"
FT CONFLICT 50
FT /note="V -> A (in Ref. 5; AAM19784/AAN46817)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="R -> Q (in Ref. 2; AAB63528)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="Q -> H (in Ref. 7; AAM65743)"
FT /evidence="ECO:0000305"
FT CONFLICT 423..424
FT /note="EA -> KT (in Ref. 2; AAB63528)"
FT /evidence="ECO:0000305"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:3T34"
FT TURN 11..16
FT /evidence="ECO:0007829|PDB:3T34"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:3T34"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3T34"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:3T34"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:3T34"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3T34"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:3T34"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:3T34"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:3T34"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:3T34"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 280..296
FT /evidence="ECO:0007829|PDB:3T34"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:3T34"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:3T34"
SQ SEQUENCE 610 AA; 68172 MW; FE77E9EDBC603D91 CRC64;
MENLISLVNK IQRACTALGD HGDSSALPTL WDSLPAIAVV GGQSSGKSSV LESIVGKDFL
PRGSGIVTRR PLVLQLQKID DGTREYAEFL HLPRKKFTDF AAVRKEIQDE TDRETGRSKA
ISSVPIHLSI YSPNVVNLTL IDLPGLTKVA VDGQSDSIVK DIENMVRSYI EKPNCIILAI
SPANQDLATS DAIKISREVD PSGDRTFGVL TKIDLMDKGT DAVEILEGRS FKLKYPWVGV
VNRSQADINK NVDMIAARKR EREYFSNTTE YRHLANKMGS EHLAKMLSKH LERVIKSRIP
GIQSLINKTV LELETELSRL GKPIAADAGG KLYSIMEICR LFDQIFKEHL DGVRAGGEKV
YNVFDNQLPA ALKRLQFDKQ LAMDNIRKLV TEADGYQPHL IAPEQGYRRL IESSIVSIRG
PAEASVDTVH AILKDLVHKS VNETVELKQY PALRVEVTNA AIESLDKMRE GSKKATLQLV
DMECSYLTVD FFRKLPQDVE KGGNPTHSIF DRYNDSYLRR IGSNVLSYVN MVCAGLRNSI
PKSIVYCQVR EAKRSLLDHF FAELGTMDMK RLSSLLNEDP AIMERRSAIS KRLELYRAAQ
SEIDAVAWSK
