Q9FIG9 · ARC6_ARATH

Function

function

Component of the plastid division machinery consisting in a binary fission accomplished by the simultaneous constriction of the FtsZ ring on the stromal side of the inner envelope membrane, and the ARC5 ring on the cytosolic side of the outer envelope membrane (PubMed:28248291, PubMed:29466386).
Involved in the initiation of proplastid and plastid division (including chloroplasts, statoliths and leukoplasts) (PubMed:29466386).
Promotes the assembly and/or stabilization of the plastid-dividing FtsZ ring, functioning as an antagonistic regulator of FtsZ dynamics against CDP1 and facilitating MCD1 positioning to membrane tethered FtsZ filaments to form the chloroplast Z-Ring; inhibits GDP-induced disassembly of FTSZ2 but enables ARC3 binding to FTSZ2-1 (PubMed:29138260, PubMed:29466386, PubMed:29769312, PubMed:29967285).
Relays plastid division site position between stroma and outer surface via interactions with the stromal FtsZ ring and the outer membrane PDV2 that recruits cytoplasmic ARC5 ring (PubMed:28248291).
Required for plastid equatorial positioning of PDV2 and ARC5. May contribute to gravitropism in stems and hypocotyls. Seems to influence stromule (stroma-filled tubular extensions of the plastid envelope membrane) length and frequency

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchloroplast
Cellular Componentchloroplast envelope
Cellular Componentchloroplast inner membrane
Cellular Componentplastid
Molecular Functionprotein homodimerization activity
Biological Processchloroplast fission
Biological Processchloroplast organization
Biological Processresponse to gibberellin

Names & Taxonomy

Protein names

  • Recommended name
    Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
  • Short names
    AtARC6

Gene names

    • Name
      ARC6
    • ORF names
      MDH9.18
    • Ordered locus names
      At5g42480

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Columbia
    • cv. Wassilewskija
    • cv. Wassilewskija-2
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9FIG9
  • Secondary accessions
    • Q7XAR9
    • Q7XAS0
    • Q7XAS1

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Plastid, chloroplast inner membrane
; Single-pass membrane protein
Note: Localized to a ring at the center of the chloroplasts (equatorial positioning) prior to and during constriction.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain68-618Stromal
Transmembrane619-638Helical
Topological domain639-801Chloroplast intermembrane

Keywords

Phenotypes & Variants

Disruption phenotype

Defective in proplastid and plastid division, with only one or two grossly enlarged plastids per cell, sometimes exhibiting alteration in stromule length and frequency in non-green tissues (e.g. increase in the frequency of stromules in nearly all cells) and in stomatal guard cells (GCs) (PubMed:29466386).
Heterogeneous chloroplasts sizes and shapes such as giant and mini-plastids in leaf epidermal pavement cells (PCs) (PubMed:29466386).
Abnormal subplastidial localization of the key plastid division proteins FTSZ1 and FTSZ2 (numerous short and disorganized FtsZ filament fragments) (PubMed:29967285).
Root cells statoliths, chloroplasts, and other plastids are also abnormally large. Impaired gravitropism of inflorescence stems and hypocotyls, but not of roots. Several mesophyll and stomatal guard cells contain chlorophyll-free plastids, probably missing chloroplastic DNA. Misexpression and mislocalization of ADT2 (PubMed:30252596).
The double mutant mcd1 arc6 exhibits similar chloroplast defect than the single mutant arc6, including the abnormal localization of FTSZ1 to short filaments and dots within chloroplasts (PubMed:29967285).
The double mutant arc6 cjd1 exhibits both phenotypes of single mutants cjd1 and arc6 including altered fatty acid profiles and heterogeneous chloroplasts sizes and shapes, respectively (PubMed:22028775).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis686Reduced interaction with PDV2 leading to altered chloroplast division and formation of dumbbell-shaped plastids.
Mutagenesis776Reduced interaction with PDV2 leading to altered chloroplast division and formation of dumbbell-shaped plastids.
Mutagenesis778Reduced interaction with PDV2 leading to altered chloroplast division and formation of dumbbell-shaped plastids.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 77 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-67Chloroplast
ChainPRO_000040633368-801Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic

Proteomic databases

PTM databases

Expression

Tissue specificity

Mostly expressed in young leaves.

Induction

Slightly induced by gibberellic acid (GA).

Developmental stage

Levels decrease slightly from young developing leaves to mature ones (at protein level).

Gene expression databases

Interaction

Subunit

Self-interacts (PubMed:28248291, PubMed:29769312).
Part of a complex made of ARC3, ARC6, FTSZ1 and FTSZ2 (PubMed:22823492).
Interacts with FTSZ2-1 and FTSZ2-2 (via C-terminus), but not with FTSZ1; this interaction enables ARC3 binding to FTSZ2 (PubMed:26527658, PubMed:29138260, PubMed:29769312, PubMed:29967285).
Binds to CDT1A. Interacts (via C-terminus) with PDV2 (via C-terminus) in the chloroplast intermembrane space; this interaction induces homodimerization and leads to the formation of a heterotetramer containing two ARC6 and two PDV2 subunits (PubMed:28248291).
Interacts with MCD1 in the chloroplast stroma and facilitates its subsequent binding to FtsZ2-1 (PubMed:29967285).
Interacts (via J domain) with CJD1 (via J-like domain) (PubMed:22028775).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9FIG9FTSZ1 Q425452EBI-2000800, EBI-2131124
BINARY Q9FIG9PDV2 Q9XII13EBI-2000800, EBI-2000823

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain89-153J
Region639-801Interaction with PDV2

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    801
  • Mass (Da)
    88,260
  • Last updated
    2001-03-01 v1
  • Checksum
    608E776FBA73FECF
MEALSHVGIGLSPFQLCRLPPATTKLRRSHNTSTTICSASKWADRLLSDFNFTSDSSSSSFATATTTATLVSPPPSIDRPERHVPIPIDFYQVLGAQTHFLTDGIRRAFEARVSKPPQFGFSDDALISRRQILQAACETLSNPRSRREYNEGLLDDEEATVITDVPWDKVPGALCVLQEGGETEIVLRVGEALLKERLPKSFKQDVVLVMALAFLDVSRDAMALDPPDFITGYEFVEEALKLLQEEGASSLAPDLRAQIDETLEEITPRYVLELLGLPLGDDYAAKRLNGLSGVRNILWSVGGGGASALVGGLTREKFMNEAFLRMTAAEQVDLFVATPSNIPAESFEVYEVALALVAQAFIGKKPHLLQDADKQFQQLQQAKVMAMEIPAMLYDTRNNWEIDFGLERGLCALLIGKVDECRMWLGLDSEDSQYRNPAIVEFVLENSNRDDNDDLPGLCKLLETWLAGVVFPRFRDTKDKKFKLGDYYDDPMVLSYLERVEVVQGSPLAAAAAMARIGAEHVKASAMQALQKVFPSRYTDRNSAEPKDVQETVFSVDPVGNNVGRDGEPGVFIAEAVRPSENFETNDYAIRAGVSESSVDETTVEMSVADMLKEASVKILAAGVAIGLISLFSQKYFLKSSSSFQRKDMVSSMESDVATIGSVRADDSEALPRMDARTAENIVSKWQKIKSLAFGPDHRIEMLPEVLDGRMLKIWTDRAAETAQLGLVYDYTLLKLSVDSVTVSADGTRALVEATLEESACLSDLVHPENNATDVRTYTTRYEVFWSKSGWKITEGSVLAS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1P8BCR9A0A1P8BCR9_ARATHARC6708

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict73in Ref. 1; AAQ18644/AAQ18645/AAQ18646
Sequence conflict158in Ref. 1; AAQ18646
Sequence conflict513in Ref. 1; AAQ18645/AAQ18646
Sequence conflict610in Ref. 1; AAQ18646

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY221467
EMBL· GenBank· DDBJ
AAQ18644.1
EMBL· GenBank· DDBJ
Genomic DNA
AY221468
EMBL· GenBank· DDBJ
AAQ18645.1
EMBL· GenBank· DDBJ
Genomic DNA
AY221469
EMBL· GenBank· DDBJ
AAQ18646.1
EMBL· GenBank· DDBJ
mRNA
AB016888
EMBL· GenBank· DDBJ
BAB10489.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED94815.1
EMBL· GenBank· DDBJ
Genomic DNA
AY091075
EMBL· GenBank· DDBJ
AAM13895.1
EMBL· GenBank· DDBJ
mRNA
AY150490
EMBL· GenBank· DDBJ
AAN12907.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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