DRP2B_ARATH
ID DRP2B_ARATH Reviewed; 920 AA.
AC Q9LQ55; Q9SLT3; Q9SLT4; Q9SXX3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Dynamin-2B {ECO:0000303|PubMed:14750516};
DE EC=3.6.5.5 {ECO:0000250|UniProtKB:O00429};
DE AltName: Full=Dynamin-like protein 3 {ECO:0000303|PubMed:10938838};
DE AltName: Full=Dynamin-related protein 2B {ECO:0000303|PubMed:14750516};
GN Name=DRP2B {ECO:0000303|PubMed:14750516};
GN Synonyms=ADL3 {ECO:0000303|PubMed:10938838},
GN CF1 {ECO:0000303|PubMed:14750516};
GN OrderedLocusNames=At1g59610 {ECO:0000312|Araport:AT1G59610};
GN ORFNames=T30E16.17 {ECO:0000312|EMBL:AAF79753.1};
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], AND TISSUE SPECIFICITY.
RX PubMed=10938838; DOI=10.1093/jexbot/51.343.317;
RA Mikami K., Iuchi S., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "A novel Arabidopsis thaliana dynamin-like protein containing the
RT pleckstrin homology domain.";
RL J. Exp. Bot. 51:317-318(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10548732; DOI=10.1016/s0378-1119(99)00403-5;
RA Kato A., Suzuki M., Kuwahara A., Ooe H., Higano-Inaba K., Komeda Y.;
RT "Isolation and analysis of cDNA within a 300 kb Arabidopsis thaliana
RT genomic region located around the 100 map unit of chromosome 1.";
RL Gene 239:309-316(1999).
RN [3]
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 [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].
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 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DRP1A.
RC STRAIN=cv. Columbia;
RX PubMed=20231465; DOI=10.1073/pnas.0913562107;
RA Fujimoto M., Arimura S., Ueda T., Takanashi H., Hayashi Y., Nakano A.,
RA Tsutsumi N.;
RT "Arabidopsis dynamin-related proteins DRP2B and DRP1A participate together
RT in clathrin-coated vesicle formation during endocytosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6094-6099(2010).
RN [9]
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).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27251533; DOI=10.1038/nplants.2015.162;
RA Stanislas T., Hueser A., Barbosa I.C.R., Kiefer C.S., Brackmann K.,
RA Pietra S., Gustavsson A., Zourelidou M., Schwechheimer C., Grebe M.;
RT "Arabidopsis D6PK is a lipid domain-dependent mediator of root epidermal
RT planar polarity.";
RL Nat. Plants 1:15162-15162(2015).
CC -!- FUNCTION: Putative microtubule-associated force-producing protein, able
CC to bind and hydrolyze GTP (By similarity). Collaboratively with DRP1A,
CC participates in clathrin-coated vesicle formation during endocytosis
CC (PubMed:20231465). With DRP1A and PIP5K3, required for the precise
CC coordination of polar ARAC3/ROP6 and ARAC4/ROP2 placement and
CC subsequent root hair positioning during planar polarity formation in
CC root hair-forming cells (PubMed:27251533).
CC {ECO:0000250|UniProtKB:O00429, ECO:0000269|PubMed:20231465,
CC ECO:0000269|PubMed:27251533}.
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 Evidence={ECO:0000250|UniProtKB:O00429};
CC -!- SUBUNIT: Interacts with DRP1A at the plasma membrane and in forming
CC clathrin-coated vesicles (CCV). {ECO:0000269|PubMed:20231465}.
CC -!- INTERACTION:
CC Q9LQ55; P42697: DRP1A; NbExp=4; IntAct=EBI-2355848, EBI-994234;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:20231465}. Cell membrane
CC {ECO:0000269|PubMed:20231465, ECO:0000269|PubMed:27251533}.
CC Note=Accumulates in a sterol-enriched, polar membrane domain during
CC root hair initiation. {ECO:0000269|PubMed:27251533}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed in siliques.
CC {ECO:0000269|PubMed:10938838}.
CC -!- DISRUPTION PHENOTYPE: Basal shift of ARAC3/ROP6 and ARAC4/ROP2
CC positioning in root hair-forming cells leading to basal shift of root
CC hair positions. {ECO:0000269|PubMed:27251533}.
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=AAF79753.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA77516.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA88113.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB026987; BAA77516.1; ALT_FRAME; mRNA.
DR EMBL; AB028467; BAA88111.1; -; mRNA.
DR EMBL; AB028469; BAA88113.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009317; AAF79753.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33594.1; -; Genomic_DNA.
DR EMBL; AY049230; AAK83573.1; -; mRNA.
DR EMBL; BT000772; AAN31911.1; -; mRNA.
DR EMBL; BT009695; AAP88329.1; -; mRNA.
DR PIR; H96619; H96619.
DR PIR; T52426; T52426.
DR RefSeq; NP_176170.1; NM_104654.5.
DR AlphaFoldDB; Q9LQ55; -.
DR SMR; Q9LQ55; -.
DR BioGRID; 27476; 13.
DR DIP; DIP-53383N; -.
DR IntAct; Q9LQ55; 6.
DR STRING; 3702.AT1G59610.1; -.
DR iPTMnet; Q9LQ55; -.
DR PaxDb; Q9LQ55; -.
DR PRIDE; Q9LQ55; -.
DR ProteomicsDB; 224365; -.
DR EnsemblPlants; AT1G59610.1; AT1G59610.1; AT1G59610.
DR GeneID; 842251; -.
DR Gramene; AT1G59610.1; AT1G59610.1; AT1G59610.
DR KEGG; ath:AT1G59610; -.
DR Araport; AT1G59610; -.
DR TAIR; locus:2202847; AT1G59610.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_016157_1_0_1; -.
DR InParanoid; Q9LQ55; -.
DR OMA; IMDESMV; -.
DR OrthoDB; 162674at2759; -.
DR PhylomeDB; Q9LQ55; -.
DR PRO; PR:Q9LQ55; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQ55; baseline and differential.
DR Genevisible; Q9LQ55; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0030276; F:clathrin binding; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:TAIR.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:TAIR.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:TAIR.
DR GO; GO:0048766; P:root hair initiation; 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; Cell membrane; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; GTP-binding; Hydrolase; Membrane; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..920
FT /note="Dynamin-2B"
FT /id="PRO_0000206583"
FT DOMAIN 35..303
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 579..703
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 737..830
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..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..761
FT /note="Important for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT REGION 828..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 788..812
FT /evidence="ECO:0000255"
FT COMPBIAS 521..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 204..210
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 246..249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 920 AA; 100228 MW; D95964FE33B79AB2 CRC64;
MEAIDELSQL SDSMRQAASL LADEDPDETS SSRRPATSLN VVALGNVGAG KSAVLNSLIG
HPVLPTGENG ATRAPIIIDL SREESLSSKA IILQIDNKNQ QVSASALRHS LQDRLSKGAS
GRGRDEIYLK LRTSTAPPLK LIDLPGLDQR IVDDSMIGEH AQHNDAILLV VVPASQASEI
SSSRALKIAK EYDPESTRTV GIISKIDQAA ENPKSLAAVQ ALLSNQGPPK TTDIPWVALI
GQSVSIASAQ SGGSENSLET AWRAESESLK SILTGAPQSK LGRIALVDTL ASQIRSRMKL
RLPNILTGLQ GKSQIVQDEL ARLGEQLVSS AEGTRAIALE LCREFEDKFL LHLAGGEGSG
WKVVASFEGN FPNRIKKLPL DRHFDLNNVK RIVLEADGYQ PYLISPEKGL RSLIKTVLEL
AKDPARLCVD EVHRVLVDIV SASANATPGL GRYPPFKREV VAIASAALDG FKNEAKKMVV
ALVDMERAFV PPQHFIRLVQ RRMERQRREE ELKGRSSKKG QDAEQSLLNR ATSPQPDGPS
STGGSLKSLR DKLMPQDKDK DKEKETPEVS GLKTAGPEGE ITAGYLMKKS AKTNGWSRRW
FVLNEKTGKL GYTKKQEERN FRGTVTLEEC SIEEISDDEG EKSKSSKDKK SNGPDSKGPG
LVFKITCRVP YKTVLKAHNA LVLKAESMVD KNEWINKLQK VIQARGGQVG SASMRQSLSE
GSLDKMVRKP VDPEEELRWM SQEVRGYVEA VLNSLAANVP KAVVLCQVEK SKEDMLNQLY
SSISAIGNER IESLIQEDQN VKRRRDRYQK QSSLLSKLTR QLSIHDNRAA AASSWSDNSG
TESSPRTNGG SSGEDWMNAF NAAASGPDSL KRYGSGGHSR RYSDPAQNGE DSSGSGGSSR
RTTPNRLPPA PPQSGSSYRY
