[1]	PROTEIN SEQUENCE. TISSUE=Seed; PubMed=1368643 [NCBI, ExPASy, EBI, Israel, Japan] Kung S.S., Kimura M., Funatsu G.; "The complete amino acid sequence of antiviral protein from the seeds of pokeweed (Phytolacca americana)."; Agric. Biol. Chem. 54:3301-3318(1990).

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.
SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

JE0401; JE0401.

3D structure databases

PDB

1GIK; X-ray; 1.80 A; A=1-261.	[ExPASy / RCSB / EBI]
1J1Q; X-ray; 1.80 A; A=1-261.	[ExPASy / RCSB / EBI]
1J1R; X-ray; 1.90 A; A=1-261.	[ExPASy / RCSB / EBI]
1J1S; X-ray; 2.00 A; A=1-261.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GIK; -.
1J1Q; -.
1J1R; -.
1J1S; -.

ModBase

P23339.

Ontologies

GO:0006952;	Biological process: defense response (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0009615;	Biological process: response to virus (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001574; Ribosome_inactivat_prot.
IPR016138; Ribosome_inactivat_prot_sub1.
IPR016139; Ribosome_inactivat_prot_sub2.
Graphical view of domain structure.

Gene3D

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

Pfam

PF00161; RIP; 1.
Pfam graphical view of domain structure.

PRINTS

PR00396; SHIGARICIN.

PROSITE

PS00275; SHIGA_RICIN; 1.

Other

DB00173; Adenine.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Antiviral defense; Direct protein sequencing; Hydrolase; Plant defense; Protein synthesis inhibitor; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 261`	`261`	`Antiviral protein S.`	`PRO_0000221415`
`ACT_SITE`	`175 175`		`By similarity.`
`DISULFID`	`34 258`
`DISULFID`	`84 105`
`STRAND`	`3 10`	`8`
`HELIX`	`13 27`	`15`
`STRAND`	`34 36`	`3`
`STRAND`	`49 55`	`7`
`STRAND`	`61 67`	`7`
`TURN`	`68 70`	`3`
`STRAND`	`73 80`	`8`
`STRAND`	`83 88`	`6`
`HELIX`	`95 104`	`10`
`STRAND`	`111 113`	`3`
`HELIX`	`122 129`	`8`
`HELIX`	`134 136`	`3`
`HELIX`	`141 151`	`11`
`HELIX`	`159 172`	`14`
`HELIX`	`174 178`	`5`
`HELIX`	`180 188`	`9`
`STRAND`	`190 192`	`3`
`HELIX`	`198 205`	`8`
`HELIX`	`207 215`	`9`
`HELIX`	`218 220`	`3`
`STRAND`	`221 229`	`9`
`STRAND`	`235 240`	`6`
`HELIX`	`241 244`	`4`

Sequence information

Length: 261 AA [This is the length of the unprocessed precursor]

Molecular weight: 29200 Da [This is the MW of the unprocessed precursor]

CRC64: D88B99962FE8399D [This is a checksum on the sequence]

        10         20         30         40         50         60 
INTITFDAGN ATINKYATFM ESLRNEAKDP SLKCYGIPML PNTNSTIKYL LVKLQGASLK 

        70         80         90        100        110        120 
TITLMLRRNN LYVMGYSDPY DNKCRYHIFN DIKGTEYSDV ENTLCPSSNP RVAKPINYNG 

       130        140        150        160        170        180 
LYPTLEKKAG VTSRNEVQLG IQILSSDIGK ISGQGSFTEK IEAKFLLVAI QMVSEAARFK 

       190        200        210        220        230        240 
YIENQVKTNF NRDFSPNDKV LDLEENWGKI STAIHNSKNG ALPKPLELKN ADGTKWIVLR 

       250        260 
VDEIKPDVGL LNYVNGTCQA T

P23339 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools