DRP2A_ARATH
ID DRP2A_ARATH Reviewed; 914 AA.
AC Q9SE83; Q0WPR7; Q56YX7; Q9SY71;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Dynamin-2A;
DE EC=3.6.5.5;
DE AltName: Full=Dynamin-like protein 6;
DE AltName: Full=Dynamin-related protein 2A;
GN Name=DRP2A; Synonyms=ADL6; OrderedLocusNames=At1g10290; ORFNames=F14N23.17;
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, AND MUTAGENESIS
RP OF LYS-51.
RX PubMed=11449048; DOI=10.2307/3871383;
RA Jin J.B., Kim Y.A., Kim S.J., Lee S.H., Kim D.H., Cheong G.-W., Hwang I.;
RT "A new dynamin-like protein, ADL6, is involved in trafficking from the
RT trans-Golgi network to the central vacuole in Arabidopsis.";
RL Plant Cell 13:1511-1526(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND LIPID-BINDING.
RX PubMed=12105222; DOI=10.1074/jbc.m204770200;
RA Lee S.H., Jin J.B., Song J., Min M.K., Park D.S., Kim Y.-W., Hwang I.;
RT "The intermolecular interaction between the PH domain and the C-terminal
RT domain of Arabidopsis dynamin-like 6 determines lipid binding
RT specificity.";
RL J. Biol. Chem. 277:31842-31849(2002).
RN [6]
RP FUNCTION, INTERACTION WITH SH3P3 AND GAMMA-ADR, SUBCELLULAR LOCATION,
RP ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=12207647; DOI=10.1046/j.1365-313x.2002.01377.x;
RA Lam B.C.-H., Sage T.L., Bianchi F., Blumwald E.;
RT "Regulation of ADL6 activity by its associated molecular network.";
RL Plant J. 31:565-576(2002).
RN [7]
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 [8]
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
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).
CC -!- FUNCTION: Microtubule-associated force-producing protein involved in
CC clathrin-mediated vesicle trafficking from the trans-Golgi network to
CC the central vacuole. Able to bind and hydrolyze GTP. Binds specifically
CC to phosphatidylinositol 3-phosphate (PtdIns3P).
CC {ECO:0000269|PubMed:11449048, ECO:0000269|PubMed:12105222,
CC ECO:0000269|PubMed:12207647}.
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; EC=3.6.5.5;
CC -!- ACTIVITY REGULATION: Increased GTPase activity in the presence of
CC phosphatidic acid. {ECO:0000269|PubMed:12207647}.
CC -!- SUBUNIT: Binds PtdIns3P (PubMed:12207647). Interacts with SH3P3 (via
CC SH3 domain) and (via C-terminus) with GAMMA-ADR (PubMed:12207647). May
CC homooligomerize or heterooligomerize (PubMed:14750520).
CC {ECO:0000269|PubMed:12207647, ECO:0000269|PubMed:14750520}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus membrane;
CC Peripheral membrane protein. Cytoplasm, cytoskeleton, phragmoplast.
CC Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:12207647}. Note=Localized in the forming cell plate
CC during cytokinesis.
CC -!- DOMAIN: The PH domain binds phospholipids. The PRD1 motif (721-728) is
CC necessary for the interaction with SH3P3.
CC {ECO:0000269|PubMed:12207647}.
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=AAD32879.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF180732; AAF22291.1; -; mRNA.
DR EMBL; AC005489; AAD32879.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28562.1; -; Genomic_DNA.
DR EMBL; AK221193; BAD95292.1; -; mRNA.
DR EMBL; AK228995; BAF00882.1; -; mRNA.
DR PIR; B86237; B86237.
DR RefSeq; NP_172500.1; NM_100903.4.
DR AlphaFoldDB; Q9SE83; -.
DR SMR; Q9SE83; -.
DR BioGRID; 22808; 14.
DR IntAct; Q9SE83; 2.
DR STRING; 3702.AT1G10290.1; -.
DR iPTMnet; Q9SE83; -.
DR PaxDb; Q9SE83; -.
DR PRIDE; Q9SE83; -.
DR ProteomicsDB; 224364; -.
DR EnsemblPlants; AT1G10290.1; AT1G10290.1; AT1G10290.
DR GeneID; 837568; -.
DR Gramene; AT1G10290.1; AT1G10290.1; AT1G10290.
DR KEGG; ath:AT1G10290; -.
DR Araport; AT1G10290; -.
DR TAIR; locus:2012763; AT1G10290.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_016157_1_0_1; -.
DR InParanoid; Q9SE83; -.
DR OMA; KMVRKPI; -.
DR OrthoDB; 162674at2759; -.
DR PhylomeDB; Q9SE83; -.
DR BRENDA; 3.6.5.5; 399.
DR PRO; PR:Q9SE83; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SE83; baseline and differential.
DR Genevisible; Q9SE83; AT.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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; ISS:TAIR.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:TAIR.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 2.30.29.30; -; 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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00233; PH; 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.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Golgi apparatus; GTP-binding; Hydrolase; Lipid-binding; Membrane;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..914
FT /note="Dynamin-2A"
FT /id="PRO_0000206582"
FT DOMAIN 35..303
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 572..696
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 730..823
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 45..52
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 71..73
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 143..146
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 204..207
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 238..241
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 507..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 781..805
FT /evidence="ECO:0000255"
FT COMPBIAS 521..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..914
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..52
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 143..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 204..207
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 51
FT /note="K->E: Affects the trafficking between the Golgi
FT apparatus and the vacuole."
FT /evidence="ECO:0000269|PubMed:11449048"
FT CONFLICT 617
FT /note="T -> S (in Ref. 4; BAD95292)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="E -> V (in Ref. 4; BAF00882)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="V -> G (in Ref. 4; BAD95292)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="A -> T (in Ref. 1; AAF22291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 914 AA; 99166 MW; B643C7F1900A2227 CRC64;
MEAIDELSQL SDSMKQAASL LADEDPDETS SSKRPATFLN VVALGNVGAG KSAVLNSLIG
HPVLPTGENG ATRAPIIIEL SRESSLSSKA IILQIDNKSQ QVSASALRHS LQDRLSKGAS
GKNRDEINLK LRTSTAPPLK LVDLPGLDQR IVDESMIAEY AQHNDAILLV IVPASQASEI
SSSRALKIAK EYDPESTRTI GIIGKIDQAA ENSKALAAVQ ALLSNQGPPK TTDIPWVAVI
GQSVSIASAQ SGSGENSLET AWRAESESLK SILTGAPQSK LGRIALVDTL ASQIRSRMKL
RLPSVLSGLQ GKSQIVQDEL ARLGEQLVNS AEGTRAIALE LCREFEDKFL LHLAGGEGSG
WKVVASFEGN FPNRIKQLPL DRHFDLNNVK RVVLEADGYQ PYLISPEKGL RSLIKIVLEL
AKDPARLCVD EVHRVLVDIV SASANATPGL GRYPPFKREV VAIASAALDG FKNEAKKMVV
ALVDMERAFV PPQHFIRLVQ RRMERQRREE ELKGRSSKKG QDAEQSLLSR ATSPQPDGPT
AGGSLKSMKD KPSPQDKETP EVSGLKTAGP EGEITAGYLM KKSAKTNGWS RRWFVLNEKT
GKLGYTKKQE ERNFRGTITL EECTIEEIPE DEVEKSKSSK DKKANGPDSK GPGLVFKITC
KVPYKTVLKA HNALVLKAES VVDKNEWINK LQKVIQARGG QVGSVSMRQS LSEGSLDKMV
RKPIDPEEEL RWMSQEVRGY VEAVLNSLAA NVPKAVVLCQ VEKAKEDMLN QLYSSISAIG
NERIESLIQE DQNVKRRRER YQKQSSLLSK LTRQLSIHDN RAAAASSYSD NSGTESSPRA
SGGSSGDDWM NAFNSAANGP SDSLSKYGSG GHSRRYSDPA QNGDAASPGS GSNRRTTPNR
LPPAPPPTGS AYRY
