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Reviewed, UniProtKB/Swiss-Prot P27559 (RIP2_SAPOF)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ribosome-inactivating protein saporin-2
      Short name=SAP-2
      Short name=SO-2
    EC=3.2.2.22
Alternative name(s):
    rRNA N-glycosidase
Gene names
Name: SAP2
OrganismSaponaria officinalis (Common soapwort)
Taxonomic identifier3572 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesCaryophyllaceaeSaponaria

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (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.

Sequence similarities

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

Ontologies

Keywords
   Biological processPlant defense
   DomainSignal
   Molecular functionHydrolase
Protein synthesis inhibitor
Toxin
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processdefense 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 functionrRNA N-glycosylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.3
Chain25 – 292268Ribosome-inactivating protein saporin-2
PRO_0000030774

Sites

Active site2001 By similarity

Natural variations

Natural variant721D → E

Sequences

Sequence LengthMass (Da)Tools
P27559-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: FA143C0E1BE88976

FASTA29232,811
        10         20         30         40         50         60 
MKIYVVATIA WILLQFSAWT TTDAVTSITL DLVNPTAGQY SSFVDKIRNN VKDPNLKYGG 

        70         80         90        100        110        120 
TDIAVIGPPS KDKFLRINFQ SSRGTVSLGL KRDNLYVVAY LAMDNTNVNR AYYFKSEITS 

       130        140        150        160        170        180 
AELTALFPEA TTANQKALEY TEDYQSIEKN AQITQGDKSR KELGLGIDLL LTFMEAVNKK 

       190        200        210        220        230        240 
ARVVKNEARF LLIAIQMTAE VARFRYIQNL VTKNFPNKFD SDNKVIQFEV SWRKISTAIY 

       250        260        270        280        290 
GDAKNGVFNK DYDFGFGKVR QVKDLQMGLL MYLGKPKSSN EANSTAYATT VL 

« Hide

References

[1]"Characterisation of saporin genes: in vitro expression and ribosome inactivation."
Fordham-Skelton A.P., Taylor P.E., Hartley M.R., Croy R.R.D.
Mol. Gen. Genet. 229:460-466(1991) [PubMed: 1719367] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The expression of saporin, a ribosome-inactivating protein from the plant Saponaria officinalis, in Escherichia coli."
Barthelemy I., Martineau D., Ong M., Matsunami R., Ling N., Benatti L., Cavallaro U., Soria M., Lappi D.A.
J. Biol. Chem. 268:6541-6548(1993) [PubMed: 8454624] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-284.
Tissue: Leaf.
[3]"Distribution and properties of major ribosome-inactivating proteins (28 S rRNA N-glycosidases) of the plant Saponaria officinalis L. (Caryophyllaceae)."
Ferreras J.M., Barbieri L., Girbes T., Battelli M.G., Rojo M.A., Arias F.J., Rocher M.A., Soriano F., Mendez E., Stirpe F.
Biochim. Biophys. Acta 1216:31-42(1993) [PubMed: 8218413] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-54.

Cross-references

Sequence databases

X59255 Genomic DNA. Translation: CAA41948.1.
X69132 Genomic DNA. Translation: CAA48886.1.
X69133 Genomic DNA. Translation: CAA48887.1.
PIRS16487.
RLQHG2. S17933.
S38527.

3D structure databases

HSSPHSSP built from PDB template 1QI7 based on UniProtKB P20656.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.2.2.22. 39707.

Family and domain databases

InterProIPR001574. 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]
Gene3DG3DSA:3.40.420.10. Ribosome_inactivat_prot_sub1. 1 hit.
G3DSA:4.10.470.10. Ribosome_inactivat_prot_sub2. 1 hit.
PfamPF00161. RIP. 1 hit.
[Graphical view]
PRINTSPR00396. SHIGARICIN.
PROSITEPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIP2_SAPOF
AccessionPrimary (citable) accession number: P27559
Secondary accession number(s): Q41390, Q9SAP5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents