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Literature summary for 2.3.2.31 extracted from

  • Fernandez, M.A.; Belda-Palazon, B.; Julian, J.; Coego, A.; Lozano-Juste, J.; Inigo, S.; Rodriguez, L.; Bueso, E.; Goossens, A.; Rodriguez, P.L.
    RBR-type E3 ligases and the ubiquitin-conjugating enzyme UBC26 regulate abscisic acid receptor levels and signaling (2020), Plant Physiol., 182, 1723-1742 .
    View publication on PubMed
Search for more literature for 2.3.2.31

Cloned(Commentary)

Cloned (Comment) Organism
-
 Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
C361A mutation in isoform RFA4, affects its own ubiquitination and capability to ubiquitinate PYL4 Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol isoform RFA1 Arabidopsis thaliana 5829
-
nucleus isoforms RFA1 and RFA4. RFA4 shows specific nuclear localization and promotes nuclear degradation of abscisic acid receptors Arabidopsis thaliana 5634
-

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
ubiquitination both isoforms RFA1 and RFA4 are ubiquitinated in vivo Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Arabidopsis thaliana
-
root
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[E2 ubiquitin-conjugating enzyme UBC26]-S-ubiquitinyl-L-cysteine + [receptor PYR1]-L-lysine
-
 Arabidopsis thaliana [E2 ubiquitin-conjugating enzyme UBC26]-L-cysteine + [receptor PYR1]-N6-ubiquitinyl-L-lysine
-
 ?

Synonyms

Synonyms Comment Organism
RFA1
-
 Arabidopsis thaliana
RFA4
-
 Arabidopsis thaliana
RING Finger ABA-Related
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function RING Finger ABA-Related1 (RFA1) and RFA4 E3 ubiquitin ligases are key regulators of abscisic acid receptor stability in root and leaf tissues, targeting abscisic acid receptors for degradation in different subcellular locations. Endogenous levels of PYR1 and PYL4 abscisic acid receptors are higher in the Rfa1 Rfa4 double mutant than in wild-type plants. UBC26 is the cognate nuclear E2 enzyme that interacts with the RFA4 E3 ligase and forms UBC26-RFA4-receptor complexes in nuclear speckles. Loss-of-function Ubc26 alleles and the Rfa1Rrfa4 double mutant show enhanced sensitivity to abscisic acid and accumulation of abscisic acid receptors compared with the wild-type Arabidopsis thaliana