ARC5_ARATH
ID ARC5_ARATH Reviewed; 777 AA.
AC Q84N64; Q3EB39; Q9LJM3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Dynamin-like protein ARC5 {ECO:0000303|PubMed:12642673};
DE EC=3.6.5.5 {ECO:0000269|PubMed:32005784};
DE AltName: Full=Dynamin-related protein 5B {ECO:0000303|PubMed:20491669};
DE AltName: Full=Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 5 {ECO:0000303|PubMed:12642673};
DE Short=AtARC5 {ECO:0000303|PubMed:23020316};
GN Name=ARC5 {ECO:0000303|PubMed:12642673};
GN Synonyms=DRP5B {ECO:0000303|PubMed:20491669};
GN OrderedLocusNames=At3g19720 {ECO:0000312|Araport:AT3G19720};
GN ORFNames=MMB12.21 {ECO:0000312|EMBL:BAB02559.1};
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 1), FUNCTION, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=12642673; DOI=10.1073/pnas.0530206100;
RA Gao H., Kadirjan-Kalbach D., Froehlich J.E., Osteryoung K.W.;
RT "ARC5, a cytosolic dynamin-like protein from plants, is part of the
RT chloroplast division machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4328-4333(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12232072; DOI=10.1104/pp.104.1.201;
RA Pyke K.A., Leech R.M.;
RT "A genetic analysis of chloroplast division and expansion in Arabidopsis
RT thaliana.";
RL Plant Physiol. 104:201-207(1994).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8819323; DOI=10.1104/pp.112.1.149;
RA Robertson E.J., Rutherford S.M., Leech R.M.;
RT "Characterization of chloroplast division using the Arabidopsis mutant
RT arc5.";
RL Plant Physiol. 112:149-159(1996).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10417716; DOI=10.1046/j.1365-313x.1999.00500.x;
RA Marrison J.L., Rutherford S.M., Robertson E.J., Lister C., Dean C.,
RA Leech R.M.;
RT "The distinctive roles of five different ARC genes in the chloroplast
RT division process in Arabidopsis.";
RL Plant J. 18:651-662(1999).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=16998069; DOI=10.1105/tpc.106.045484;
RA Miyagishima S.-Y., Froehlich J.E., Osteryoung K.W.;
RT "PDV1 and PDV2 mediate recruitment of the dynamin-related protein ARC5 to
RT the plastid division site.";
RL Plant Cell 18:2517-2530(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=18764889; DOI=10.1111/j.1751-1097.2008.00437.x;
RA Holzinger A., Kwok E.Y., Hanson M.R.;
RT "Effects of arc3, arc5 and arc6 mutations on plastid morphology and
RT stromule formation in green and nongreen tissues of Arabidopsis thaliana.";
RL Photochem. Photobiol. 84:1324-1335(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=18812496; DOI=10.1105/tpc.108.061440;
RA Glynn J.M., Froehlich J.E., Osteryoung K.W.;
RT "Arabidopsis ARC6 coordinates the division machineries of the inner and
RT outer chloroplast membranes through interaction with PDV2 in the
RT intermembrane space.";
RL Plant Cell 20:2460-2470(2008).
RN [10]
RP REVIEW.
RX PubMed=20491669; DOI=10.1042/bst0380817;
RA Aung K., Zhang X., Hu J.;
RT "Peroxisome division and proliferation in plants.";
RL Biochem. Soc. Trans. 38:817-822(2010).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SELF-INTERACTION, INTERACTION WITH FIS1A;
RP DRP3A; DRP3B; PEX11A; PEX11B; PEX11C; PEX11D AND PEX11E, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=20179140; DOI=10.1105/tpc.109.071324;
RA Zhang X., Hu J.;
RT "The Arabidopsis chloroplast division protein DYNAMIN-RELATED PROTEIN5B
RT also mediates peroxisome division.";
RL Plant Cell 22:431-442(2010).
RN [12]
RP INDUCTION BY GIBBERELLIC ACID.
RX PubMed=23020316; DOI=10.1111/j.1365-313x.2012.05118.x;
RA Jiang X., Li H., Wang T., Peng C., Wang H., Wu H., Wang X.;
RT "Gibberellin indirectly promotes chloroplast biogenesis as a means to
RT maintain the chloroplast population of expanded cells.";
RL Plant J. 72:768-780(2012).
RN [13]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25736058; DOI=10.1105/tpc.115.136234;
RA Okazaki K., Miyagishima S.-Y., Wada H.;
RT "Phosphatidylinositol 4-phosphate negatively regulates chloroplast division
RT in Arabidopsis.";
RL Plant Cell 27:663-674(2015).
RN [14]
RP ACTIVITY REGULATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=27988788; DOI=10.1007/s00299-016-2096-6;
RA Chang N., Sun Q., Li Y., Mu Y., Hu J., Feng Y., Liu X., Gao H.;
RT "PDV2 has a dosage effect on chloroplast division in Arabidopsis.";
RL Plant Cell Rep. 36:471-480(2017).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=29466386; DOI=10.1371/journal.pone.0192380;
RA Fujiwara M.T., Yasuzawa M., Kojo K.H., Niwa Y., Abe T., Yoshida S.,
RA Nakano T., Itoh R.D.;
RT "The Arabidopsis arc5 and arc6 mutations differentially affect plastid
RT morphology in pavement and guard cells in the leaf epidermis.";
RL PLoS ONE 13:e0192380-e0192380(2018).
RN [16]
RP FUNCTION, MUTAGENESIS OF LYS-61 AND THR-82, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, PTM, ACTIVITY REGULATION, AND INTERACTION
RP WITH PDV1 AND PDV2.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=32005784; DOI=10.1104/pp.19.01490;
RA Sun B., Zhang Q.-Y., Yuan H., Gao W., Han B., Zhang M.;
RT "PDV1 and PDV2 differentially affect remodeling and assembly of the
RT chloroplast DRP5B ring.";
RL Plant Physiol. 182:1966-1978(2020).
CC -!- FUNCTION: Mechanochemical GTPase component of both plastid and
CC peroxisome division machinery (PubMed:32005784). Required for the last
CC steps of plastid division specifically in mesophyll-cell, when the
CC narrow isthmus breaks, facilitating the separation of the daughter
CC plastids (PubMed:29466386). Necessary for peroxisome activities. Seems
CC to influence stromule (stroma-filled tubular extensions of the plastid
CC envelope membrane) length and frequency (PubMed:29466386).
CC {ECO:0000269|PubMed:10417716, ECO:0000269|PubMed:12232072,
CC ECO:0000269|PubMed:12642673, ECO:0000269|PubMed:18764889,
CC ECO:0000269|PubMed:20179140, ECO:0000269|PubMed:29466386,
CC ECO:0000269|PubMed:32005784, ECO:0000269|PubMed:8819323}.
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:0000269|PubMed:32005784};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19671;
CC Evidence={ECO:0000269|PubMed:32005784};
CC -!- ACTIVITY REGULATION: GTPase activity is repressed by PDV2 thus
CC increasing stability at the plastid outer envelope membranes (OEMs)
CC periphery. {ECO:0000269|PubMed:27988788, ECO:0000269|PubMed:32005784}.
CC -!- SUBUNIT: Forms a homodimer and heterodimers with DRP3A and DRP3B on
CC peroxisomes. Interacts also with FIS1A (but not FIS1B) and PEX11
CC proteins (PEX11A, PEX11B, PEX11C, PEX11D and PEX11E) on peroxisomes.
CC Interacts with PDV1 and PDV2 (PubMed:32005784).
CC {ECO:0000269|PubMed:20179140, ECO:0000269|PubMed:32005784}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32005784}. Plastid,
CC chloroplast outer membrane {ECO:0000269|PubMed:25736058,
CC ECO:0000269|PubMed:32005784}; Peripheral membrane protein
CC {ECO:0000269|PubMed:32005784}. Peroxisome
CC {ECO:0000269|PubMed:20179140}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:32005784}. Note=Plastid equatorial positioning (in
CC a discontinuous ring shape) mediated by PDV2 in complex with ARC6 and
CC dissociation from the outer envelope membranes (OEMs) is triggered by
CC PDV1; this localization with OEMs is repressed by phosphatidylinositol
CC 4-phosphate (PI4P) (PubMed:32005784, PubMed:25736058). Dynamic subunit
CC exchange within chloroplastic DRP5B rings with a cytosolic pool during
CC chloroplast membrane constriction in a GTPase activity-dependent manner
CC (PubMed:32005784). {ECO:0000269|PubMed:25736058,
CC ECO:0000269|PubMed:32005784}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84N64-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84N64-2; Sequence=VSP_040936;
CC -!- INDUCTION: Induced by gibberellic acid (GA).
CC {ECO:0000269|PubMed:23020316}.
CC -!- PTM: Stabilized at the plastid outer envelope membranes (OEMs) in the
CC constriction site when in complex with GTP, but destabilized after
CC conversion of GTP into GDP leading to turnover with a cytosolic pool.
CC {ECO:0000269|PubMed:32005784}.
CC -!- DISRUPTION PHENOTYPE: Defects in plastid constriction leading to large
CC and dumbbell-shaped chloroplasts in mesophyll-cell only
CC (PubMed:29466386, PubMed:32005784). Sligthly larger division-competent
CC chloroplasts in leaf epidermal pavement cells (PCs) with normal shapes
CC (PubMed:29466386). A few stomatal guard cells (GCs) are missing
CC chlorophyll-bearing plastids (chloroplasts) while accumulating minute
CC chlorophyll-less plastids (PubMed:29466386). Reduced number of large
CC chloroplasts in green tissues. Mostly normal vascular and epidermal
CC chloroplasts and normal plastid size in non green tissues, sometimes
CC exhibiting alteration in stromule length and frequency (e.g. increase
CC in the frequency of stromules in cells of stamen filaments). Presence
CC of highly clustered peroxisomes unable to complete fission and/or
CC enlarged peroxisomes. Impaired peroxisome-related functions, such as
CC photorespiration and fatty acid beta-oxidation.
CC {ECO:0000269|PubMed:10417716, ECO:0000269|PubMed:12232072,
CC ECO:0000269|PubMed:12642673, ECO:0000269|PubMed:18764889,
CC ECO:0000269|PubMed:20179140, ECO:0000269|PubMed:29466386,
CC ECO:0000269|PubMed:32005784, ECO:0000269|PubMed:8819323}.
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=BAB02559.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY212885; AAO89221.1; -; mRNA.
DR EMBL; AP000417; BAB02559.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76279.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76280.1; -; Genomic_DNA.
DR PIR; T52402; T52402.
DR RefSeq; NP_188606.2; NM_112862.4. [Q84N64-1]
DR RefSeq; NP_850615.2; NM_180284.3. [Q84N64-2]
DR AlphaFoldDB; Q84N64; -.
DR BioGRID; 6842; 12.
DR STRING; 3702.AT3G19720.1; -.
DR iPTMnet; Q84N64; -.
DR PaxDb; Q84N64; -.
DR PRIDE; Q84N64; -.
DR ProteomicsDB; 244427; -. [Q84N64-1]
DR EnsemblPlants; AT3G19720.1; AT3G19720.1; AT3G19720. [Q84N64-1]
DR EnsemblPlants; AT3G19720.2; AT3G19720.2; AT3G19720. [Q84N64-2]
DR GeneID; 821509; -.
DR Gramene; AT3G19720.1; AT3G19720.1; AT3G19720. [Q84N64-1]
DR Gramene; AT3G19720.2; AT3G19720.2; AT3G19720. [Q84N64-2]
DR KEGG; ath:AT3G19720; -.
DR Araport; AT3G19720; -.
DR TAIR; locus:2091226; AT3G19720.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; Q84N64; -.
DR OMA; PIAINMK; -.
DR PhylomeDB; Q84N64; -.
DR PRO; PR:Q84N64; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84N64; baseline and differential.
DR Genevisible; Q84N64; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0035452; C:extrinsic component of plastid membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR GO; GO:0016559; P:peroxisome fission; IMP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IEP: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; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Coiled coil; Cytoplasm; GTP-binding;
KW Hydrolase; Membrane; Motor protein; Nucleotide-binding; Peroxisome;
KW Peroxisome biogenesis; Plastid; Plastid outer membrane; Reference proteome.
FT CHAIN 1..777
FT /note="Dynamin-like protein ARC5"
FT /id="PRO_0000407220"
FT DOMAIN 45..343
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 55..62
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 81..83
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 160..163
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 231..234
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 265..268
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 300..320
FT /evidence="ECO:0000255"
FT COILED 728..765
FT /evidence="ECO:0000255"
FT BINDING 55..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 160..164
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 231..234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 601..636
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040936"
FT MUTAGEN 61
FT /note="K->A: Reduced GTPase activity but normal
FT localization at the constriction site of dividing
FT chloroplasts; however, reduced turnover between cytosolic
FT and chloroplastic pools."
FT /evidence="ECO:0000269|PubMed:32005784"
FT MUTAGEN 82
FT /note="T->D: Reduced GTPase activity but normal
FT localization at the constriction site of dividing
FT chloroplasts; however, reduced turnover between cytosolic
FT and chloroplastic pools."
FT /evidence="ECO:0000269|PubMed:32005784"
FT CONFLICT 121
FT /note="Q -> H (in Ref. 1; AAO89221)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="P -> Q (in Ref. 1; AAO89221)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="I -> V (in Ref. 1; AAO89221)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 87171 MW; 8C5CBF0852EA7B8A CRC64;
MAEVSAKSVT VEEMAEEDDA AIEERWSLYE AYNELHALAQ ELETPFEAPA VLVVGQQTDG
KSALVEALMG FQFNHVGGGT KTRRPITLHM KYDPQCQFPL CHLGSDDDPS VSLPKSLSQI
QAYIEAENMR LEQEPCSPFS AKEIIVKVQY KYCPNLTIID TPGLIAPAPG LKNRALQVQA
RAVEALVRAK MQHKEFIILC LEDSSDWSIA TTRRIVMQVD PELSRTIVVS TKLDTKIPQF
SCSSDVEVFL SPPASALDSS LLGDSPFFTS VPSGRVGYGQ DSVYKSNDEF KQAVSLREME
DIASLEKKLG RLLTKQEKSR IGISKLRLFL EELLWKRYKE SVPLIIPLLG KEYRSTVRKL
DTVSKELSSL DEAKLKERGR TFHDLFLTKL SLLLKGTVVA PPDKFGETLQ DERTQGGAFV
GTDGLQFSHK LIPNAGMRLY GGAQYHRAMA EFRFLVGAIK CPPITREEIV NACGVEDIHD
GTNYSRTACV IAVAKARETF EPFLHQLGAR LLHILKRLLP ISVYLLQKEG EYLSGHEVFL
KRVASAFNSF VESTEKSCRD KCMEDLASTT RYVTWSLHNK NRAGLRQFLD SFGGTEHNTT
SGNAIGFSLP QDALGGTTDT KSRSDVKLSH LASNIDSGSS IQTTEMRLAD LLDSTLWNRK
LAPSSERIVY ALVQQIFQGI REYFLASAEL KFNCFLLMPI VDKLPALLRE ELENAFEDDL
DSIFDITNLR QSLDQKKRST EIELRRIKRI KEKFRVMNEK LNSHEFAQNL KAPSVQH
