ID DRP1B_ARATH Reviewed; 610 AA.
AC Q84XF3; Q9M362;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Phragmoplastin DRP1B {ECO:0000305};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P42697};
DE AltName: Full=Dynamin-like protein B {ECO:0000303|PubMed:11351070};
DE AltName: Full=Dynamin-related protein 1B {ECO:0000303|PubMed:14750516};
DE Short=AtDRP1B {ECO:0000303|PubMed:14750516};
GN Name=DRP1B {ECO:0000303|PubMed:14750516};
GN Synonyms=ADL1B {ECO:0000303|PubMed:11351070};
GN OrderedLocusNames=At3g61760 {ECO:0000312|Araport:AT3G61760};
GN ORFNames=F15G16.150 {ECO:0000312|EMBL:CAB71106.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=11351070; DOI=10.1104/pp.126.1.47;
RA Kang B.-H., Busse J.S., Dickey C., Rancour D.M., Bednarek S.Y.;
RT "The Arabidopsis cell plate-associated dynamin-like protein, ADL1Ap, is
RT required for multiple stages of plant growth and development.";
RL Plant Physiol. 126:47-68(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18612642; DOI=10.1007/s00299-008-0583-0;
RA Fujimoto M., Arimura S., Nakazono M., Tsutsumi N.;
RT "Arabidopsis dynamin-related protein DRP2B is co-localized with DRP1A on
RT the leading edge of the forming cell plate.";
RL Plant Cell Rep. 27:1581-1586(2008).
RN [6]
RP INTERACTION WITH PHIP1.
RX PubMed=18621982; DOI=10.1104/pp.108.120527;
RA Ma L., Xie B., Hong Z., Verma D.P.S., Zhang Z.;
RT "A novel RNA-binding protein associated with cell plate formation.";
RL Plant Physiol. 148:223-234(2008).
RN [7]
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).
CC -!- FUNCTION: Microtubule-associated force-producing protein that is
CC targeted to at the leading edges of the forming cell plate during
CC cytokinesis (PubMed:18612642). Has a GTPase activity (By similarity).
CC {ECO:0000250|UniProtKB:P42697, ECO:0000269|PubMed:18612642}.
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;
CC Evidence={ECO:0000250|UniProtKB:P42697};
CC -!- SUBUNIT: Forms homodimer and may homooligomerize and heterooligomerize
CC to form the phragmoplastin complex (By similarity). Binds to PHIP1
CC (PubMed:18621982). {ECO:0000250|UniProtKB:P42697,
CC ECO:0000269|PubMed:18621982}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18612642}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18612642}. Cytoplasm,
CC cytoskeleton, phragmoplast {ECO:0000269|PubMed:18612642}.
CC Note=Microtubule-associated and localized in the forming cell plate
CC during cytokinesis, especially at the leading edges.
CC {ECO:0000269|PubMed:18612642}.
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=CAB71106.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY189279; AAO16682.1; -; mRNA.
DR EMBL; AL132959; CAB71106.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80253.1; -; Genomic_DNA.
DR PIR; T47968; T47968.
DR RefSeq; NP_191735.2; NM_116041.3.
DR AlphaFoldDB; Q84XF3; -.
DR SMR; Q84XF3; -.
DR BioGRID; 10663; 2.
DR IntAct; Q84XF3; 1.
DR STRING; 3702.Q84XF3; -.
DR iPTMnet; Q84XF3; -.
DR PaxDb; 3702-AT3G61760-1; -.
DR ProteomicsDB; 224360; -.
DR EnsemblPlants; AT3G61760.1; AT3G61760.1; AT3G61760.
DR GeneID; 825349; -.
DR Gramene; AT3G61760.1; AT3G61760.1; AT3G61760.
DR KEGG; ath:AT3G61760; -.
DR Araport; AT3G61760; -.
DR TAIR; AT3G61760; DL1B.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_3_1; -.
DR InParanoid; Q84XF3; -.
DR OMA; DGHYRNI; -.
DR OrthoDB; 1052588at2759; -.
DR PhylomeDB; Q84XF3; -.
DR PRO; PR:Q84XF3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84XF3; baseline and differential.
DR Genevisible; Q84XF3; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF241; PHRAGMOPLASTIN DRP1B; 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; P-loop containing nucleoside triphosphate hydrolases; 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; Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..610
FT /note="Phragmoplastin DRP1B"
FT /id="PRO_0000206578"
FT DOMAIN 31..300
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 518..610
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 41..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 67..69
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 142..145
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 211..214
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 241..244
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 44..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT BINDING 212..217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT BINDING 242..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 610 AA; 68084 MW; 10B9C488898C9F5B CRC64;
MESLIALVNK IQRACTALGD HGEGSSLPTL WDSLPAIAVV GGQSSGKSSV LESVVGKDFL
PRGAGIVTRR PLVLQLHRID EGKEYAEFMH LPKKKFTDFA AVRQEISDET DRETGRSSKV
ISTVPIHLSI FSPNVVNLTL VDLPGLTKVA VDGQPESIVQ DIENMVRSFI EKPNCIILAI
SPANQDLATS DAIKISREVD PKGDRTFGVL TKIDLMDQGT NAVDILEGRG YKLRYPWVGV
VNRSQADINK SVDMIAARRR ERDYFQTSPE YRHLTERMGS EYLGKMLSKH LEVVIKSRIP
GLQSLITKTI SELETELSRL GKPVAADAGG KLYMIMEICR AFDQTFKEHL DGTRSGGEKI
NSVFDNQFPA AIKRLQFDKH LSMDNVRKLI TEADGYQPHL IAPEQGYRRL IESCLVSIRG
PAEAAVDAVH SILKDLIHKS MGETSELKQY PTLRVEVSGA AVDSLDRMRD ESRKATLLLV
DMESGYLTVE FFRKLPQDSE KGGNPTHSIF DRYNDAYLRR IGSNVLSYVN MVCAGLRNSI
PKSIVYCQVR EAKRSLLDIF FTELGQKEMS KLSKLLDEDP AVQQRRTSIA KRLELYRSAQ
TDIEAVAWSK
//
