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P16094 (RIP1_MOMCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosome-inactivating protein momordin I

EC=3.2.2.22
Alternative name(s):
Alpha-momorcharin
Short name=Alpha-MMC
rRNA N-glycosidase
OrganismMomordica charantia (Bitter gourd) (Balsam pear)
Taxonomic identifier3673 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeMomordiceaeMomordica

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 term3D-structure
Direct 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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.2 Ref.3
Chain24 – 269246Ribosome-inactivating protein momordin I
PRO_0000030770
Propeptide270 – 28617Removed in mature form
PRO_0000030771

Sites

Active site1831

Amino acid modifications

Glycosylation2501N-linked (GlcNAc...)
CAR_000082

Secondary structure

................................................ 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16094 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: E1B013ABEBC216CF

FASTA28631,532
        10         20         30         40         50         60 
MSRFSVLSFL ILAIFLGGSI VKGDVSFRLS GADPRSYGMF IKDLRNALPF REKVYNIPLL 

        70         80         90        100        110        120 
LPSVSGAGRY LLMHLFNYDG KTITVAVDVT NVYIMGYLAD TTSYFFNEPA AELASQYVFR 

       130        140        150        160        170        180 
DARRKITLPY SGNYERLQIA AGKPREKIPI GLPALDSAIS TLLHYDSTAA AGALLVLIQT 

       190        200        210        220        230        240 
TAEAARFKYI EQQIQERAYR DEVPSLATIS LENSWSGLSK QIQLAQGNNG IFRTPIVLVD 

       250        260        270        280 
NKGNRVQITN VTSKVVTSNI QLLLNTRNIA EGDNGDVSTT HGFSSY 

« Hide

References

[1]"Cloning of the cDNA of alpha-momorcharin: a ribosome inactivating protein."
Ho W.K.K., Liu S.C., Shaw P.C., Yeung H.W., Ng T.B., Chan W.Y.
Biochim. Biophys. Acta 1088:311-314(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Seed.
[2]"N-terminal sequence of some ribosome-inactivating proteins."
Montecucchi P.-C., Lazzarini A.M., Barbieri L., Stirpe F., Soria M., Lappi D.
Int. J. Pept. Protein Res. 33:263-267(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-38.
Tissue: Seed.
[3]"Trichokirin, a ribosome-inactivating protein from the seeds of Trichosanthes kirilowii Maximowicz. Purification, partial characterization and use for preparation of immunotoxins."
Casellas P., Dussossoy D., Falasca A.I., Barbieri L., Guillemot J.-C., Ferrara P., Bolognesi A., Cenini P., Stirpe F.
Eur. J. Biochem. 176:581-588(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-70.
Tissue: Seed.
[4]"The N-glycosidase mechanism of ribosome-inactivating proteins implied by crystal structures of alpha-momorcharin."
Ren J., Wang Y., Dong Y., Stuart D.I.
Structure 2:7-16(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]"Crystal structure of momordin, a type I ribosome inactivating protein from the seeds of Momordica charantia."
Husain J., Tickle I.J., Wood S.P.
FEBS Lett. 342:154-158(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS).
[6]"Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins."
Huang Q., Liu S., Tang Y., Jin S., Wang Y.
Biochem. J. 309:285-298(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57682 mRNA. Translation: CAA40869.1.
PIRRLPUGG. S14273.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHAX-ray2.20A24-269[»]
1AHBX-ray2.20A24-269[»]
1AHCX-ray2.00A24-269[»]
1F8QX-ray2.20A24-286[»]
1MOMX-ray2.16A24-269[»]
1MRGX-ray1.80A24-286[»]
1MRHX-ray2.00A24-286[»]
1MRIX-ray2.20A24-286[»]
ProteinModelPortalP16094.
SMRP16094. Positions 24-269.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00173. Adenine.

Protein family/group databases

Allergome2800. Mom c RIP.

PTM databases

UniCarbKBP16094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
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]
PfamPF00161. RIP. 1 hit.
[Graphical view]
PRINTSPR00396. SHIGARICIN.
SUPFAMSSF56371. SSF56371. 1 hit.
PROSITEPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16094.

Entry information

Entry nameRIP1_MOMCH
AccessionPrimary (citable) accession number: P16094
Secondary accession number(s): P24697
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 90 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references