Q8LL04 · CPL3_ARATH
- ProteinRNA polymerase II C-terminal domain phosphatase-like 3
- GeneCPL3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1241 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Completely dephosphorylates 'Ser-2', and partially 'Ser-5' and 'Ser-7' of the heptad repeats YSPTSPS in the C-terminal domain (CTD) of the largest RNA polymerase II subunit (RPB1) (PubMed:25464831).
Involved in defense response (PubMed:25464831).
Acts as a negative regulator of immune gene expression and immunity to pathogen infections (PubMed:25464831).
Preferentially dephosphorylates 'Ser-2' of RNA polymerase II CTD (PubMed:25464831).
This counterregulates the MAP kinase (MAPK) or cyclin-dependent kinase C (CDKC)-mediated phosphorylation of CTD in response to pathogens and upon perception of microbe-associated molecular patterns (MAMPs) (PubMed:25464831).
MAPKs phosphorylate and activate CDKCs, which are CTD kinases that positively regulate plant innate immunity (PubMed:25464831).
Acts as a negative regulator of stress gene transcription involved in abscisic acid (ABA) mediated signaling pathway and cold resistance (PubMed:12149434, PubMed:16905668).
Acts as a post-transcriptional gene silencing (PTGS) suppressor (PubMed:31076735).
Involved in defense response (PubMed:25464831).
Acts as a negative regulator of immune gene expression and immunity to pathogen infections (PubMed:25464831).
Preferentially dephosphorylates 'Ser-2' of RNA polymerase II CTD (PubMed:25464831).
This counterregulates the MAP kinase (MAPK) or cyclin-dependent kinase C (CDKC)-mediated phosphorylation of CTD in response to pathogens and upon perception of microbe-associated molecular patterns (MAMPs) (PubMed:25464831).
MAPKs phosphorylate and activate CDKCs, which are CTD kinases that positively regulate plant innate immunity (PubMed:25464831).
Acts as a negative regulator of stress gene transcription involved in abscisic acid (ABA) mediated signaling pathway and cold resistance (PubMed:12149434, PubMed:16905668).
Acts as a post-transcriptional gene silencing (PTGS) suppressor (PubMed:31076735).
Catalytic activity
- O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
Cofactor
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds Mg2+, Co2+ or Mn2+.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA polymerase II CTD heptapeptide repeat phosphatase activity | |
Biological Process | defense response | |
Biological Process | negative regulation of abscisic acid-activated signaling pathway | |
Biological Process | negative regulation of post-transcriptional gene silencing by regulatory ncRNA | |
Biological Process | response to salt stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRNA polymerase II C-terminal domain phosphatase-like 3
- EC number
- Short namesFCP-like 3
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8LL04
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Grows more slowly and flower earlier than wild-type plants. ABA hyperactivation of stress-inducible genes.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 933 | Loss of phosphatase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1064 | Loss of phosphatase activity; when associated with A-1065. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1065 | Loss of phosphatase activity; when associated with A-1064. | ||||
Sequence: D → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 57 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000376085 | 1-1241 | RNA polymerase II C-terminal domain phosphatase-like 3 | |||
Sequence: MLVARSGCSRTLIRMGNDENLMVMVDVEEGEIPDSVNTEIEVKHKSTTTTADVGGDVDVGVVAGGRGGGGGGSNGNSRVWTMEELISQYPAYRPYANSGLSNLAWARAVQNKPFNEGLVMDYEPRESDKIVIEDSDDEKEEGELEEGEIDLVDNASDDNLVEKDTESVVLISADKVEDDRILKERDLEKKVKLIRGVLESTSLVEAQTGFEGVCSRILGALESLRELVSDNDDFPKRDTLVQLSFASLQTINYVFCSMNNISKERNKETMSRLLTLVNDHFSQFLSFNQKNEIETMNQDLSRSAIAVFAGTSSEENVNQMTQPSNGDSFLAKKLTSESTHRGAAYLRSRLPMLPLLDLHKDHDADSLPSPTRETTPSLPVNGRHTMVRPGFPVGRESQTTEGAKVYSYESDARKAVSTYQQKFGLNSVFKTDDLPSPTPSGEPNDGNGDVGGEVSSSVVKSSNPGSHLIYGQDVPLPSNFNSRSMPVANSVSSTVPPHHLSIHAISAPTASDQTVKPSAKSRDPRLRLAKPDAANVTIYSYSSGDARNLSKVELSADLVNPRKQKAADEFLIDGPAWKRQKSDTDAPKAAGTGGWLEDTESSGLLKLESKPRLIENGVTSMTSSVMPTSAVSVSQKVRTASTDTASLQSLLKDIAVNPTMLLNLLKMGERQKVPEKAIQKPMDPRRAAQLPGSSVQPGVSTPLSIPASNALAANSLNSGVLQDSSQNAPAAESGSIRMKPRDPRRILHGSTLQRTDSSMEKQTKVNDPSTLGTLTMKGKAEDLETPPQLDPRQNISQNGTSKMKISGELLSGKTPDFSTQFTKNLKSIADMVVVSQQLGNPPASMHSVQLKTERDVKHNPSNPNAQDEDVSVSAASVTAAAGPTRSMNSWGDVEHLFEGYDDIQRVAIQRERVRRLEEQNKMFASQKLSLVLDIDHTLLNSAKFNEVESRHEEILRKKEEQDREKPYRHLFRFLHMGMWTKLRPGIWNFLEKASKLYELHLYTMGNKLYATEMAKLLDPKGVLFNGRVISKGDDGDPLDGDERVPKSKDLEGVMGMESSVVIIDDSVRVWPQHKMNLIAVERYLYFPCSRRQFGLLGPSLLELDRDEVPEEGTLASSLAVIEKIHQNFFSHTSLDEVDVRNILASEQRKILAGCRIVFSRIIPVGEAKPHLHPLWQTAEQFGAVCTTQVDEHVTHVVTNSLGTDKVNWALTRGRFVVHPGWVEASAFLYQRANENLYAINP |
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 361-402 | Disordered | ||||
Sequence: DHDADSLPSPTRETTPSLPVNGRHTMVRPGFPVGRESQTTEG | ||||||
Compositional bias | 428-443 | Polar residues | ||||
Sequence: VFKTDDLPSPTPSGEP | ||||||
Region | 428-470 | Disordered | ||||
Sequence: VFKTDDLPSPTPSGEPNDGNGDVGGEVSSSVVKSSNPGSHLIY | ||||||
Compositional bias | 450-468 | Polar residues | ||||
Sequence: VGGEVSSSVVKSSNPGSHL | ||||||
Region | 505-525 | Disordered | ||||
Sequence: ISAPTASDQTVKPSAKSRDPR | ||||||
Region | 578-598 | Disordered | ||||
Sequence: KRQKSDTDAPKAAGTGGWLED | ||||||
Region | 677-702 | Disordered | ||||
Sequence: AIQKPMDPRRAAQLPGSSVQPGVSTP | ||||||
Region | 720-800 | Disordered | ||||
Sequence: VLQDSSQNAPAAESGSIRMKPRDPRRILHGSTLQRTDSSMEKQTKVNDPSTLGTLTMKGKAEDLETPPQLDPRQNISQNGT | ||||||
Compositional bias | 750-773 | Polar residues | ||||
Sequence: STLQRTDSSMEKQTKVNDPSTLGT | ||||||
Region | 852-885 | Disordered | ||||
Sequence: TERDVKHNPSNPNAQDEDVSVSAASVTAAAGPTR | ||||||
Compositional bias | 863-885 | Polar residues | ||||
Sequence: PNAQDEDVSVSAASVTAAAGPTR | ||||||
Domain | 923-1103 | FCP1 homology | ||||
Sequence: FASQKLSLVLDIDHTLLNSAKFNEVESRHEEILRKKEEQDREKPYRHLFRFLHMGMWTKLRPGIWNFLEKASKLYELHLYTMGNKLYATEMAKLLDPKGVLFNGRVISKGDDGDPLDGDERVPKSKDLEGVMGMESSVVIIDDSVRVWPQHKMNLIAVERYLYFPCSRRQFGLLGPSLLEL | ||||||
Domain | 1146-1239 | BRCT | ||||
Sequence: EQRKILAGCRIVFSRIIPVGEAKPHLHPLWQTAEQFGAVCTTQVDEHVTHVVTNSLGTDKVNWALTRGRFVVHPGWVEASAFLYQRANENLYAI |
Domain
The BRCT domain is required for interaction with RAP74.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,241
- Mass (Da)136,479
- Last updated2009-05-26 v2
- ChecksumCEFFBD725719D404
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8B2G0 | A0A1P8B2G0_ARATH | CPL3 | 984 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 428-443 | Polar residues | ||||
Sequence: VFKTDDLPSPTPSGEP | ||||||
Compositional bias | 450-468 | Polar residues | ||||
Sequence: VGGEVSSSVVKSSNPGSHL | ||||||
Compositional bias | 750-773 | Polar residues | ||||
Sequence: STLQRTDSSMEKQTKVNDPSTLGT | ||||||
Compositional bias | 863-885 | Polar residues | ||||
Sequence: PNAQDEDVSVSAASVTAAAGPTR | ||||||
Sequence conflict | 1010 | in Ref. 1; AAM94371 | ||||
Sequence: A → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF486633 EMBL· GenBank· DDBJ | AAM94371.1 EMBL· GenBank· DDBJ | mRNA | ||
AC002332 EMBL· GenBank· DDBJ | AAB80671.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002685 EMBL· GenBank· DDBJ | AEC08850.1 EMBL· GenBank· DDBJ | Genomic DNA |