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Dynamin-like protein ARC5 (EC 3.6.5.5) (Dynamin-related protein 5B) (Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 5)

 ARC5_ARATH              Reviewed;         777 AA.
Q84N64; Q3EB39; Q9LJM3;
05-APR-2011, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 2.
23-MAY-2018, entry version 101.
RecName: Full=Dynamin-like protein ARC5;
EC=3.6.5.5;
AltName: Full=Dynamin-related protein 5B;
AltName: Full=Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 5;
Name=ARC5; Synonyms=DRP5B; OrderedLocusNames=At3g19720;
ORFNames=MMB12.21;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION
PHENOTYPE, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=12642673; DOI=10.1073/pnas.0530206100;
Gao H., Kadirjan-Kalbach D., Froehlich J.E., Osteryoung K.W.;
"ARC5, a cytosolic dynamin-like protein from plants, is part of the
chloroplast division machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:4328-4333(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Landsberg erecta;
PubMed=12232072; DOI=10.1104/pp.104.1.201;
Pyke K.A., Leech R.M.;
"A genetic analysis of chloroplast division and expansion in
Arabidopsis thaliana.";
Plant Physiol. 104:201-207(1994).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Landsberg erecta;
PubMed=8819323; DOI=10.1104/pp.112.1.149;
Robertson E.J., Rutherford S.M., Leech R.M.;
"Characterization of chloroplast division using the Arabidopsis mutant
arc5.";
Plant Physiol. 112:149-159(1996).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10417716; DOI=10.1046/j.1365-313x.1999.00500.x;
Marrison J.L., Rutherford S.M., Robertson E.J., Lister C., Dean C.,
Leech R.M.;
"The distinctive roles of five different ARC genes in the chloroplast
division process in Arabidopsis.";
Plant J. 18:651-662(1999).
[7]
SUBCELLULAR LOCATION.
PubMed=16998069; DOI=10.1105/tpc.106.045484;
Miyagishima S.-Y., Froehlich J.E., Osteryoung K.W.;
"PDV1 and PDV2 mediate recruitment of the dynamin-related protein ARC5
to the plastid division site.";
Plant Cell 18:2517-2530(2006).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=18764889; DOI=10.1111/j.1751-1097.2008.00437.x;
Holzinger A., Kwok E.Y., Hanson M.R.;
"Effects of arc3, arc5 and arc6 mutations on plastid morphology and
stromule formation in green and nongreen tissues of Arabidopsis
thaliana.";
Photochem. Photobiol. 84:1324-1335(2008).
[9]
SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=18812496; DOI=10.1105/tpc.108.061440;
Glynn J.M., Froehlich J.E., Osteryoung K.W.;
"Arabidopsis ARC6 coordinates the division machineries of the inner
and outer chloroplast membranes through interaction with PDV2 in the
intermembrane space.";
Plant Cell 20:2460-2470(2008).
[10]
REVIEW.
PubMed=20491669; DOI=10.1042/BST0380817;
Aung K., Zhang X., Hu J.;
"Peroxisome division and proliferation in plants.";
Biochem. Soc. Trans. 38:817-822(2010).
[11]
FUNCTION, DISRUPTION PHENOTYPE, SELF-INTERACTION, INTERACTION WITH
FIS1A; DRP3A; DRP3B; PEX11A; PEX11B; PEX11C; PEX11D AND PEX11E, AND
SUBCELLULAR LOCATION.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=20179140; DOI=10.1105/tpc.109.071324;
Zhang X., Hu J.;
"The Arabidopsis chloroplast division protein DYNAMIN-RELATED
PROTEIN5B also mediates peroxisome division.";
Plant Cell 22:431-442(2010).
-!- FUNCTION: Probable GTPase component of both plastid and peroxisme
division machinery. Required for the last steps of plastid
division specifically in mesophyll-cell, when the narrow isthmus
breaks, facilitating the separation of the daughter plastids.
Necessary for peroxisome activities. Seems to influence stromule
(stroma-filled tubular extensions of the plastid envelope
membrane) length and frequency. {ECO:0000269|PubMed:10417716,
ECO:0000269|PubMed:12232072, ECO:0000269|PubMed:12642673,
ECO:0000269|PubMed:18764889, ECO:0000269|PubMed:20179140,
ECO:0000269|PubMed:8819323}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
-!- SUBUNIT: Forms a homodimer and heterodimers with DRP3A and DRP3B
on peroxisomes. Interacts also with FIS1A (but not FIS1B) and
PEX11 proteins (PEX11A, PEX11B, PEX11C, PEX11D and PEX11E) on
peroxisomes. {ECO:0000269|PubMed:20179140}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Plastid, chloroplast outer
membrane; Peripheral membrane protein. Peroxisome. Note=Plastid
equatorial positioning (in a discontinuous ring shape) mediated by
PDV2 in complex with ARC6 and by PDV1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q84N64-1; Sequence=Displayed;
Name=2;
IsoId=Q84N64-2; Sequence=VSP_040936;
Note=Derived from EST data. No experimental confirmation
available.;
-!- DISRUPTION PHENOTYPE: Defects in plastid constriction leading to
large and dumbbell-shaped chloroplasts in mesophyll-cell only.
Reduced number of large chloroplasts in green tissues. Mostly
normal vascular and epidermal chloroplasts and normal plastid size
in non green tissues, sometimes exhibiting alteration in stromule
length and frequency (e.g. increase in the frequency of stromules
in cells of stamen filaments). Presence of highly clustered
peroxisomes unable to complete fission and/or enlarged
peroxisomes. Impaired peroxisome-related functions, such as
photorespiration and fatty acid beta-oxidation.
{ECO:0000269|PubMed:10417716, ECO:0000269|PubMed:12232072,
ECO:0000269|PubMed:12642673, ECO:0000269|PubMed:18764889,
ECO:0000269|PubMed:20179140, ECO:0000269|PubMed:8819323}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
-!- SEQUENCE CAUTION:
Sequence=BAB02559.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AY212885; AAO89221.1; -; mRNA.
EMBL; AP000417; BAB02559.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE76279.1; -; Genomic_DNA.
EMBL; CP002686; AEE76280.1; -; Genomic_DNA.
PIR; T52402; T52402.
RefSeq; NP_188606.2; NM_112862.4. [Q84N64-1]
RefSeq; NP_850615.2; NM_180284.3. [Q84N64-2]
UniGene; At.38361; -.
ProteinModelPortal; Q84N64; -.
SMR; Q84N64; -.
BioGrid; 6842; 12.
STRING; 3702.AT3G19720.1; -.
iPTMnet; Q84N64; -.
PaxDb; Q84N64; -.
EnsemblPlants; AT3G19720.1; AT3G19720.1; AT3G19720. [Q84N64-1]
EnsemblPlants; AT3G19720.2; AT3G19720.2; AT3G19720. [Q84N64-2]
GeneID; 821509; -.
Gramene; AT3G19720.1; AT3G19720.1; AT3G19720. [Q84N64-1]
Gramene; AT3G19720.2; AT3G19720.2; AT3G19720. [Q84N64-2]
KEGG; ath:AT3G19720; -.
Araport; AT3G19720; -.
TAIR; locus:2091226; AT3G19720.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
HOGENOM; HOG000029906; -.
InParanoid; Q84N64; -.
PhylomeDB; Q84N64; -.
PRO; PR:Q84N64; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q84N64; baseline and differential.
Genevisible; Q84N64; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0010020; P:chloroplast fission; IMP:TAIR.
GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
GO; GO:0016559; P:peroxisome fission; IMP:TAIR.
CDD; cd08771; DLP_1; 1.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11566; PTHR11566; 1.
Pfam; PF00350; Dynamin_N; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
1: Evidence at protein level;
Alternative splicing; Chloroplast; Coiled coil; Complete proteome;
Cytoplasm; GTP-binding; Hydrolase; Membrane; Motor protein;
Nucleotide-binding; Peroxisome; Peroxisome biogenesis; Plastid;
Plastid outer membrane; Reference proteome.
CHAIN 1 777 Dynamin-like protein ARC5.
/FTId=PRO_0000407220.
DOMAIN 45 343 Dynamin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
NP_BIND 55 62 GTP. {ECO:0000255}.
NP_BIND 160 164 GTP. {ECO:0000255}.
NP_BIND 231 234 GTP. {ECO:0000255}.
REGION 55 62 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 81 83 G2 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 160 163 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 231 234 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 265 268 G5 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
COILED 300 320 {ECO:0000255}.
COILED 728 765 {ECO:0000255}.
VAR_SEQ 601 636 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_040936.
CONFLICT 121 121 Q -> H (in Ref. 1; AAO89221).
{ECO:0000305}.
CONFLICT 433 433 P -> Q (in Ref. 1; AAO89221).
{ECO:0000305}.
CONFLICT 747 747 I -> V (in Ref. 1; AAO89221).
{ECO:0000305}.
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


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