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P56626 (RIP1_TRIAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Type I ribosome-inactivating protein trichoanguina
Short name=RIP
EC=3.2.2.22
Alternative name(s):
Trichoanguin
rRNA N-glycosidase
Gene names
Name:TCA
OrganismTrichosanthes anguina (Snake gourd)
Taxonomic identifier50544 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Cucurbitales › Cucurbitaceae › Sicyoeae › Trichosanthes

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits protein synthesis by depurinating 28S rRNA in ribosomes.

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
   PTMGlycoprotein
   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

   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 – 1919 Ref.2
Chain20 – 264245Type I ribosome-inactivating protein trichoanguina
PRO_0000030763
Propeptide265 – 29430
PRO_0000030764

Sites

Active site1771 By similarity
Active site1801 By similarity

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) Probable
Glycosylation2201N-linked (GlcNAc...) Probable

Experimental info

Sequence conflict511C → Y AA sequence Ref.2
Sequence conflict651W → R AA sequence Ref.2
Sequence conflict841N → D AA sequence Ref.2
Sequence conflict1521A → S AA sequence Ref.2
Sequence conflict1741C → S AA sequence Ref.2
Sequence conflict2451N → H AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P56626 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: DA4F8B7CE3290994

FASTA29432,235
        10         20         30         40         50         60 
MALSFFFLAI SLGSPTAIGD VSFDLSTATK KSYSSFITQL RDALPTQGTV CGIPLLPSTA 

        70         80         90        100        110        120 
SGSQWFRFFN LTNYNDETVT VAVNVTNVYI VAYRADAVSY FFEDTPAEAF KLIFAGTKTV 

       130        140        150        160        170        180 
KLPYSGNYDK LQSVVGKQRD MIELGIPALS SAITNMVYYD YQSTAAALLV LIQCTAEAAR 

       190        200        210        220        230        240 
YKYIEQQVSS HISSNFYPNQ AVISLENKWG ALSKQIQIAN RTGHGQFENP VELYNPDGTR 

       250        260        270        280        290 
FSVTNTSAGV VKGNIKLLLY YKASVGSEYD IPTTILHPGA MGMLHNQNGN YVTM

« Hide

References

[1]"Purification, characterization and molecular cloning of trichoanguin, a novel type I ribosome-inactivating protein from the seeds of Trichosanthes anguina."
Chow L.-P., Chou M.-H., Ho C.-Y., Chuang C.-C., Pan F.-M., Wu S.-H., Lin J.-Y.
Biochem. J. 338:211-219(1999) [PubMed: 9931318] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
Strain: cv. Anguina.
Tissue: Seed.
[2]"Amino acid sequence of trichoanguina, a ribosomal-inactivating protein from Trichosanthes anguina seeds."
Chow L.-P., Kamo M., Lin J.-Y., Wang S.-H., Ueno Y., Tsugita A.
J. Biomed. Sci. 3:178-186(1996) [PubMed: 11725098] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-264.
Tissue: Seed.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF055086 mRNA. Translation: AAD02686.1.
PIRJC4840.

3D structure databases

ProteinModelPortalP56626.
SMRP56626. Positions 20-260.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001574. Ribosome_inactivat_prot.
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.
SUPFAMSSF56371. Ribosome_inactivat_prot. 1 hit.
PROSITEPS00275. SHIGA_RICIN. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIP1_TRIAN
AccessionPrimary (citable) accession number: P56626
Secondary accession number(s): Q9ZQY7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 30, 2000
Last modified: May 31, 2011
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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