Reviewed, UniProtKB/Swiss-Prot P10297 (RIP1_PHYAM)

Names and origin

Protein names

Recommended name:
    Antiviral protein I
    EC=3.2.2.22
Alternative name(s):
    PAP-I
    PAP-C
    Ribosome-inactivating protein
    rRNA N-glycosidase

Gene names

Name:

PAP1

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	313 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.
Catalytic activity	Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Tissue specificity	Spring leaves and roots.
Sequence similarities	Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.

Ontologies

Keywords
Biological process	Antiviral defense Plant defense
Domain	Signal
Molecular function	Hydrolase Protein synthesis inhibitor Toxin
PTM	Disulfide bond
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 response to virus 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

Signal peptide

1 – 22

22

Ref.1 Ref.2 Ref.3 Ref.4 Ref.5

Chain

23 – 285

263

Antiviral protein I

PRO_0000030781

Propeptide

286 – 313

28

PRO_0000030782

Sites

Active site

198

1

By similarity

Amino acid modifications

Disulfide bond

56 ↔ 281

Disulfide bond

107 ↔ 128

Secondary structure

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313

Helix Strand Turn

Details...

Beta strand

25 – 32

8

Helix

35 – 49

15

Beta strand

59 – 61

3

Beta strand

71 – 77

7

Helix

79 – 81

3

Beta strand

83 – 89

7

Turn

90 – 92

3

Beta strand

95 – 102

8

Turn

103 – 105

3

Beta strand

106 – 111

6

Helix

118 – 127

10

Helix

131 – 133

3

Beta strand

134 – 136

3

Helix

145 – 151

7

Helix

157 – 159

3

Helix

164 – 174

11

Helix

182 – 201

20

Helix

203 – 211

9

Turn

212 – 214

3

Helix

221 – 228

8

Helix

230 – 239

10

Beta strand

244 – 252

9

Beta strand

258 – 263

6

Helix

264 – 267

4

Helix

268 – 270

3

Sequences

	Sequence		Length	Mass (Da)
	P10297-1 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: 2C57B2861EBA57F5	FASTA	313	35,219
	10 20 30 40 50 60 MKSMLVVTIS IWLILAPTST WAVNTIIYNV GSTTISKYAT FLNDLRNEAK DPSLKCYGIP 70 80 90 100 110 120 MLPNTNTNPK YVLVELQGSN KKTITLMLRR NNLYVMGYSD PFETNKCRYH IFNDISGTER 130 140 150 160 170 180 QDVETTLCPN ANSRVSKNIN FDSRYPTLES KAGVKSRSQV QLGIQILDSN IGKISGVMSF 190 200 210 220 230 240 TEKTEAEFLL VAIQMVSEAA RFKYIENQVK TNFNRAFNPN PKVLNLQETW GKISTAIHDA 250 260 270 280 290 300 KNGVLPKPLE LVDASGAKWI VLRVDEIKPD VALLNYVGGS CQTTYNQNAM FPQLIMSTYY 310 NYMVNLGDLF EGF

References

[1]	"Isolation and characterization of a cDNA clone encoding the anti-viral protein from Phytolacca americana." Lin Q., Chen Z.C., Antoniw J.F., White R.F. Plant Mol. Biol. 17:609-614(1991) [PubMed: 1912488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-62. Tissue: Leaf.
[2]	"Ribosome-inactivating proteins from plant cells in culture." Barbieri L., Bolognesi A., Cenini P., Falasca A.I., Minghetti A., Garofano L., Guicciardi A., Lappi D., Miller S.P. Biochem. J. 257:801-807(1989) [PubMed: 2930487] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-65.
[3]	"Seasonal variations in different forms of pokeweed antiviral protein, a potent inactivator of ribosomes." Houston L.L., Ramakrishnan S., Hermodson M.A. J. Biol. Chem. 258:9601-9604(1983) [PubMed: 6885760] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-54. Tissue: Leaf.
[4]	"Characterization of translational inhibitors from Phytolacca americana. Amino-terminal sequence determination and antibody-inhibitor conjugates." Bjorn M.J., Larrick J., Piatak M., Wilson K.J. Biochim. Biophys. Acta 790:154-163(1984) [PubMed: 6091760] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-54. Tissue: Leaf.
[5]	"Purification and properties of new ribosome-inactivating proteins with RNA N-glycosidase activity." Bolognesi A., Barbieri L., Abbondanza A., Falasca A.I., Carnicelli D., Battelli M.G., Stirpe F. Biochim. Biophys. Acta 1087:293-302(1990) [PubMed: 2248976] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-54. Tissue: Root.
[6]	"The 2.5 A structure of pokeweed antiviral protein." Monzingo A.F., Collins E.J., Ernst S.R., Irvin J.D., Robertus J.D. J. Mol. Biol. 233:705-715(1993) [PubMed: 8411176] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[7]	"X-ray crystallographic analysis of the structural basis for the interactions of pokeweed antiviral protein with its active site inhibitor and ribosomal RNA substrate analogs." Kurinov I.V., Myers D.E., Irvin J.D., Uckun F.M. Protein Sci. 8:1765-1772(1999) [PubMed: 10493577] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-284.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X55383 mRNA. Translation: CAA39054.1.

PIR

S17757.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D6A	X-ray	2.10	A/B	23-284	[»]
1PAF	X-ray	2.50	A/B	23-284	[»]
1PAG	X-ray	2.80	A/B	23-284	[»]
1QCG	X-ray	2.10	A/B	23-284	[»]
1QCI	X-ray	2.00	A/B	23-284	[»]
1QCJ	X-ray	2.10	A/B	23-284	[»]

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...

Other Resources

DrugBank

DB00173. Adenine.

Entry information

Entry name

RIP1_PHYAM

Accession

Primary (citable) accession number: P10297

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)