Reviewed, UniProtKB/Swiss-Prot Q03464 (RIPA_PHYAM)

Names and origin

Protein names	Recommended name:     Antiviral protein alpha     EC=3.2.2.22 Alternative name(s):     PAP-alpha     Ribosome-inactivating protein     rRNA N-glycosidase
Organism	Phytolacca americana (American pokeweed) (Phytolacca decandra)
Taxonomic identifier	3527 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Phytolaccaceae › Phytolacca

Protein attributes

Sequence length	294 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	Inhibits viral infection of plants, and protein synthesis in vitro. Has also been shown to inhibit the replication of mammalian viruses. The protein may provide a means of cellular suicide upon invasion by a virus.
Catalytic activity	Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Subunit structure	Monomer.
Subcellular location	Secreted › cell wall.
Sequence similarities	Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.

Ontologies

Keywords
Biological process	Antiviral defense Plant defense
Cellular component	Cell wall Secreted
Domain	Signal
Molecular function	Hydrolase Protein synthesis inhibitor Toxin
PTM	Disulfide bond
Technical term	3D-structure
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 response to virus Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region 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

Signal peptide

1 – 24

24

By similarity

Chain

25 – 285

261

Antiviral protein alpha

PRO_0000030779

Propeptide

286 – 294

9

PRO_0000030780

Sites

Active site

199

1

By similarity

Amino acid modifications

Disulfide bond

58 ↔ 282

Disulfide bond

108 ↔ 130

Secondary structure

1

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294

Helix Strand Turn

Details...

Beta strand

28 – 31

4

Helix

32 – 34

3

Helix

37 – 51

15

Beta strand

61 – 63

3

Beta strand

69 – 71

3

Beta strand

73 – 79

7

Beta strand

85 – 91

7

Turn

92 – 94

3

Beta strand

97 – 104

8

Beta strand

107 – 113

7

Helix

119 – 129

11

Beta strand

132 – 138

7

Helix

147 – 154

8

Helix

158 – 160

3

Helix

165 – 175

11

Helix

183 – 195

13

Helix

198 – 202

5

Helix

204 – 212

9

Turn

213 – 215

3

Helix

222 – 240

19

Beta strand

245 – 253

9

Beta strand

259 – 264

6

Helix

265 – 268

4

Helix

269 – 271

3

Sequences

	Sequence		Length	Mass (Da)
	Q03464-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: F2EC27724FA85596	FASTA	294	33,069
	10 20 30 40 50 60 MKMMVVVVVM MLSWLILKPP STWAINTITF DVGNATINKY ATFMKSIHNQ AKDPTLKCYG 70 80 90 100 110 120 IPMLPNTNLT PKYLLVTLQD SSLKTITLML KRNNLYVMGY ADTYNGKCRY HIFKDISNTT 130 140 150 160 170 180 ERNDVMTTLC PNPSSRVGKN INYDSSYPAL EKKVGRPRSQ VQLGIQILNS GIGKIYGVDS 190 200 210 220 230 240 FTEKTEAEFL LVAIQMVSEA ARFKYIENQV KTNFNRAFYP NAKVLNLEES WGKISTAIHN 250 260 270 280 290 AKNGALTSPL ELKNANGSKW IVLRVDDIEP DVGLLKYVNG TCQATYQSAM FPHL

References

[1]	"Isolation and analysis of a genomic clone encoding a pokeweed antiviral protein." Kataoka J., Habuka N., Masuta C., Miyano M., Koiwai A. Plant Mol. Biol. 20:879-886(1992) [PubMed: 1281438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leaf, Root and Seed.
[2]	"X-ray structure of a pokeweed antiviral protein, coded by a new genomic clone, at 0.23-nm resolution. A model structure provides a suitable electrostatic field for substrate binding." Ago H., Kataoka J., Tsuge H., Hakuba N., Inagaki E., Noma M., Miyano M. Eur. J. Biochem. 225:369-374(1994) [PubMed: 7925458] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

D10600 Genomic DNA. Translation: BAA01451.1.

PIR

S28421.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1APA	X-ray	2.30	A	25-285	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.2.2.22. 257893.

Family and domain databases

InterPro

IPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
[Graphical view]

Gene3D

G3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit.
G3DSA:4.10.470.10. Ribosome_inactivat_prot_sub2. 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

RIPA_PHYAM

Accession

Primary (citable) accession number: Q03464

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)