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 21-MAR-2012, entry version 67. DE RecName: Full=Dynamin-related protein 3B; DE AltName: Full=Dynamin-like protein 2b; GN Name=DRP3B; Synonyms=ADL2B; OrderedLocusNames=At2g14120; GN ORFNames=T22C12.1; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX MEDLINE=21957292; 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 MEDLINE=20083487; 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., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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., RA Verma D.P.S.; RT "A unified nomenclature for Arabidopsis dynamin-related large GTPases RT based 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 RT in plant mitochondrial division."; RL Plant Cell Physiol. 45:236-242(2004). RN [9] 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 RT PROTEIN5B also mediates peroxisome division."; RL Plant Cell 22:431-442(2010). CC -!- FUNCTION: Involved in the control of mitochondrial division and CC morphology. CC -!- SUBUNIT: Interacts with ARC5 on peroxisomes. CC -!- INTERACTION: CC Q8S944:DRP3A; NbExp=6; IntAct=EBI-2265511, EBI-2265428; CC -!- SUBCELLULAR LOCATION: Mitochondrion. Peroxisome. 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 Note=May be due to an intron retention. No experimental CC confirmation available. Ref.5 (AAM61220) sequence is in conflict CC in position: 369:V->I; CC -!- SIMILARITY: Belongs to the dynamin family. CC -!- SIMILARITY: Contains 1 GED domain. 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 IPI; IPI00524723; -. DR IPI; IPI00530031; -. DR PIR; D84514; D84514. DR RefSeq; NP_565362.1; NM_126984.3. DR UniGene; At.21893; -. DR UniGene; At.67230; -. DR ProteinModelPortal; Q8LFT2; -. DR SMR; Q8LFT2; 18-741. DR IntAct; Q8LFT2; 1. DR STRING; Q8LFT2; -. DR PRIDE; Q8LFT2; -. DR EnsemblPlants; AT2G14120.1; AT2G14120.1; AT2G14120. DR GeneID; 815898; -. DR GenomeReviews; CT485783_GR; AT2G14120. DR KEGG; ath:AT2G14120; -. DR GeneFarm; 4745; 463. DR TAIR; At2g14120; -. DR eggNOG; COG0699; -. DR HOGENOM; HBG434086; -. DR InParanoid; Q8LFT2; -. DR KO; K01528; -. DR PhylomeDB; Q8LFT2; -. DR ProtClustDB; CLSN2688106; -. DR ArrayExpress; Q8LFT2; -. DR Genevestigator; Q8LFT2; -. 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; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW. DR InterPro; IPR022812; Dynamin. DR InterPro; IPR000375; Dynamin_central. DR InterPro; IPR001401; Dynamin_GTPase. DR InterPro; IPR019762; Dynamin_GTPase_CS. DR InterPro; IPR003130; GED. DR InterPro; IPR020850; GTPase_effector_domain_GED. 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 PROSITE; PS00410; DYNAMIN; 1. DR PROSITE; PS51388; GED; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Cell division; Complete proteome; KW GTP-binding; Hydrolase; Mitochondrion; Motor protein; KW Nucleotide-binding; Peroxisome; Peroxisome biogenesis; KW Reference proteome. FT CHAIN 1 780 Dynamin-related protein 3B. FT /FTId=PRO_0000206585. FT DOMAIN 654 745 GED. FT NP_BIND 50 57 GTP (Potential). FT NP_BIND 157 161 GTP (By similarity). FT NP_BIND 226 229 GTP (By similarity). FT VAR_SEQ 343 370 GGQGALLLSFITKYCEAYSSTLEGKSKE -> VCGFWPVLA FT LYIPSILNDGIAICFFCVV (in isoform 2). FT /FTId=VSP_012757. FT VAR_SEQ 371 780 Missing (in isoform 2). FT /FTId=VSP_012758. FT CONFLICT 96 96 S -> P (in Ref. 1; BAB85645). FT CONFLICT 204 204 N -> S (in Ref. 4; AAM20619). 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 //