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Protein

Ribosome-inactivating protein momordin I

Gene
N/A
Organism
Momordica charantia (Bitter gourd) (Balsam pear)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei183 – 1831

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein synthesis inhibitor, Toxin

Keywords - Biological processi

Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome-inactivating protein momordin I (EC:3.2.2.22)
Alternative name(s):
Alpha-momorcharin
Short name:
Alpha-MMC
rRNA N-glycosidase
OrganismiMomordica charantia (Bitter gourd) (Balsam pear)
Taxonomic identifieri3673 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeMomordiceaeMomordica

Pathology & Biotechi

Protein family/group databases

Allergomei2800. Mom c RIP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23232 PublicationsAdd
BLAST
Chaini24 – 269246Ribosome-inactivating protein momordin IPRO_0000030770Add
BLAST
Propeptidei270 – 28617Removed in mature formPRO_0000030771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi250 – 2501N-linked (GlcNAc...)CAR_000082

Keywords - PTMi

Glycoprotein

PTM databases

UniCarbKBiP16094.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 317Combined sources
Helixi34 – 4714Combined sources
Beta strandi50 – 545Combined sources
Beta strandi57 – 604Combined sources
Helixi66 – 694Combined sources
Beta strandi70 – 767Combined sources
Beta strandi82 – 887Combined sources
Turni89 – 913Combined sources
Beta strandi94 – 996Combined sources
Beta strandi102 – 1054Combined sources
Helixi109 – 1146Combined sources
Turni115 – 1173Combined sources
Beta strandi123 – 1275Combined sources
Helixi134 – 1418Combined sources
Helixi145 – 1473Combined sources
Helixi152 – 16211Combined sources
Helixi167 – 18620Combined sources
Helixi188 – 1958Combined sources
Beta strandi198 – 2003Combined sources
Helixi206 – 22520Combined sources
Turni226 – 2305Combined sources
Beta strandi231 – 2388Combined sources
Beta strandi242 – 2443Combined sources
Beta strandi246 – 2505Combined sources
Helixi254 – 2585Combined sources
Helixi266 – 2683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP16094.
SMRiP16094. Positions 24-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16094.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. 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]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SUPFAMiSSF56371. SSF56371. 1 hit.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16094-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRFSVLSFL ILAIFLGGSI VKGDVSFRLS GADPRSYGMF IKDLRNALPF
60 70 80 90 100
REKVYNIPLL LPSVSGAGRY LLMHLFNYDG KTITVAVDVT NVYIMGYLAD
110 120 130 140 150
TTSYFFNEPA AELASQYVFR DARRKITLPY SGNYERLQIA AGKPREKIPI
160 170 180 190 200
GLPALDSAIS TLLHYDSTAA AGALLVLIQT TAEAARFKYI EQQIQERAYR
210 220 230 240 250
DEVPSLATIS LENSWSGLSK QIQLAQGNNG IFRTPIVLVD NKGNRVQITN
260 270 280
VTSKVVTSNI QLLLNTRNIA EGDNGDVSTT HGFSSY
Length:286
Mass (Da):31,532
Last modified:December 1, 1992 - v2
Checksum:iE1B013ABEBC216CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57682 mRNA. Translation: CAA40869.1.
PIRiS14273. RLPUGG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57682 mRNA. Translation: CAA40869.1.
PIRiS14273. RLPUGG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP16094.
SMRiP16094. Positions 24-269.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei2800. Mom c RIP.

PTM databases

UniCarbKBiP16094.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP16094.

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. 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]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SUPFAMiSSF56371. SSF56371. 1 hit.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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).

Entry informationi

Entry nameiRIP1_MOMCH
AccessioniPrimary (citable) accession number: P16094
Secondary accession number(s): P24697
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 1, 1992
Last modified: November 26, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.