ARC6_ARATH
ID ARC6_ARATH Reviewed; 801 AA.
AC Q9FIG9; Q7XAR9; Q7XAS0; Q7XAS1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic {ECO:0000303|PubMed:12897262};
DE Short=AtARC6 {ECO:0000303|PubMed:23020316};
DE Flags: Precursor;
GN Name=ARC6 {ECO:0000303|PubMed:12897262};
GN OrderedLocusNames=At5g42480 {ECO:0000312|Araport:AT5G42480};
GN ORFNames=MDH9.18 {ECO:0000312|EMBL:BAB10489.1};
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 [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=cv. Columbia, cv. Wassilewskija, and cv. Wassilewskija-2;
RX PubMed=12897262; DOI=10.1105/tpc.013292;
RA Vitha S., Froehlich J.E., Koksharova O., Pyke K.A., van Erp H.,
RA Osteryoung K.W.;
RT "ARC6 is a J-domain plastid division protein and an evolutionary descendant
RT of the cyanobacterial cell division protein Ftn2.";
RL Plant Cell 15:1918-1933(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12232400; DOI=10.1104/pp.106.3.1169;
RA Pyke K.A., Rutherford S.M., Robertson E.J., Leech R.M.;
RT "arc6, a fertile Arabidopsis mutant with only two mesophyll cell
RT chloroplasts.";
RL Plant Physiol. 106:1169-1177(1994).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=8537433; DOI=10.1242/jcs.108.9.2937;
RA Robertson E.J., Pyke K.A., Leech R.M.;
RT "arc6, an extreme chloroplast division mutant of Arabidopsis also alters
RT proplastid proliferation and morphology in shoot and root apices.";
RL J. Cell Sci. 108:2937-2944(1995).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9489024; DOI=10.1104/pp.116.2.797;
RA Pyke K.A., Page A.M.;
RT "Plastid ontogeny during petal development in Arabidopsis.";
RL Plant Physiol. 116:797-803(1998).
RN [8]
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 [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11975738; DOI=10.1034/j.1399-3054.2002.1140417.x;
RA Yamamoto K., Pyke K.A., Kiss J.Z.;
RT "Reduced gravitropism in inflorescence stems and hypocotyls, but not roots,
RT of Arabidopsis mutants with large plastids.";
RL Physiol. Plantarum 114:627-636(2002).
RN [10]
RP INTERACTION WITH FTSZ2-1, AND SELF-INTERACTION.
RX PubMed=16146521; DOI=10.1111/j.1365-313x.2005.02493.x;
RA Maple J., Aldridge C., Moeller S.G.;
RT "Plastid division is mediated by combinatorial assembly of plastid division
RT proteins.";
RL Plant J. 43:811-823(2005).
RN [11]
RP INTERACTION WITH CDT1A, AND SUBCELLULAR LOCATION.
RX PubMed=15928083; DOI=10.1073/pnas.0502564102;
RA Raynaud C., Perennes C., Reuzeau C., Catrice O., Brown S., Bergounioux C.;
RT "Cell and plastid division are coordinated through the prereplication
RT factor AtCDT1.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8216-8221(2005).
RN [12]
RP SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=18284374; DOI=10.1042/bj20071354;
RA McAndrew R.S., Olson B.J., Kadirjan-Kalbach D.K., Chi-Ham C.L., Vitha S.,
RA Froehlich J.E., Osteryoung K.W.;
RT "In vivo quantitative relationship between plastid division proteins FtsZ1
RT and FtsZ2 and identification of ARC6 and ARC3 in a native FtsZ complex.";
RL Biochem. J. 412:367-378(2008).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
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 [14]
RP FUNCTION, INTERACTION WITH PDV2, SUBCELLULAR LOCATION, AND TOPOLOGY.
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 [15]
RP INTERACTION WITH FTSZ2-1 AND FTSZ2-2.
RX PubMed=19995726; DOI=10.1093/mp/ssp077;
RA Schmitz A.J., Glynn J.M., Olson B.J.S.C., Stokes K.D., Osteryoung K.W.;
RT "Arabidopsis FtsZ2-1 and FtsZ2-2 are functionally redundant, but FtsZ-based
RT plastid division is not essential for chloroplast partitioning or plant
RT growth and development.";
RL Mol. Plant 2:1211-1222(2009).
RN [16]
RP DISRUPTION PHENOTYPE.
RX PubMed=19318374; DOI=10.1093/pcp/pcp047;
RA Chen Y., Asano T., Fujiwara M.T., Yoshida S., Machida Y., Yoshioka Y.;
RT "Plant cells without detectable plastids are generated in the crumpled leaf
RT mutant of Arabidopsis thaliana.";
RL Plant Cell Physiol. 50:956-969(2009).
RN [17]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CJD1.
RC STRAIN=cv. Columbia;
RX PubMed=22028775; DOI=10.1371/journal.pone.0025368;
RA Ajjawi I., Coku A., Froehlich J.E., Yang Y., Osteryoung K.W., Benning C.,
RA Last R.L.;
RT "A J-like protein influences fatty acid composition of chloroplast lipids
RT in Arabidopsis.";
RL PLoS ONE 6:e25368-e25368(2011).
RN [18]
RP INTERACTION WITH FTSZ1-1; FTSZ2-1 AND FTSZ2-2.
RX PubMed=22823492; DOI=10.1042/bj20120404;
RA Gargano D., Maple-Groedem J., Moeller S.G.;
RT "In vivo phosphorylation of FtsZ2 in Arabidopsis thaliana.";
RL Biochem. J. 446:517-521(2012).
RN [19]
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 [20]
RP INTERACTION WITH FTSZ2-1.
RC STRAIN=cv. Columbia;
RX PubMed=26527658; DOI=10.1104/pp.15.01460;
RA Zhang M., Chen C., Froehlich J.E., TerBush A.D., Osteryoung K.W.;
RT "Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division
RT Complex and Negative Regulation of FtsZ Assembly.";
RL Plant Physiol. 170:250-262(2016).
RN [21]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [22]
RP SUBUNIT, INTERACTION WITH ARC3 AND FTSZ2-1, AND FUNCTION.
RX PubMed=29138260; DOI=10.1042/bcj20170697;
RA Shaik R.S., Sung M.W., Vitha S., Holzenburg A.;
RT "Chloroplast division protein ARC3 acts on FtsZ2 by preventing filament
RT bundling and enhancing GTPase activity.";
RL Biochem. J. 475:99-115(2018).
RN [23]
RP FUNCTION, HOMODIMER, AND INTERACTION WITH FTSZ2-1.
RX PubMed=29769312; DOI=10.1074/jbc.ra117.000999;
RA Sung M.W., Shaik R., TerBush A.D., Osteryoung K.W., Vitha S.,
RA Holzenburg A.;
RT "The chloroplast division protein ARC6 acts to inhibit disassembly of GDP-
RT bound FtsZ2.";
RL J. Biol. Chem. 293:10692-10706(2018).
RN [24]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH MCD1 AND FTSZ2-1.
RC STRAIN=cv. Columbia;
RX PubMed=29967285; DOI=10.1105/tpc.18.00189;
RA Chen L., Sun B., Gao W., Zhang Q.Y., Yuan H., Zhang M.;
RT "MCD1 associates with FtsZ filaments via the membrane-tethering protein
RT ARC6 to guide chloroplast division.";
RL Plant Cell 30:1807-1823(2018).
RN [25]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=30252596; DOI=10.1080/15592324.2018.1517075;
RA Abolhassani Rad S., Clayton E.J., Cornelius E.J., Howes T.R., Kohalmi S.E.;
RT "Moonlighting proteins: putting the spotlight on enzymes.";
RL Plant Signal. Behav. 13:e1517075-e1517075(2018).
RN [26]
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 [27]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 636-801.
RX PubMed=26452626; DOI=10.1002/pro.2825;
RA Kumar N., Radhakrishnan A., Su C.-C., Osteryoung K.W., Yu E.W.;
RT "Crystal structure of a conserved domain in the intermembrane space region
RT of the plastid division protein ARC6.";
RL Protein Sci. 25:523-529(2016).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 646-801 IN COMPLEX WITH PDV2,
RP FUNCTION, DIMERIZATION, INTERACTION WITH PDV2, MUTAGENESIS OF TRP-686;
RP ARG-776 AND TYR-778, AND SUBCELLULAR LOCATION.
RX PubMed=28248291; DOI=10.1038/nplants.2017.11;
RA Wang W., Li J., Sun Q., Yu X., Zhang W., Jia N., An C., Li Y., Dong Y.,
RA Han F., Chang N., Liu X., Zhu Z., Yu Y., Fan S., Yang M., Luo S.-Z.,
RA Gao H., Feng Y.;
RT "Structural insights into the coordination of plastid division by the ARC6-
RT PDV2 complex.";
RL Nat. Plants 3:17011-17011(2017).
CC -!- FUNCTION: Component of the plastid division machinery consisting in a
CC binary fission accomplished by the simultaneous constriction of the
CC FtsZ ring on the stromal side of the inner envelope membrane, and the
CC ARC5 ring on the cytosolic side of the outer envelope membrane
CC (PubMed:28248291, PubMed:29466386). Involved in the initiation of
CC proplastid and plastid division (including chloroplasts, statoliths and
CC leukoplasts) (PubMed:29466386). Promotes the assembly and/or
CC stabilization of the plastid-dividing FtsZ ring, functioning as an
CC antagonistic regulator of FtsZ dynamics against CDP1 and facilitating
CC MCD1 positioning to membrane tethered FtsZ filaments to form the
CC chloroplast Z-Ring; inhibits GDP-induced disassembly of FTSZ2 but
CC enables ARC3 binding to FTSZ2-1 (PubMed:29466386, PubMed:29967285,
CC PubMed:29769312, PubMed:29138260). Relays plastid division site
CC position between stroma and outer surface via interactions with the
CC stromal FtsZ ring and the outer membrane PDV2 that recruits cytoplasmic
CC ARC5 ring (PubMed:28248291). Required for plastid equatorial
CC positioning of PDV2 and ARC5. May contribute to gravitropism in stems
CC and hypocotyls. Seems to influence stromule (stroma-filled tubular
CC extensions of the plastid envelope membrane) length and frequency.
CC {ECO:0000269|PubMed:10417716, ECO:0000269|PubMed:11975738,
CC ECO:0000269|PubMed:12232400, ECO:0000269|PubMed:12897262,
CC ECO:0000269|PubMed:18764889, ECO:0000269|PubMed:18812496,
CC ECO:0000269|PubMed:28248291, ECO:0000269|PubMed:29138260,
CC ECO:0000269|PubMed:29466386, ECO:0000269|PubMed:29769312,
CC ECO:0000269|PubMed:29967285, ECO:0000269|PubMed:8537433,
CC ECO:0000269|PubMed:9489024}.
CC -!- SUBUNIT: Self-interacts (PubMed:28248291, PubMed:29769312). Part of a
CC complex made of ARC3, ARC6, FTSZ1 and FTSZ2 (PubMed:22823492).
CC Interacts with FTSZ2-1 and FTSZ2-2 (via C-terminus), but not with
CC FTSZ1; this interaction enables ARC3 binding to FTSZ2 (PubMed:29967285,
CC PubMed:29769312, PubMed:29138260, PubMed:26527658). Binds to CDT1A.
CC Interacts (via C-terminus) with PDV2 (via C-terminus) in the
CC chloroplast intermembrane space; this interaction induces
CC homodimerization and leads to the formation of an heterotetramer
CC containing two ARC6 and two PDV2 subunits (PubMed:28248291). Interacts
CC with MCD1 in the chloroplast stroma and facilitates its subsequent
CC binding to FtsZ2-1 (PubMed:29967285). Interacts (via J domain) with
CC CJD1 (via J-like domain) (PubMed:22028775).
CC {ECO:0000269|PubMed:15928083, ECO:0000269|PubMed:16146521,
CC ECO:0000269|PubMed:18284374, ECO:0000269|PubMed:18812496,
CC ECO:0000269|PubMed:19995726, ECO:0000269|PubMed:22028775,
CC ECO:0000269|PubMed:22823492, ECO:0000269|PubMed:26527658,
CC ECO:0000269|PubMed:28248291, ECO:0000269|PubMed:29138260,
CC ECO:0000269|PubMed:29769312, ECO:0000269|PubMed:29967285}.
CC -!- INTERACTION:
CC Q9FIG9; Q42545: FTSZ1; NbExp=2; IntAct=EBI-2000800, EBI-2131124;
CC Q9FIG9; Q9XII1: PDV2; NbExp=3; IntAct=EBI-2000800, EBI-2000823;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:12897262, ECO:0000269|PubMed:15928083,
CC ECO:0000269|PubMed:18812496}; Single-pass membrane protein
CC {ECO:0000269|PubMed:12897262, ECO:0000269|PubMed:15928083,
CC ECO:0000269|PubMed:18812496}. Note=Localized to a ring at the center of
CC the chloroplasts (equatorial positioning) prior to and during
CC constriction. {ECO:0000269|PubMed:18812496,
CC ECO:0000269|PubMed:28248291}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in young leaves.
CC {ECO:0000269|PubMed:27988788}.
CC -!- DEVELOPMENTAL STAGE: Levels decrease slightly from young developing
CC leaves to mature ones (at protein level).
CC {ECO:0000269|PubMed:27988788}.
CC -!- INDUCTION: Slightly induced by gibberellic acid (GA).
CC {ECO:0000269|PubMed:23020316}.
CC -!- DISRUPTION PHENOTYPE: Defective in proplastid and plastid division,
CC with only one or two grossly enlarged plastids per cell, sometimes
CC exhibiting alteration in stromule length and frequency in non-green
CC tissues (e.g. increase in the frequency of stromules in nearly all
CC cells) and in stomatal guard cells (GCs) (PubMed:29466386).
CC Heterogeneous chloroplasts sizes and shapes such as giant and mini-
CC plastids in leaf epidermal pavement cells (PCs) (PubMed:29466386).
CC Abnormal subplastidial localization of the key plastid division
CC proteins FTSZ1 and FTSZ2 (numerous short and disorganized FtsZ filament
CC fragments) (PubMed:29967285). Root cells statoliths, chloroplasts, and
CC other plastids are also abnormally large. Impaired gravitropism of
CC inflorescence stems and hypocotyls, but not of roots. Several mesophyll
CC and stomatal guard cells contain chlorophyll-free plastids, probably
CC missing chloroplastic DNA. Misexpression and mislocalization of ADT2
CC (PubMed:30252596). The double mutant mcd1 arc6 exhibits similar
CC chloroplast defect than the single mutant arc6, including the abnormal
CC localization of FTSZ1 to short filaments and dots within chloroplasts
CC (PubMed:29967285). The double mutant arc6 cjd1 exhibits both phenotypes
CC of single mutants cjd1 and arc6 including altered fatty acid profiles
CC and heterogeneous chloroplasts sizes and shapes, respectively
CC (PubMed:22028775). {ECO:0000269|PubMed:10417716,
CC ECO:0000269|PubMed:11975738, ECO:0000269|PubMed:12232400,
CC ECO:0000269|PubMed:12897262, ECO:0000269|PubMed:18764889,
CC ECO:0000269|PubMed:19318374, ECO:0000269|PubMed:22028775,
CC ECO:0000269|PubMed:29466386, ECO:0000269|PubMed:29967285,
CC ECO:0000269|PubMed:30252596, ECO:0000269|PubMed:8537433,
CC ECO:0000269|PubMed:9489024}.
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DR EMBL; AY221467; AAQ18644.1; -; Genomic_DNA.
DR EMBL; AY221468; AAQ18645.1; -; Genomic_DNA.
DR EMBL; AY221469; AAQ18646.1; -; mRNA.
DR EMBL; AB016888; BAB10489.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94815.1; -; Genomic_DNA.
DR EMBL; AY091075; AAM13895.1; -; mRNA.
DR EMBL; AY150490; AAN12907.1; -; mRNA.
DR RefSeq; NP_199063.1; NM_123613.4.
DR PDB; 5D9R; X-ray; 2.05 A; A=636-801.
DR PDB; 5GTB; X-ray; 2.87 A; A=646-801.
DR PDB; 5HAD; X-ray; 2.24 A; A=646-801.
DR PDBsum; 5D9R; -.
DR PDBsum; 5GTB; -.
DR PDBsum; 5HAD; -.
DR AlphaFoldDB; Q9FIG9; -.
DR SMR; Q9FIG9; -.
DR BioGRID; 19505; 4.
DR IntAct; Q9FIG9; 5.
DR STRING; 3702.AT5G42480.1; -.
DR iPTMnet; Q9FIG9; -.
DR PaxDb; Q9FIG9; -.
DR PRIDE; Q9FIG9; -.
DR ProteomicsDB; 240611; -.
DR EnsemblPlants; AT5G42480.1; AT5G42480.1; AT5G42480.
DR GeneID; 834255; -.
DR Gramene; AT5G42480.1; AT5G42480.1; AT5G42480.
DR KEGG; ath:AT5G42480; -.
DR Araport; AT5G42480; -.
DR TAIR; locus:2162341; AT5G42480.
DR eggNOG; ENOG502QQSA; Eukaryota.
DR HOGENOM; CLU_013174_0_0_1; -.
DR InParanoid; Q9FIG9; -.
DR OMA; WLQTEVF; -.
DR OrthoDB; 253756at2759; -.
DR PhylomeDB; Q9FIG9; -.
DR PRO; PR:Q9FIG9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIG9; baseline and differential.
DR Genevisible; Q9FIG9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:UniProtKB.
DR GO; GO:0031357; C:integral component of chloroplast inner membrane; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
DR InterPro; IPR044685; ARC6-like.
DR InterPro; IPR025344; ARC6-like_IMS.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR33925; PTHR33925; 1.
DR Pfam; PF13355; ARC6-like_IMS; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Membrane; Plastid; Plastid inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..801
FT /note="Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS
FT 6, chloroplastic"
FT /id="PRO_0000406333"
FT TOPO_DOM 68..618
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..801
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 89..153
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 639..801
FT /note="Interaction with PDV2"
FT /evidence="ECO:0000269|PubMed:18812496,
FT ECO:0000269|PubMed:28248291, ECO:0007744|PDB:5GTB"
FT MUTAGEN 686
FT /note="W->A: Reduced interaction with PDV2 leading to
FT altered chloroplast division and formation of dumbbell-
FT shaped plastids."
FT /evidence="ECO:0000269|PubMed:28248291"
FT MUTAGEN 776
FT /note="R->A,D: Reduced interaction with PDV2 leading to
FT altered chloroplast division and formation of dumbbell-
FT shaped plastids."
FT /evidence="ECO:0000269|PubMed:28248291"
FT MUTAGEN 778
FT /note="Y->A: Reduced interaction with PDV2 leading to
FT altered chloroplast division and formation of dumbbell-
FT shaped plastids."
FT /evidence="ECO:0000269|PubMed:28248291"
FT CONFLICT 73
FT /note="P -> L (in Ref. 1; AAQ18644/AAQ18645/AAQ18646)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="E -> G (in Ref. 1; AAQ18646)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="A -> T (in Ref. 1; AAQ18645/AAQ18646)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="D -> E (in Ref. 1; AAQ18646)"
FT /evidence="ECO:0000305"
FT HELIX 676..694
FT /evidence="ECO:0007829|PDB:5D9R"
FT HELIX 700..705
FT /evidence="ECO:0007829|PDB:5D9R"
FT HELIX 709..725
FT /evidence="ECO:0007829|PDB:5D9R"
FT STRAND 727..743
FT /evidence="ECO:0007829|PDB:5D9R"
FT STRAND 747..766
FT /evidence="ECO:0007829|PDB:5D9R"
FT HELIX 768..770
FT /evidence="ECO:0007829|PDB:5D9R"
FT STRAND 772..787
FT /evidence="ECO:0007829|PDB:5D9R"
FT STRAND 790..798
FT /evidence="ECO:0007829|PDB:5D9R"
SQ SEQUENCE 801 AA; 88260 MW; 608E776FBA73FECF CRC64;
MEALSHVGIG LSPFQLCRLP PATTKLRRSH NTSTTICSAS KWADRLLSDF NFTSDSSSSS
FATATTTATL VSPPPSIDRP ERHVPIPIDF YQVLGAQTHF LTDGIRRAFE ARVSKPPQFG
FSDDALISRR QILQAACETL SNPRSRREYN EGLLDDEEAT VITDVPWDKV PGALCVLQEG
GETEIVLRVG EALLKERLPK SFKQDVVLVM ALAFLDVSRD AMALDPPDFI TGYEFVEEAL
KLLQEEGASS LAPDLRAQID ETLEEITPRY VLELLGLPLG DDYAAKRLNG LSGVRNILWS
VGGGGASALV GGLTREKFMN EAFLRMTAAE QVDLFVATPS NIPAESFEVY EVALALVAQA
FIGKKPHLLQ DADKQFQQLQ QAKVMAMEIP AMLYDTRNNW EIDFGLERGL CALLIGKVDE
CRMWLGLDSE DSQYRNPAIV EFVLENSNRD DNDDLPGLCK LLETWLAGVV FPRFRDTKDK
KFKLGDYYDD PMVLSYLERV EVVQGSPLAA AAAMARIGAE HVKASAMQAL QKVFPSRYTD
RNSAEPKDVQ ETVFSVDPVG NNVGRDGEPG VFIAEAVRPS ENFETNDYAI RAGVSESSVD
ETTVEMSVAD MLKEASVKIL AAGVAIGLIS LFSQKYFLKS SSSFQRKDMV SSMESDVATI
GSVRADDSEA LPRMDARTAE NIVSKWQKIK SLAFGPDHRI EMLPEVLDGR MLKIWTDRAA
ETAQLGLVYD YTLLKLSVDS VTVSADGTRA LVEATLEESA CLSDLVHPEN NATDVRTYTT
RYEVFWSKSG WKITEGSVLA S
