Reviewed, UniProtKB/Swiss-Prot P28522 (RIPX_MAIZE)

Names and origin

Protein names	Recommended name:     Ribosome-inactivating protein     EC=3.2.2.22 Alternative name(s):     rRNA N-glycosidase Cleaved into the following 2 chains:     1- Recommended name:             Ribosome-inactivating protein alpha chain     2- Recommended name:             Ribosome-inactivating protein beta chain
Organism	Zea mays (Maize)
Taxonomic identifier	4577 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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	Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Subunit structure	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.
Sequence similarities	Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.

Ontologies

Keywords
Biological process	Plant defense
Molecular function	Hydrolase Protein synthesis inhibitor Toxin
PTM	Cleavage on pair of basic residues Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response 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
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

Propeptide

1 – 16

16

Or 12 (in 10% of the molecules)

PRO_0000030758

Chain

17 – 161

145

Ribosome-inactivating protein alpha chain

PRO_0000030759

Propeptide

162 – 186

25

PRO_0000030760

Chain

187 – ?257

71

Ribosome-inactivating protein beta chain

PRO_0000030761

Propeptide

?258 – 301

44

PRO_0000030762

Sites

Active site

207

1

By similarity

Secondary structure

1

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301

Helix Strand Turn

Details...

Beta strand

23 – 28

6

Helix

36 – 48

13

Beta strand

71 – 78

8

Beta strand

83 – 89

7

Turn

90 – 92

3

Beta strand

105 – 107

3

Helix

130 – 133

4

Helix

147 – 156

10

Helix

180 – 188

9

Helix

192 – 204

13

Helix

212 – 219

8

Helix

238 – 240

3

Helix

241 – 253

13

Helix

260 – 263

4

Helix

270 – 273

4

Turn

274 – 276

3

Beta strand

277 – 280

4

Sequences

	Sequence		Length	Mass (Da)
	P28522-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: C73F599A2121D360	FASTA	301	33,330
	10 20 30 40 50 60 MAEITLEPSD LMAQTNKRIV PKFTEIFPVE DANYPYSAFI ASVRKDVIKH CTDHKGIFQP 70 80 90 100 110 120 VLPPEKKVPE LWFYTELKTR TSSITLAIRM DNLYLVGFRT PGGVWWEFGK DGDTHLLGDN 130 140 150 160 170 180 PRWLGFGGRY QDLIGNKGLE TVTMGRAEMT RAVNDLAKKK KMATLEEEEV KMQMQMPEAA 190 200 210 220 230 240 DLAAAAAADP QADTKSKLVK LVVMVCEGLR FNTVSRTVDA GFNSQHGVTL TVTQGKQVQK 250 260 270 280 290 300 WDRISKAAFE WADHPTAVIP DMQKLGIKDK NEAARIVALV KNQTTAAAAT AASADNDDDE A

References

[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: 1744135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 13-49; 155-161 AND 187-215.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M77122 mRNA. Translation: AAA33508.1.

PIR

RLZMRI. A41590.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K6H	NMR	-	A	17-288	[»]
2PQI	X-ray	2.50	A/B/C	22-288	[»]
2PQJ	X-ray	2.80	A/B/C	22-288	[»]

ModBase

Search...

Organism-specific databases

Gramene

P28522.

MaizeGDB

30000.

Enzyme and pathway databases

BRENDA

3.2.2.22. 289.

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

RIPX_MAIZE

Accession

Primary (citable) accession number: P28522

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	September 22, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)