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Protein

Ribosome-inactivating protein

Gene
N/A
Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei207 – 2071By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein synthesis inhibitor, Toxin

Keywords - Biological processi

Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-inactivating protein (EC:3.2.2.22)
Alternative name(s):
rRNA N-glycosidase
Cleaved into the following 2 chains:
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Organism-specific databases

MaizeGDBi30000.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1616Or 12 (in 10% of the molecules)PRO_0000030758Add
BLAST
Chaini17 – 161145Ribosome-inactivating protein alpha chainPRO_0000030759Add
BLAST
Propeptidei162 – 186251 PublicationPRO_0000030760Add
BLAST
Chaini187 – ?25771Ribosome-inactivating protein beta chainPRO_0000030761Add
BLAST
Propeptidei?258 – 30144PRO_0000030762Add
BLAST

Keywords - PTMi

Cleavage on pair of basic residues, Zymogen

Proteomic databases

PaxDbiP28522.
PRIDEiP28522.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

STRINGi4577.GRMZM2G063536_P01.

Structurei

Secondary structure

1
301
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 304Combined sources
Helixi36 – 4813Combined sources
Beta strandi51 – 544Combined sources
Beta strandi57 – 615Combined sources
Beta strandi72 – 787Combined sources
Beta strandi83 – 897Combined sources
Helixi90 – 923Combined sources
Beta strandi94 – 996Combined sources
Turni101 – 1033Combined sources
Beta strandi105 – 1095Combined sources
Helixi115 – 1173Combined sources
Beta strandi118 – 1214Combined sources
Helixi130 – 1345Combined sources
Beta strandi135 – 1373Combined sources
Helixi139 – 1413Combined sources
Beta strandi142 – 1454Combined sources
Helixi146 – 15712Combined sources
Helixi194 – 20411Combined sources
Helixi206 – 2105Combined sources
Helixi212 – 2209Combined sources
Turni221 – 2233Combined sources
Beta strandi224 – 2263Combined sources
Helixi232 – 2387Combined sources
Helixi241 – 25313Combined sources
Helixi260 – 2634Combined sources
Turni264 – 2663Combined sources
Helixi270 – 2767Combined sources
Beta strandi277 – 2804Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K6HNMR-A17-162[»]
A190-288[»]
2PQIX-ray2.50A/B/C22-162[»]
A/B/C190-288[»]
2PQJX-ray2.80A/B/C22-162[»]
A/B/C190-288[»]
ProteinModelPortaliP28522.
SMRiP28522. Positions 22-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28522.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410JJGF. Eukaryota.
ENOG410ZF6B. LUCA.

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
InterProiIPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR017989. Ribosome_inactivat_prot_subgr.
[Graphical view]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SUPFAMiSSF56371. SSF56371. 2 hits.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEITLEPSD LMAQTNKRIV PKFTEIFPVE DANYPYSAFI ASVRKDVIKH
60 70 80 90 100
CTDHKGIFQP VLPPEKKVPE LWFYTELKTR TSSITLAIRM DNLYLVGFRT
110 120 130 140 150
PGGVWWEFGK DGDTHLLGDN PRWLGFGGRY QDLIGNKGLE TVTMGRAEMT
160 170 180 190 200
RAVNDLAKKK KMATLEEEEV KMQMQMPEAA DLAAAAAADP QADTKSKLVK
210 220 230 240 250
LVVMVCEGLR FNTVSRTVDA GFNSQHGVTL TVTQGKQVQK WDRISKAAFE
260 270 280 290 300
WADHPTAVIP DMQKLGIKDK NEAARIVALV KNQTTAAAAT AASADNDDDE

A
Length:301
Mass (Da):33,330
Last modified:December 1, 1992 - v1
Checksum:iC73F599A2121D360
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77122 mRNA. Translation: AAA33508.1.
PIRiA41590. RLZMRI.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77122 mRNA. Translation: AAA33508.1.
PIRiA41590. RLZMRI.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K6HNMR-A17-162[»]
A190-288[»]
2PQIX-ray2.50A/B/C22-162[»]
A/B/C190-288[»]
2PQJX-ray2.80A/B/C22-162[»]
A/B/C190-288[»]
ProteinModelPortaliP28522.
SMRiP28522. Positions 22-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G063536_P01.

Proteomic databases

PaxDbiP28522.
PRIDEiP28522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MaizeGDBi30000.

Phylogenomic databases

eggNOGiENOG410JJGF. Eukaryota.
ENOG410ZF6B. LUCA.

Miscellaneous databases

EvolutionaryTraceiP28522.

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
InterProiIPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR017989. Ribosome_inactivat_prot_subgr.
[Graphical view]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SUPFAMiSSF56371. SSF56371. 2 hits.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize. Novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton internal peptide segment."
    Walsh T.A., Morgan A.E., Hey T.D.
    J. Biol. Chem. 266:23422-23427(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 13-49; 155-161 AND 187-215.

Entry informationi

Entry nameiRIPX_MAIZE
AccessioniPrimary (citable) accession number: P28522
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: February 17, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.