DRP1D_ARATH
ID DRP1D_ARATH Reviewed; 612 AA.
AC Q8S3C9; O80499; Q9FNX3; Q9FNX4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Phragmoplastin DRP1D {ECO:0000305};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P42697};
DE AltName: Full=Dynamin-like protein 1D {ECO:0000303|PubMed:11351070};
DE AltName: Full=Dynamin-like protein DLP3 {ECO:0000303|PubMed:14750516};
DE AltName: Full=Dynamin-related protein 1D {ECO:0000303|PubMed:14750516};
DE Short=AtDRP1D {ECO:0000303|PubMed:14750516};
GN Name=DRP1D {ECO:0000303|PubMed:14750516};
GN Synonyms=ADL1D {ECO:0000303|PubMed:11351070, ECO:0000303|PubMed:14750516},
GN DLP3 {ECO:0000303|PubMed:14750516};
GN OrderedLocusNames=At2g44590 {ECO:0000312|Araport:AT2G44590};
GN ORFNames=F16B22.8 {ECO:0000312|EMBL:AAC27461.1};
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 3).
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 [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Jasper F., Menzel D.;
RT "Identification of a subgroup of closely related dynamin-like proteins in
RT Arabidopsis thaliana.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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 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 [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).
CC -!- FUNCTION: Putative microtubule-associated force-producing protein. Has
CC a GTPase activity (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P42697}.
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:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Microtubule-associated. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=DLP3a;
CC IsoId=Q8S3C9-1; Sequence=Displayed;
CC Name=2; Synonyms=DLP3b;
CC IsoId=Q8S3C9-2; Sequence=VSP_012753;
CC Name=3;
CC IsoId=Q8S3C9-3; Sequence=VSP_012753, VSP_012754;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to competing acceptor splice
CC sites. {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; AF488807; AAL92169.1; -; mRNA.
DR EMBL; AJ304843; CAC19658.1; -; mRNA.
DR EMBL; AJ304844; CAC19659.1; -; mRNA.
DR EMBL; AC003672; AAC27461.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10443.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10444.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10445.1; -; Genomic_DNA.
DR PIR; T01586; T01586.
DR RefSeq; NP_850418.1; NM_180087.1. [Q8S3C9-3]
DR RefSeq; NP_850419.1; NM_180088.3. [Q8S3C9-2]
DR RefSeq; NP_850420.1; NM_180089.2. [Q8S3C9-1]
DR AlphaFoldDB; Q8S3C9; -.
DR SMR; Q8S3C9; -.
DR STRING; 3702.AT2G44590.3; -.
DR PaxDb; Q8S3C9; -.
DR PRIDE; Q8S3C9; -.
DR ProteomicsDB; 224362; -. [Q8S3C9-1]
DR EnsemblPlants; AT2G44590.1; AT2G44590.1; AT2G44590. [Q8S3C9-3]
DR EnsemblPlants; AT2G44590.2; AT2G44590.2; AT2G44590. [Q8S3C9-2]
DR EnsemblPlants; AT2G44590.3; AT2G44590.3; AT2G44590. [Q8S3C9-1]
DR GeneID; 819067; -.
DR Gramene; AT2G44590.1; AT2G44590.1; AT2G44590. [Q8S3C9-3]
DR Gramene; AT2G44590.2; AT2G44590.2; AT2G44590. [Q8S3C9-2]
DR Gramene; AT2G44590.3; AT2G44590.3; AT2G44590. [Q8S3C9-1]
DR KEGG; ath:AT2G44590; -.
DR Araport; AT2G44590; -.
DR TAIR; locus:2042371; AT2G44590.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_3_1; -.
DR InParanoid; Q8S3C9; -.
DR OMA; HGTDEYA; -.
DR PhylomeDB; Q8S3C9; -.
DR PRO; PR:Q8S3C9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S3C9; baseline and differential.
DR Genevisible; Q8S3C9; 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: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 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; Cytoplasm; Cytoskeleton; GTP-binding;
KW Hydrolase; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..612
FT /note="Phragmoplastin DRP1D"
FT /id="PRO_0000206580"
FT DOMAIN 32..301
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 520..612
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 42..49
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 68..70
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 212..215
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 242..245
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 45..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT BINDING 213..218
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P42697"
FT BINDING 243..246
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:0000250|UniProtKB:P42697"
FT VAR_SEQ 136..152
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11351070, ECO:0000303|Ref.2"
FT /id="VSP_012753"
FT VAR_SEQ 570
FT /note="Q -> QQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11351070"
FT /id="VSP_012754"
SQ SEQUENCE 612 AA; 68373 MW; DA3F7E8718166558 CRC64;
MESLIVLINT IQRACTVVGD HGGDSNALSS LWEALPSVAV VGGQSSGKSS VLESIVGRDF
LPRGSGIVTR RPLVLQLHKT ENGTEDNAEF LHLTNKKFTN FSLVRKEIED ETDRITGKNK
QISSIPIHLS IFSPNVVNLT LIDLPGLTKV AVEGQPETIV EDIESMVRSY VEKPNCLILA
ISPANQDIAT SDAMKLAKEV DPIGDRTFGV LTKLDLMDKG TNALDVINGR SYKLKYPWVG
IVNRSQADIN KNVDMMVARR KEREYFETSP DYGHLATRMG SEYLAKLLSK LLESVIRSRI
PSILSLINNN IEELERELDQ LGRPIAIDAG AQLYTILGMC RAFEKIFKEH LDGGRPGGAR
IYGIFDYNLP TAIKKLPFDR HLSLQSVKRI VSESDGYQPH LIAPELGYRR LIEGSLNHFR
GPAEASVNAI HLILKELVRK AIAETEELKR FPSLQIELVA AANSSLDKFR EESMKSVLRL
VDMESSYLTV DFFRKLHVES QNMSLSSPTS AIDQYGDGHF RKIASNVAAY IKMVAETLVN
TIPKAVVHCQ VRQAKLSLLN YFYAQISQSQ GKRLGQLLDE NPALMERRMQ CAKRLELYKK
ARDEIDAAVW VR
