Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P85208 (RIPD2_PHYDI)

Last modified June 16, 2009. Version 2. 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:
    Dioicin-2
    EC=3.2.2.22
Alternative name(s):
    Ribosome-inactivating protein
    rRNA N-glycosidase
OrganismPhytolacca dioica (Bella sombra tree) (Phytolacca arborea)
Taxonomic identifier29725 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesPhytolaccaceaePhytolacca

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Nicks pBR322 dsDNA. Has adenine polynucleotide glycosidase activity on herring sperm ssDNA. Ref.1

Catalytic activity

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. Ref.1

Subcellular location

Secretedextracellular space. Golgi apparatus. Vacuole Ref.1.

Developmental stage

Detected in fully expanded leaves of 8 to 34 month old plants, levels peak in autumn. Also present in developing leaves (10-60 days old) of adult plants. Ref.1

Sequence similarities

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

Mass spectrometry

Molecular mass is 29910.00 Da from positions 1 - 266. Determined by ESI. Ref.1

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentGolgi apparatus
Secreted
Vacuole
   Molecular functionHydrolase
Protein synthesis inhibitor
Toxin
   PTMDisulfide bond
   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

   Cellular componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

vacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Chain1 – 266266Dioicin-2
PRO_0000372680

Sites

Active site1761 By similarity UniProtKB P20656

Amino acid modifications

Disulfide bond32 ↔ 263 Ref.1
Disulfide bond85 ↔ 102 Ref.1

Sequences

Sequence LengthMass (Da)Tools
P85208-1 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 3D8363C8CC46C53A

FASTA26629,914
        10         20         30         40         50         60 
NIVFDVENAT PETYSSFLTS LREAVKDKKS TCHGMIMATT TTELPKYVLV DLKLGSEKDA 

        70         80         90        100        110        120 
KTFTLAIRRG NLYLEGYSDI YNEKCRYRIF EDSESDAQQT VCPGDLTLPG SQNKIPYKKS 

       130        140        150        160        170        180 
YQSMESKGGD RTKLGLGQIT LESRMNKIYG KDATDQKQFQ KNEAEFLLIA VQMITEASRF 

       190        200        210        220        230        240 
KYIENKVKDS FDDAIGYKPD PKAISLETSW DKISNAIAKV NTPGNSIVTL PKGLLDENKK 

       250        260 
PWTTATMDEL KNDIMGLLTH VTCKIK 

« Hide

References

[1]"Type 1 ribosome-inactivating proteins from Phytolacca dioica L. leaves: differential seasonal and age expression, and cellular localization."
Parente A., Conforto B., Di Maro A., Chambery A., De Luca P., Bolognesi A., Iriti M., Faoro F.
Planta 228:963-975(2008) [PubMed: 18704492] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MASS SPECTROMETRY, DISULFIDE BONDS.
Tissue: Leaf.

Cross-references

3D structure databases

ModBaseSearch...

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 nameRIPD2_PHYDI
AccessionPrimary (citable) accession number: P85208
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: June 16, 2009
This is version 2 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