DRP3B_ARATH
ID DRP3B_ARATH Reviewed; 780 AA.
AC Q8LFT2; Q8LPH8; Q8S8A4; Q8S943; Q9SI47;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Dynamin-related protein 3B;
DE AltName: Full=Dynamin-like protein 2b;
GN Name=DRP3B; Synonyms=ADL2B; OrderedLocusNames=At2g14120; ORFNames=T22C12.1;
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).
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 [2]
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 [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] (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 [5]
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 [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 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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [11]
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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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: Involved in the control of mitochondrial and peroxisomal
CC division and morphology. {ECO:0000269|PubMed:14754924,
CC ECO:0000269|PubMed:14988495, ECO:0000269|PubMed:18785999}.
CC -!- SUBUNIT: Interacts with ARC5 on peroxisomes and ELM1 on mitochondria.
CC {ECO:0000269|PubMed:18559960, ECO:0000269|PubMed:20179140}.
CC -!- INTERACTION:
CC Q8LFT2; Q8S944: DRP3A; NbExp=6; IntAct=EBI-2265511, EBI-2265428;
CC Q8LFT2; P94077: LSD1; NbExp=3; IntAct=EBI-2265511, EBI-5849461;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14988495}.
CC Peroxisome {ECO:0000269|PubMed:18785999, ECO:0000269|PubMed:20179140}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LFT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LFT2-2; Sequence=VSP_012757, VSP_012758;
CC -!- DISRUPTION PHENOTYPE: Reduced plant growth. Increase in the size of
CC peroxisomes and decrease in the number of peroxisomes per cell.
CC {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; AB072375; BAB85645.1; -; mRNA.
DR EMBL; AC007197; AAM15450.1; -; Genomic_DNA.
DR EMBL; AC007197; AAD25856.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06282.1; -; Genomic_DNA.
DR EMBL; AY099768; AAM20619.1; -; mRNA.
DR EMBL; AY084657; AAM61220.1; -; mRNA.
DR PIR; D84514; D84514.
DR RefSeq; NP_565362.1; NM_126984.4. [Q8LFT2-1]
DR AlphaFoldDB; Q8LFT2; -.
DR SMR; Q8LFT2; -.
DR BioGRID; 1258; 6.
DR IntAct; Q8LFT2; 2.
DR STRING; 3702.AT2G14120.3; -.
DR iPTMnet; Q8LFT2; -.
DR PaxDb; Q8LFT2; -.
DR ProteomicsDB; 224367; -. [Q8LFT2-1]
DR EnsemblPlants; AT2G14120.1; AT2G14120.1; AT2G14120. [Q8LFT2-1]
DR GeneID; 815898; -.
DR Gramene; AT2G14120.1; AT2G14120.1; AT2G14120. [Q8LFT2-1]
DR KEGG; ath:AT2G14120; -.
DR Araport; AT2G14120; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; Q8LFT2; -.
DR PhylomeDB; Q8LFT2; -.
DR PRO; PR:Q8LFT2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LFT2; baseline and differential.
DR Genevisible; Q8LFT2; 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: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 Acetylation; Alternative splicing; Cell cycle; Cell division; GTP-binding;
KW Hydrolase; Mitochondrion; Motor protein; Nucleotide-binding; Peroxisome;
KW Peroxisome biogenesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..780
FT /note="Dynamin-related protein 3B"
FT /id="PRO_0000206585"
FT DOMAIN 40..315
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 654..745
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 50..57
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 76..78
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 157..160
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 226..229
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 256..259
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 536..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 157..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 226..229
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 343..370
FT /note="GGQGALLLSFITKYCEAYSSTLEGKSKE -> VCGFWPVLALYIPSILNDGI
FT AICFFCVV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_012757"
FT VAR_SEQ 371..780
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_012758"
FT CONFLICT 96
FT /note="S -> P (in Ref. 1; BAB85645)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="N -> S (in Ref. 4; AAM20619)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8LFT2-2:369
FT /note="V -> I (in Ref. 5; AAM61220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 780 AA; 86644 MW; CB50374F3F428714 CRC64;
MSVDDLPPSS ASAVTPLGSS VIPIVNKLQD IFAQLGSQST IALPQVAVVG SQSSGKSSVL
EALVGRDFLP RGNDICTRRP LRLQLVQTKP SSDGGSDEEW GEFLHHDPVR RIYDFSEIRR
EIEAETNRVS GENKGVSDIP IGLKIFSPNV LDISLVDLPG ITKVPVGDQP SDIEARIRTM
ILTYIKEPSC LILAVSPANT DLANSDALQI AGNADPDGHR TIGVITKLDI MDRGTDARNH
LLGKTIPLRL GYVGVVNRSQ EDILMNRSIK DALVAEEKFF RSRPVYSGLT DRLGVPQLAK
KLNQVLVQHI KALLPSLKSR INNALFATAK EYESYGDITE SRGGQGALLL SFITKYCEAY
SSTLEGKSKE MSTSELSGGA RILYIFQSVF VKSLEEVDPC EDLTADDIRT AIQNATGPRS
ALFVPDVPFE VLVRRQISRL LDPSLQCARF IFDELVKISH QCMMKELQRF PVLQKRMDEV
IGNFLREGLE PSQAMIRDLI EMEMDYINTS HPNFIGGTKA VEQAMQTVKS SRIPHPVARP
RDTVEPERTA SSGSQIKTRS FLGRQANGII TDQAVPTAAD AERPAPAGST SWSGFSSIFR
GSDGQAAAKN NLLNKPFSET TQEVYQNLST IYLKEPPTIL KSSETHSEQE SVEIEITKLL
LKSYYDIVRK NVEDLVPKAI MHFLVNYTKR ELHNVFIEKL YRENLIEELL KEPDELAIKR
KRTQETLRIL QQANRTLDEL PLEAESVERG YKIGSEAKHE ELPGTRRSRT ETNGNGRLHM
