DRP3A_ARATH
ID DRP3A_ARATH Reviewed; 808 AA.
AC Q8S944; O22403; O81882; Q94CF3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Dynamin-related protein 3A;
DE AltName: Full=Dynamin-like protein 2;
DE AltName: Full=Dynamin-like protein 2a;
GN Name=DRP3A; Synonyms=ADL2, ADL2A; OrderedLocusNames=At4g33650;
GN ORFNames=T16L1.140;
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;
RX PubMed=9747851; DOI=10.1023/a:1006099718761;
RA Kang S.G., Jin J.B., Piao H.L., Pih K.T., Jang H.J., Lim J.H., Hwang I.;
RT "Molecular cloning of an Arabidopsis cDNA encoding a dynamin-like protein
RT that is localized to plastids.";
RL Plant Mol. Biol. 38:437-447(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11960028; DOI=10.1073/pnas.082663299;
RA Arimura S., Tsutsumi N.;
RT "A dynamin-like protein (ADL2b), rather than FtsZ, is involved in
RT Arabidopsis mitochondrial division.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5727-5731(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 2).
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 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 [7]
RP FUNCTION.
RX PubMed=14754924; DOI=10.1093/jxb/erh073;
RA Logan D.C., Scott I., Tobin A.K.;
RT "ADL2a, like ADL2b, is involved in the control of higher plant
RT mitochondrial morphology.";
RL J. Exp. Bot. 55:783-785(2004).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14988495; DOI=10.1093/pcp/pch024;
RA Arimura S., Aida G.P., Fujimoto M., Nakazono M., Tsutsumi N.;
RT "Arabidopsis dynamin-like protein 2a (ADL2a), like ADL2b, is involved in
RT plant mitochondrial division.";
RL Plant Cell Physiol. 45:236-242(2004).
RN [9]
RP SUBUNIT, AND INTERACTION WITH ELM1.
RX PubMed=18559960; DOI=10.1105/tpc.108.058578;
RA Arimura S., Fujimoto M., Doniwa Y., Kadoya N., Nakazono M., Sakamoto W.,
RA Tsutsumi N.;
RT "Arabidopsis ELONGATED MITOCHONDRIA1 is required for localization of
RT DYNAMIN-RELATED PROTEIN3A to mitochondrial fission sites.";
RL Plant Cell 20:1555-1566(2008).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18539750; DOI=10.1105/tpc.107.057679;
RA Lingard M.J., Gidda S.K., Bingham S., Rothstein S.J., Mullen R.T.,
RA Trelease R.N.;
RT "Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A
RT cooperate in cell cycle-associated replication of peroxisomes.";
RL Plant Cell 20:1567-1585(2008).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-82 AND ALA-209.
RX PubMed=18785999; DOI=10.1111/j.1365-313x.2008.03677.x;
RA Zhang X., Hu J.;
RT "Two small protein families, DYNAMIN-RELATED PROTEIN3 and FISSION1, are
RT required for peroxisome fission in Arabidopsis.";
RL Plant J. 57:146-159(2009).
RN [12]
RP INTERACTION WITH ARC5, AND SUBCELLULAR LOCATION.
RX PubMed=20179140; DOI=10.1105/tpc.109.071324;
RA Zhang X., Hu J.;
RT "The Arabidopsis chloroplast division protein DYNAMIN-RELATED PROTEIN5B
RT also mediates peroxisome division.";
RL Plant Cell 22:431-442(2010).
CC -!- FUNCTION: Involved in the control of mitochondrial and peroxisomal
CC division and morphology. In association with PEX11C, PEX11D, PEX11E and
CC FIS1B, is involved in cell cycle-associated constitutive self-
CC replication of preexisting peroxisomes. {ECO:0000269|PubMed:14754924,
CC ECO:0000269|PubMed:14988495, ECO:0000269|PubMed:18539750,
CC ECO:0000269|PubMed:18785999}.
CC -!- SUBUNIT: Homooligomer. Interacts with ARC5 on peroxisomes and ELM1 on
CC mitochondria. {ECO:0000269|PubMed:18559960,
CC ECO:0000269|PubMed:20179140}.
CC -!- INTERACTION:
CC Q8S944; Q8S944: DRP3A; NbExp=3; IntAct=EBI-2265428, EBI-2265428;
CC Q8S944; Q8LFT2: DRP3B; NbExp=6; IntAct=EBI-2265428, EBI-2265511;
CC Q8S944; P94077: LSD1; NbExp=7; IntAct=EBI-2265428, EBI-5849461;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14988495}.
CC Peroxisome {ECO:0000269|PubMed:18539750, ECO:0000269|PubMed:20179140}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S944-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S944-2; Sequence=VSP_012755, VSP_012756;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed in flowers.
CC {ECO:0000269|PubMed:9747851}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant growth. Increase in the size of
CC peroxisomes and decrease in the number of peroxisomes per cell.
CC Elongated mitochondria. {ECO:0000269|PubMed:18785999}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; AF012833; AAC61784.1; -; mRNA.
DR EMBL; AB072373; BAB85643.1; -; mRNA.
DR EMBL; AB072374; BAB85644.1; -; mRNA.
DR EMBL; AL031394; CAA20578.1; -; Genomic_DNA.
DR EMBL; AL161583; CAB80082.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86260.1; -; Genomic_DNA.
DR EMBL; AY034905; AAK59412.1; -; mRNA.
DR EMBL; AY063086; AAL34260.1; -; mRNA.
DR PIR; T04982; T04982.
DR RefSeq; NP_567931.1; NM_119521.5. [Q8S944-1]
DR AlphaFoldDB; Q8S944; -.
DR SMR; Q8S944; -.
DR BioGRID; 14788; 7.
DR DIP; DIP-47338N; -.
DR IntAct; Q8S944; 2.
DR STRING; 3702.AT4G33650.2; -.
DR iPTMnet; Q8S944; -.
DR PaxDb; Q8S944; -.
DR PRIDE; Q8S944; -.
DR ProteomicsDB; 224366; -. [Q8S944-1]
DR EnsemblPlants; AT4G33650.1; AT4G33650.1; AT4G33650. [Q8S944-1]
DR GeneID; 829506; -.
DR Gramene; AT4G33650.1; AT4G33650.1; AT4G33650. [Q8S944-1]
DR KEGG; ath:AT4G33650; -.
DR Araport; AT4G33650; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; Q8S944; -.
DR PhylomeDB; Q8S944; -.
DR BioCyc; ARA:AT4G33650-MON; -.
DR PRO; PR:Q8S944; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8S944; baseline and differential.
DR Genevisible; Q8S944; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0000266; P:mitochondrial fission; IBA:GO_Central.
DR GO; GO:0016559; P:peroxisome fission; IBA:GO_Central.
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 Alternative splicing; Cell cycle; Cell division; GTP-binding; Hydrolase;
KW Mitochondrion; Motor protein; Nucleotide-binding; Peroxisome;
KW Peroxisome biogenesis; Reference proteome.
FT CHAIN 1..808
FT /note="Dynamin-related protein 3A"
FT /id="PRO_0000206584"
FT DOMAIN 56..330
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 670..761
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..73
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 92..94
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 172..175
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 241..244
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 271..274
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 548..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 172..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 241..244
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 473..480
FT /note="ISHRCMMN -> VSVFLVCC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_012755"
FT VAR_SEQ 481..808
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_012756"
FT MUTAGEN 82
FT /note="R->H: In drp3a-1; elongated mitochondria."
FT /evidence="ECO:0000269|PubMed:18785999"
FT MUTAGEN 209
FT /note="A->T: In drp3a-2; elongated mitochondria."
FT /evidence="ECO:0000269|PubMed:18785999"
FT CONFLICT 495..497
FT /note="VIG -> LSGR (in Ref. 1; AAC61784)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="A -> T (in Ref. 1; AAC61784)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="I -> V (in Ref. 1; AAC61784)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="S -> N (in Ref. 1; AAC61784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 808 AA; 89627 MW; A3A3E5154AF659ED CRC64;
MTIEEVSGET PPSTPPSSST PSPSSSTTNA APLGSSVIPI VNKLQDIFAQ LGSQSTIALP
QVVVVGSQSS GKSSVLEALV GRDFLPRGND ICTRRPLVLQ LLQTKSRANG GSDDEWGEFR
HLPETRFYDF SEIRREIEAE TNRLVGENKG VADTQIRLKI SSPNVLNITL VDLPGITKVP
VGDQPSDIEA RIRTMILSYI KQDTCLILAV TPANTDLANS DALQIASIVD PDGHRTIGVI
TKLDIMDKGT DARKLLLGNV VPLRLGYVGV VNRCQEDILL NRTVKEALLA EEKFFRSHPV
YHGLADRLGV PQLAKKLNQI LVQHIKVLLP DLKSRISNAL VATAKEHQSY GELTESRAGQ
GALLLNFLSK YCEAYSSLLE GKSEEMSTSE LSGGARIHYI FQSIFVKSLE EVDPCEDLTD
DDIRTAIQNA TGPRSALFVP DVPFEVLVRR QISRLLDPSL QCARFIFEEL IKISHRCMMN
ELQRFPVLRK RMDEVIGDFL REGLEPSEAM IGDIIDMEMD YINTSHPNFI GGTKAVEAAM
HQVKSSRIPH PVARPKDTVE PDRTSSSTSQ VKSRSFLGRQ ANGIVTDQGV VSADAEKAQP
AANASDTRWG IPSIFRGGDT RAVTKDSLLN KPFSEAVEDM SHNLSMIYLK EPPAVLRPTE
THSEQEAVEI QITKLLLRSY YDIVRKNIED SVPKAIMHFL VNHTKRELHN VFIKKLYREN
LFEEMLQEPD EIAVKRKRTQ ETLHVLQQAY RTLDELPLEA DSVSAGMSKH QELLTSSKYS
TSSSYSASPS TTRRSRRAGD QHQNGYGF
