Reviewed, UniProtKB/Swiss-Prot P04399 (RIP2_HORVU)

Names and origin

Protein names

Recommended name:
    Protein synthesis inhibitor II
    EC=3.2.2.22
Alternative name(s):
    Ribosome-inactivating protein II
    rRNA N-glycosidase

Gene names

Name:

RIP30A

Organism

Hordeum vulgare (Barley)

Taxonomic identifier

4513 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Inhibits the elongation phase of protein synthesis. It inactivates fungal ribosomes even more effectively than mammalian ribosomes and is thought to function as a constitutive antifungal agent in plants.
Catalytic activity	Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Subcellular location	Cytoplasm. Note: Starchy endosperm of mature seeds.
Miscellaneous	Three similar RIP 30 isoforms I, II, and III have been described in Barley.
Sequence similarities	Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.

Ontologies

Keywords
Biological process	Plant defense
Cellular component	Cytoplasm
Molecular function	Antimicrobial Fungicide Hydrolase Protein synthesis inhibitor Toxin
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response to fungus Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW xenobiotic metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	rRNA N-glycosylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 280	280	Protein synthesis inhibitor II		PRO_0000221402
Sites
	Active site	174	1	By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylalanine

Sequences

	Sequence		Length	Mass (Da)
	P04399-1 [UniParc]. Last modified March 20, 1987. Version 1. Checksum: A5BDBE8642BF4198	FASTA	280	29,863
	10 20 30 40 50 60 AAKMAKNVDK PLFTATFNVQ ASSADYATFI AGIRNKLRNP AHFSHNEPVL PPVEPNVPPS 70 80 90 100 110 120 RWFHVVLKAS PTSAGLTLAI RADNIYLEGF KSSDGTWWEL TPGLIPGATY VGFGGTYRDL 130 140 150 160 170 180 LGDTDKLTNV ALGRQQLEDA VTALHGRTKA DKASGPKQQQ AREAVTTLLL MVNEATRFQT 190 200 210 220 230 240 VSGFVAGLLH PKAVEKKSGK IGNEMKAQVN GWQDLSAALL KTDVKPPPGK SPAKFTPIEK 250 260 270 280 MGVRTAEQAA ATLGILLFVE VPGGLTVAKA LELFHASGGK

References

[1]	"The complete primary structure of protein synthesis inhibitor II from barley seeds." Asano K., Svensson B., Svendsen I., Poulsen F.M., Roepstorff P. Carlsberg Res. Commun. 51:129-141(1986) Cited for: PROTEIN SEQUENCE.
[2]	"Biochemical and molecular characterization of three barley seed proteins with antifungal properties." Leah R., Tommerup H., Svendsen I., Mundy J. J. Biol. Chem. 266:1564-1573(1991) [PubMed: 1899089] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 164-280. Strain: cv. Piggy.
[3]	"Isolation and partial characterization of two antifungal proteins from barley." Roberts W.K., Selitrennikoff C.P. Biochim. Biophys. Acta 880:161-170(1986) [PubMed: 3942788] [Abstract] Cited for: ANTIFUNGAL ACTIVITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M62906 mRNA. Translation: AAA32951.1.
PIR	RLBH. A03373.
UniGene	Hv.24482
3D structure databases
ModBase	Search...
Organism-specific databases
Gramene	P04399.
Enzyme and pathway databases
BRENDA	3.2.2.22. 283.
Family and domain databases
InterPro	IPR001574. Ribosome_inactivat_prot. IPR017988. Ribosome_inactivat_prot_CS. IPR016138. Ribosome_inactivat_prot_sub1. IPR017989. Ribosome_inactivat_prot_subgr. [Graphical view]
Gene3D	G3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit.
Pfam	PF00161. RIP. 1 hit. [Graphical view]
PRINTS	PR00396. SHIGARICIN.
PROSITE	PS00275. SHIGA_RICIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIP2_HORVU

Accession

Primary (citable) accession number: P04399

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	March 20, 1987
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)