Q9FIG9 · ARC6_ARATH
- ProteinProtein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- GeneARC6
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids801 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
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 annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast envelope | |
Cellular Component | chloroplast inner membrane | |
Cellular Component | plastid | |
Molecular Function | protein homodimerization activity | |
Biological Process | chloroplast fission | |
Biological Process | chloroplast organization | |
Biological Process | response to gibberellin |
Names & Taxonomy
Protein names
- Recommended nameProtein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic
- Short namesAtARC6
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9FIG9
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 68-618 | Stromal | ||||
Sequence: ATLVSPPPSIDRPERHVPIPIDFYQVLGAQTHFLTDGIRRAFEARVSKPPQFGFSDDALISRRQILQAACETLSNPRSRREYNEGLLDDEEATVITDVPWDKVPGALCVLQEGGETEIVLRVGEALLKERLPKSFKQDVVLVMALAFLDVSRDAMALDPPDFITGYEFVEEALKLLQEEGASSLAPDLRAQIDETLEEITPRYVLELLGLPLGDDYAAKRLNGLSGVRNILWSVGGGGASALVGGLTREKFMNEAFLRMTAAEQVDLFVATPSNIPAESFEVYEVALALVAQAFIGKKPHLLQDADKQFQQLQQAKVMAMEIPAMLYDTRNNWEIDFGLERGLCALLIGKVDECRMWLGLDSEDSQYRNPAIVEFVLENSNRDDNDDLPGLCKLLETWLAGVVFPRFRDTKDKKFKLGDYYDDPMVLSYLERVEVVQGSPLAAAAAMARIGAEHVKASAMQALQKVFPSRYTDRNSAEPKDVQETVFSVDPVGNNVGRDGEPGVFIAEAVRPSENFETNDYAIRAGVSESSVDETTVEMSVADMLKEASVK | ||||||
Transmembrane | 619-638 | Helical | ||||
Sequence: ILAAGVAIGLISLFSQKYFL | ||||||
Topological domain | 639-801 | Chloroplast intermembrane | ||||
Sequence: KSSSSFQRKDMVSSMESDVATIGSVRADDSEALPRMDARTAENIVSKWQKIKSLAFGPDHRIEMLPEVLDGRMLKIWTDRAAETAQLGLVYDYTLLKLSVDSVTVSADGTRALVEATLEESACLSDLVHPENNATDVRTYTTRYEVFWSKSGWKITEGSVLAS |
Keywords
- Cellular component
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 686 | Reduced interaction with PDV2 leading to altered chloroplast division and formation of dumbbell-shaped plastids. | ||||
Sequence: W → A | ||||||
Mutagenesis | 776 | Reduced interaction with PDV2 leading to altered chloroplast division and formation of dumbbell-shaped plastids. | ||||
Sequence: R → A or D | ||||||
Mutagenesis | 778 | Reduced interaction with PDV2 leading to altered chloroplast division and formation of dumbbell-shaped plastids. | ||||
Sequence: Y → A |
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.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-67 | Chloroplast | ||||
Sequence: MEALSHVGIGLSPFQLCRLPPATTKLRRSHNTSTTICSASKWADRLLSDFNFTSDSSSSSFATATTT | ||||||
Chain | PRO_0000406333 | 68-801 | Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic | |||
Sequence: ATLVSPPPSIDRPERHVPIPIDFYQVLGAQTHFLTDGIRRAFEARVSKPPQFGFSDDALISRRQILQAACETLSNPRSRREYNEGLLDDEEATVITDVPWDKVPGALCVLQEGGETEIVLRVGEALLKERLPKSFKQDVVLVMALAFLDVSRDAMALDPPDFITGYEFVEEALKLLQEEGASSLAPDLRAQIDETLEEITPRYVLELLGLPLGDDYAAKRLNGLSGVRNILWSVGGGGASALVGGLTREKFMNEAFLRMTAAEQVDLFVATPSNIPAESFEVYEVALALVAQAFIGKKPHLLQDADKQFQQLQQAKVMAMEIPAMLYDTRNNWEIDFGLERGLCALLIGKVDECRMWLGLDSEDSQYRNPAIVEFVLENSNRDDNDDLPGLCKLLETWLAGVVFPRFRDTKDKKFKLGDYYDDPMVLSYLERVEVVQGSPLAAAAAMARIGAEHVKASAMQALQKVFPSRYTDRNSAEPKDVQETVFSVDPVGNNVGRDGEPGVFIAEAVRPSENFETNDYAIRAGVSESSVDETTVEMSVADMLKEASVKILAAGVAIGLISLFSQKYFLKSSSSFQRKDMVSSMESDVATIGSVRADDSEALPRMDARTAENIVSKWQKIKSLAFGPDHRIEMLPEVLDGRMLKIWTDRAAETAQLGLVYDYTLLKLSVDSVTVSADGTRALVEATLEESACLSDLVHPENNATDVRTYTTRYEVFWSKSGWKITEGSVLAS |
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9FIG9 | FTSZ1 Q42545 | 2 | EBI-2000800, EBI-2131124 | |
BINARY | Q9FIG9 | PDV2 Q9XII1 | 3 | EBI-2000800, EBI-2000823 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 89-153 | J | ||||
Sequence: DFYQVLGAQTHFLTDGIRRAFEARVSKPPQFGFSDDALISRRQILQAACETLSNPRSRREYNEGL | ||||||
Region | 639-801 | Interaction with PDV2 | ||||
Sequence: KSSSSFQRKDMVSSMESDVATIGSVRADDSEALPRMDARTAENIVSKWQKIKSLAFGPDHRIEMLPEVLDGRMLKIWTDRAAETAQLGLVYDYTLLKLSVDSVTVSADGTRALVEATLEESACLSDLVHPENNATDVRTYTTRYEVFWSKSGWKITEGSVLAS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length801
- Mass (Da)88,260
- Last updated2001-03-01 v1
- Checksum608E776FBA73FECF
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8BCR9 | A0A1P8BCR9_ARATH | ARC6 | 708 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 73 | in Ref. 1; AAQ18644/AAQ18645/AAQ18646 | ||||
Sequence: P → L | ||||||
Sequence conflict | 158 | in Ref. 1; AAQ18646 | ||||
Sequence: E → G | ||||||
Sequence conflict | 513 | in Ref. 1; AAQ18645/AAQ18646 | ||||
Sequence: A → T | ||||||
Sequence conflict | 610 | in Ref. 1; AAQ18646 | ||||
Sequence: D → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |