[1]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-283, AND PROTEIN SEQUENCE OF 25-115; 206-213 AND 234-277. TISSUE=Leaf; PubMed=2547612 [NCBI, ExPASy, EBI, Israel, Japan] Benatti L., Saccardo M.B., Dani M., Nitti G., Sassano M., Lorenzetti R., Lappi D.A., Soria M.; "Nucleotide sequence of cDNA coding for saporin-6, a type-1 ribosome-inactivating protein from Saponaria officinalis."; Eur. J. Biochem. 183:465-470(1989).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-277. PubMed=8454624 [NCBI, ExPASy, EBI, Israel, Japan] Barthelemy I., Martineau D., Ong M., Matsunami R., Ling N., Benatti L., Cavallaro U., Soria M., Lappi D.A.; "The expression of saporin, a ribosome-inactivating protein from the plant Saponaria officinalis, in Escherichia coli."; J. Biol. Chem. 268:6541-6548(1993).
[3]	NUCLEOTIDE SEQUENCE OF 275-299. TISSUE=Leaf; DOI=10.1016/0014-5793(91)81303-P; PubMed=1936274 [NCBI, ExPASy, EBI, Israel, Japan] Benatti L., Nitti G., Solinas M., Valsasina B., Vitale A., Ceriotti A., Soria M.R.; "A Saporin-6 cDNA containing a precursor sequence coding for a carboxyl-terminal extension."; FEBS Lett. 291:285-288(1991).
[4]	PROTEIN SEQUENCE OF 25-61. DOI=10.1016/0006-291X(85)91981-3; PubMed=3925952 [NCBI, ExPASy, EBI, Israel, Japan] Lappi D.A., Esch F.S., Barbieri L., Stirpe F., Soria M.; "Characterization of a Saponaria officinalis seed ribosome-inactivating protein: immunoreactivity and sequence homologies."; Biochem. Biophys. Res. Commun. 129:934-942(1985).
[5]	PROTEIN SEQUENCE OF 25-72 AND 114-154. DOI=10.1007/BF00280379; PubMed=2325629 [NCBI, ExPASy, EBI, Israel, Japan] Fordham-Skelton A.P., Yarwood A., Croy R.R.D.; "Synthesis of saporin gene probes from partial protein sequence data: use of inosine-oligonucleotides, genomic DNA and the polymerase chain reaction."; Mol. Gen. Genet. 221:134-138(1990).
[6]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-277, AND ACTIVE SITE. DOI=10.1016/S0014-5793(00)01325-9; PubMed=10745075 [NCBI, ExPASy, EBI, Israel, Japan] Savino C., Federici L., Ippoliti R., Lendaro E., Tsernoglou D.; "The crystal structure of saporin SO6 from Saponaria officinalis and its interaction with the ribosome."; FEBS Lett. 470:239-243(2000).

Comments

FUNCTION: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells. Useful as immunotoxin for pharmacological applications.
CATALYTIC ACTIVITY: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
TISSUE SPECIFICITY: Seeds and leaves of the plant.
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

EMBL

X15655; CAA33685.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S57638; AAB25863.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X69135; CAA48889.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X64917; CAA46110.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S05205; S05205.
S16487; S16487.
S18307; S18307.
S29931; S29931.
S38527; S38527.

3D structure databases

PDB

1QI7; X-ray; 2.00 A; A=25-277.

[ExPASy / RCSB / EBI]

1QI7; -.

P20656; 25-277.

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

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`CHAIN`	`25 277`	`253`	`Ribosome-inactivating protein saporin-6.`	`PRO_0000030776`
`PROPEP`	`278 299`	`22`	`Potential.`	`PRO_0000030777`
`ACT_SITE`	`200 200`
`CARBOHYD`	`283 283`		`N-linked (GlcNAc...) (Potential).`
`VARIANT`	`72 72`	`1`	`E -> D.`
`VARIANT`	`115 115`	`1`	`R -> K.`
`CONFLICT`	`60 60`		`G -> S (in Ref. 4; AA sequence).`
`CONFLICT`	`123 123`		`S -> L (in Ref. 2 and 5).`
`CONFLICT`	`212 212`		`I -> T (in Ref. 1; AA sequence).`

Sequence information

Length: 299 AA [This is the length of the unprocessed precursor]

Molecular weight: 33607 Da [This is the MW of the unprocessed precursor]

CRC64: 4BC312958BB4E79B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIYVVATIA WILLQFSAWT TTDAVTSITL DLVNPTAGQY SSFVDKIRNN VKDPNLKYGG 

        70         80         90        100        110        120 
TDIAVIGPPS KEKFLRINFQ SSRGTVSLGL KRDNLYVVAY LAMDNTNVNR AYYFRSEITS 

       130        140        150        160        170        180 
AESTALFPEA TTANQKALEY TEDYQSIEKN AQITQGDQSR KELGLGIDLL STSMEAVNKK 

       190        200        210        220        230        240 
ARVVKDEARF LLIAIQMTAE AARFRYIQNL VIKNFPNKFN SENKVIQFEV NWKKISTAIY 

       250        260        270        280        290 
GDAKNGVFNK DYDFGFGKVR QVKDLQMGLL MYLGKPKSSN EANSTVRHYG PLKPTLLIT

P20656 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