NCBI Accession #
NP_189143.2
NCBI GenBank Nucleotide #
NM_113411.3
NCBI Official Full Name
RPM1 interacting protein 4
NCBI Official Symbol
RIN4
NCBI Official Synonym Symbols
AtRIN4; RPM1 interacting protein 4
NCBI Protein Information
RPM1 interacting protein 4
NCBI Summary
Encodes a member of the R protein complex and may represent a virulence target of type III pili effector proteins (virulence factors) from bacterial pathogens, which is 'guarded' by R protein complex (RPM1 and RPS2 proteins). RIN4 physically interacts with RPS2 and RPM1 in vivo. Bacterial avirulence (Avr) effectors AvrB, AvrRpm1, and AvrRpt2 induce a mobility shift in RIN4 and expression of AvrRpt2 induces rapid degradation of RIN4. RIN4 contains 2 sites for AvrRpt2 autocleavage, called RCS1 and RCS2. Overexpression of RIN4 inhibits multiple phenotypes associated with AvrRpt2 function and also inhibits PAMP-induced defense signaling. Attached to the plasma membrane at its carboxyl terminus. Cleaved by AvrRpt2 at two PxFGxW motifs, one releasing a large portion of RIN4 from the plasma membrane and both exposing amino-terminal residues that destabilized the carboxyl-terminal cleavage products by targeting them for N-end ubiquitylation and proteasomal degradation. Major virulence target of the TTSE HopF2Pto.
UniProt Protein Name
RPM1-interacting protein 4
UniProt Primary Accession #
Q8GYN5
UniProt Secondary Accession #
Q9LSG9
UniProt Related Accession #
Q8GYN5
UniProt Comments
Essential regulator of plant defense, which plays a central role in resistance in case of infection by a pathogen. It is a common target for both type III avirulence proteins from P.syringae (AvrB, AvrRpm1 and AvrRpt2) and for the plant Resistance (R) proteins RPM1 and RPS2. In strains carrying the appropriate R gene for avirulence proteins of the pathogen, its association with avirulence proteins triggers a defense system including the hypersensitive response, which limits the spread of disease. In contrast, in plants lacking appropriate R genes, its association with avirulence proteins of the pathogen impairs the defense system and leads to the pathogen multiplication.