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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)DescriptionActionsGraphical viewLength
Active sitei207By similarity1

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)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000307581 – 16Or 12 (in 10% of the molecules)Add BLAST16
ChainiPRO_000003075917 – 161Ribosome-inactivating protein alpha chainAdd BLAST145
PropeptideiPRO_0000030760162 – 1861 PublicationAdd BLAST25
ChainiPRO_0000030761187 – ?257Ribosome-inactivating protein beta chainAdd BLAST71
PropeptideiPRO_0000030762?258 – 301Add BLAST44

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

1301
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 30Combined sources4
Helixi36 – 48Combined sources13
Beta strandi51 – 54Combined sources4
Beta strandi57 – 61Combined sources5
Beta strandi72 – 78Combined sources7
Beta strandi83 – 89Combined sources7
Helixi90 – 92Combined sources3
Beta strandi94 – 99Combined sources6
Turni101 – 103Combined sources3
Beta strandi105 – 109Combined sources5
Helixi115 – 117Combined sources3
Beta strandi118 – 121Combined sources4
Helixi130 – 134Combined sources5
Beta strandi135 – 137Combined sources3
Helixi139 – 141Combined sources3
Beta strandi142 – 145Combined sources4
Helixi146 – 157Combined sources12
Helixi194 – 204Combined sources11
Helixi206 – 210Combined sources5
Helixi212 – 220Combined sources9
Turni221 – 223Combined sources3
Beta strandi224 – 226Combined sources3
Helixi232 – 238Combined sources7
Helixi241 – 253Combined sources13
Helixi260 – 263Combined sources4
Turni264 – 266Combined sources3
Helixi270 – 276Combined sources7
Beta strandi277 – 280Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
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...

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: November 2, 2016
This is version 84 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.