UniProt functional annotation for P28522



	UniProt functional annotation for P28522

UniProt code: P28522.

Organism: Zea mays (Maize).

Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.

Function: Potent catalytic inactivator of eukaryotic protein synthesis. It may be a component of natural defense mechanisms involved in protecting the kernel against soil-borne fungal infections.

Catalytic activity: Reaction=Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.; EC=3.2.2.22;

Subunit: Synthesized and stored in the kernel as a 34 kDa inactive precursor. During germination, this neutral precursor is converted into a basic, active form by limited proteolysis, which removes 25 AA of net charge -6 from the center of the polypeptide chain. Additional processing also occurs at the N- and C-termini of the polypeptide. A two-chain active RIP (comprised of 16.5 and 8.5 kDa fragments that remain tightly associated) is produced from this processing event.

Similarity: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Zea mays (Maize).
Taxonomy:		Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.



Function:		Potent catalytic inactivator of eukaryotic protein synthesis. It may be a component of natural defense mechanisms involved in protecting the kernel against soil-borne fungal infections.


Catalytic activity:		Reaction=Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.; EC=3.2.2.22;
Subunit:		Synthesized and stored in the kernel as a 34 kDa inactive precursor. During germination, this neutral precursor is converted into a basic, active form by limited proteolysis, which removes 25 AA of net charge -6 from the center of the polypeptide chain. Additional processing also occurs at the N- and C-termini of the polypeptide. A two-chain active RIP (comprised of 16.5 and 8.5 kDa fragments that remain tightly associated) is produced from this processing event.
Similarity:		Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily. {ECO:0000305}.