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 02-JUN-2021, entry version 128. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q8LFT2; -. DR BioGRID; 1258; 3. 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:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. 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:0007031; P:peroxisome organization; IEA:UniProtKB-KW. DR CDD; cd08771; DLP_1; 1. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR001401; Dynamin_GTPase. DR InterPro; IPR019762; Dynamin_GTPase_CS. DR InterPro; IPR022812; Dynamin_SF. 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 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 NP_BIND 50..57 FT /note="GTP" FT /evidence="ECO:0000255" FT NP_BIND 157..161 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 226..229 FT /note="GTP" FT /evidence="ECO:0000250" 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 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 //