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Reviewed, UniProtKB/Swiss-Prot Q6EH50 (RIP4_PHYHE)

Last modified March 3, 2009. Version 21. 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:
    Heterotepalin-4
    EC=3.2.2.22
Alternative name(s):
    Ribosome-inactivating protein
    rRNA N-glycosidase
Gene names
Name: RIP1
OrganismPhytolacca heterotepala (Mexican pokeweed)
Taxonomic identifier248308 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesPhytolaccaceaePhytolacca

Protein attributes

Sequence length312 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 in vitro. Ref.2

Catalytic activity

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. Ref.2

Sequence similarities

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

Mass spectrometry

Molecular mass is 29326 Da from positions 23 - 283. Determined by ESI. Ref.2

Ontologies

Keywords
   Biological processPlant defense
   DomainSignal
   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 Ref.2

Inferred from direct assay. Source: UniProtKB

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionrRNA N-glycosylase activity Ref.2

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.2
Chain23 – 283261Heterotepalin-4 Ref.2
PRO_0000352792
Propeptide284 – 31229 Ref.2
PRO_0000352793

Sites

Active site1971 By similarity UniProtKB P20656

Amino acid modifications

Disulfide bond56 ↔ 280 By similarity UniProtKB P10297
Disulfide bond107 ↔ 128 By similarity UniProtKB P10297

Experimental info

Sequence conflict2661I → M in AAQ95991. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6EH50-1 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 4C55B0D9FB8F189B

FASTA31235,153
        10         20         30         40         50         60 
MKSMLVVTIS VWLILAPTST WAVNTIIYNV GSTTISKYAT FLDDLRNEAK DPNLKCYGIP 

        70         80         90        100        110        120 
MLPNTNSNPK YVLVELQGSN KKTITLMLRR NNLYVMGYSD PFDTSKCRYH IFNDISGTER 

       130        140        150        160        170        180 
QDVETTLCPN SNSRVSKNIN YDSRYPTLES KVGVKSRSQV QLGIQILDSD IGKISGVTSF 

       190        200        210        220        230        240 
SEKTEAEFLL VAIQISEAAR FKYIENQVKT NFNRAFNPNP KVLNLEETWG KISTAIHDAK 

       250        260        270        280        290        300 
NGVLPKPLEL VDASGAKWIV LRVDEIKPDV ALLNYVSGSC QTTYNQNAMF PQLIMSTYYN 

       310 
YMANLGDLFE EF 

« Hide

References

[1]Delli Bovi P., Corrado G.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and characterization of heterotepalins, type 1 ribosome-inactivating proteins from Phytolacca heterotepala leaves."
Di Maro A., Chambery A., Daniele A., Casoria P., Parente A.
Phytochemistry 68:767-776(2007) [PubMed: 17258249] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-37; 38-46; 71-81; 91-106; 109-120; 145-151; 158-173; 174-183; 203-209; 222-231; 232-240; 247-257 AND 262-283, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY.
Tissue: Leaf.

Cross-references

Sequence databases

AY327475 mRNA. Translation: AAQ95991.1.

3D structure databases

SMRQ6EH50. Positions 23-283.
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.
IPR016331. Shiga-like_toxin_subunit_A.
[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]
PIRSFPIRSF001924. Shigella_toxin_subunit_A. 1 hit.
PRINTSPR00396. SHIGARICIN.
PROSITEPS00275. SHIGA_RICIN. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIP4_PHYHE
AccessionPrimary (citable) accession number: Q6EH50
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 14, 2008
Last modified: March 3, 2009
This is version 21 of the entry and version 2 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