DRP1C_ARATH
ID DRP1C_ARATH Reviewed; 614 AA.
AC Q8LF21; Q8S3C8; Q9FNX6; Q9LQU8; Q9SE81;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phragmoplastin DRP1C {ECO:0000305};
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P42697};
DE AltName: Full=Dynamin-like protein 1C {ECO:0000303|PubMed:11351070, ECO:0000303|PubMed:12834397, ECO:0000303|PubMed:14750516};
DE AltName: Full=Dynamin-like protein 5 {ECO:0000303|PubMed:14750516};
DE AltName: Full=Dynamin-like protein DLP1 {ECO:0000303|PubMed:14750516};
DE AltName: Full=Dynamin-related protein 1C {ECO:0000303|PubMed:14750516, ECO:0000303|PubMed:14750520};
DE Short=AtDRP1C {ECO:0000303|PubMed:14750516, ECO:0000303|PubMed:14750520};
GN Name=DRP1C {ECO:0000303|PubMed:14750516, ECO:0000303|PubMed:14750520};
GN Synonyms=ADL1C {ECO:0000303|PubMed:11351070, ECO:0000303|PubMed:12834397,
GN ECO:0000303|PubMed:14750516}, ADL5 {ECO:0000303|PubMed:14750516},
GN DLP1 {ECO:0000303|PubMed:14750516};
GN OrderedLocusNames=At1g14830 {ECO:0000312|Araport:AT1G14830};
GN ORFNames=F10B6.23 {ECO:0000312|EMBL:AAF79238.1};
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].
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].
RA Kang Y.N., Kim S.H., Hwang I.;
RT "Presence of multiple isoforms of dynamin-like proteins in Arabidopsis and
RT their differential expression.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Root;
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 [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12834397; DOI=10.1046/j.1365-313x.2003.01775.x;
RA Kang B.-H., Rancour D.M., Bednarek S.Y.;
RT "The dynamin-like protein ADL1C is essential for plasma membrane
RT maintenance during pollen maturation.";
RL Plant J. 35:1-15(2003).
RN [9]
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 [10]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=14750520; DOI=10.1023/b:plan.0000006936.50532.3a;
RA Hong Z., Geisler-Lee C.J., Zhang Z., Verma D.P.S.;
RT "Phragmoplastin dynamics: multiple forms, microtubule association and their
RT roles in cell plate formation in plants.";
RL Plant Mol. Biol. 53:297-312(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18344418; DOI=10.1104/pp.108.116863;
RA Konopka C.A., Bednarek S.Y.;
RT "Comparison of the dynamics and functional redundancy of the Arabidopsis
RT dynamin-related isoforms DRP1A and DRP1C during plant development.";
RL Plant Physiol. 147:1590-1602(2008).
RN [13]
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: Microtubule-associated force-producing protein that is
CC targeted to the growing edges of the cell plate during cytokinesis.
CC Also plays a major role in plasma membrane maintenance during pollen
CC maturation (PubMed:18344418). Has a GTPase activity (By similarity).
CC {ECO:0000250|UniProtKB:P42697, ECO:0000269|PubMed:12834397,
CC ECO:0000269|PubMed:14750520, ECO:0000269|PubMed:18344418}.
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 (PubMed:14750520). Binds to PHIP1
CC (PubMed:18621982). {ECO:0000269|PubMed:14750520,
CC ECO:0000269|PubMed:18621982}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14750520}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14750520,
CC ECO:0000269|PubMed:18344418}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:18344418}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:18344418}. Cytoplasm, cytoskeleton,
CC phragmoplast {ECO:0000269|PubMed:14750520}. Note=Microtubule-associated
CC and localized in the forming cell plate during cytokinesis
CC (PubMed:14750520). Forms dynamic foci in the cell cortex, which
CC colocalize with part of the clathrin endocytic machinery
CC (PubMed:18344418). {ECO:0000269|PubMed:14750520,
CC ECO:0000269|PubMed:18344418}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12834397}.
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=AAF79238.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL92170.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF488808; AAL92170.1; ALT_INIT; mRNA.
DR EMBL; AF180734; AAF22293.1; -; mRNA.
DR EMBL; AJ304841; CAC19656.1; -; mRNA.
DR EMBL; AC006917; AAF79238.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29232.1; -; Genomic_DNA.
DR EMBL; AY039955; AAK64059.1; -; mRNA.
DR EMBL; AY150494; AAN12911.1; -; mRNA.
DR EMBL; AY085091; AAM61645.1; -; mRNA.
DR RefSeq; NP_172936.1; NM_101352.3.
DR AlphaFoldDB; Q8LF21; -.
DR SMR; Q8LF21; -.
DR BioGRID; 23288; 10.
DR IntAct; Q8LF21; 8.
DR STRING; 3702.AT1G14830.1; -.
DR SwissPalm; Q8LF21; -.
DR PaxDb; Q8LF21; -.
DR PRIDE; Q8LF21; -.
DR ProteomicsDB; 224361; -.
DR EnsemblPlants; AT1G14830.1; AT1G14830.1; AT1G14830.
DR GeneID; 838048; -.
DR Gramene; AT1G14830.1; AT1G14830.1; AT1G14830.
DR KEGG; ath:AT1G14830; -.
DR Araport; AT1G14830; -.
DR TAIR; locus:2006777; AT1G14830.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_3_1; -.
DR InParanoid; Q8LF21; -.
DR OMA; VNSYINM; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; Q8LF21; -.
DR PRO; PR:Q8LF21; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LF21; baseline and differential.
DR Genevisible; Q8LF21; AT.
DR GO; GO:0005938; C:cell cortex; IDA:TAIR.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; IMP:TAIR.
DR GO; GO:0007005; P:mitochondrion organization; IMP:TAIR.
DR GO; GO:0010152; P:pollen maturation; IMP:UniProtKB.
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 Cell cycle; Cell division; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW GTP-binding; Hydrolase; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..614
FT /note="Phragmoplastin DRP1C"
FT /id="PRO_0000206579"
FT DOMAIN 32..301
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 523..614
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 REGION 499..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 CONFLICT 23
FT /note="D -> H (in Ref. 1; AAL92170 and 2; AAF22293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 614 AA; 68723 MW; 3671AE59885A6C97 CRC64;
MATMKSLIGL INKIQRACTV LGDHGGEGMS LWEALPTVAV VGGQSSGKSS VLESVVGRDF
LPRGSGIVTR RPLVLQLHKT EDGTTEYAEF LHAPKKRFAD FAAVRKEIED ETDRITGKSK
QISNIPIQLS IYSPNVVNLT LIDLPGLTKV AVDGQPESIV QDIENMVRSY VEKPNCIILA
ISPANQDIAT SDAIKLAREV DPTGERTFGV ATKLDIMDKG TDCLDVLEGR SYRLQHPWVG
IVNRSQADIN KRVDMIAARR KEQEYFETSP EYGHLASRMG SEYLAKLLSQ HLETVIRQKI
PSIVALINKS IDEINAELDR IGRPIAVDSG AQLYTILELC RAFDRVFKEH LDGGRPGGDR
IYGVFDHQLP AALKKLPFDR HLSTKNVQKV VSEADGYQPH LIAPEQGYRR LIDGSISYFK
GPAEATVDAV HFVLKELVRK SISETEELKR FPTLASDIAA AANEALERFR DESRKTVLRL
VDMESSYLTV EFFRKLHLEP EKEKPNPRNA PAPNADPYSD NHFRKIGSNV SAYINMVCDT
LRNSLPKAVV YCQVREAKRS LLNFFYAQVG RKEKEKLGAM LDEDPQLMER RGTLAKRLEL
YKQARDDIDA VAWK
