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P16094

- RIP1_MOMCH

UniProt

P16094 - RIP1_MOMCH

Protein

Ribosome-inactivating protein momordin I

Gene
N/A
Organism
Momordica charantia (Bitter gourd) (Balsam pear)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (01 Dec 1992)
      Previous versions | rss
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    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

    1. rRNA N-glycosylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. defense response Source: UniProtKB-KW
    2. negative regulation of translation Source: UniProtKB-KW

    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 – 317
    Helixi34 – 4714
    Beta strandi50 – 545
    Beta strandi57 – 604
    Helixi66 – 694
    Beta strandi70 – 767
    Beta strandi82 – 887
    Turni89 – 913
    Beta strandi94 – 996
    Beta strandi102 – 1054
    Helixi109 – 1146
    Turni115 – 1173
    Beta strandi123 – 1275
    Helixi134 – 1418
    Helixi145 – 1473
    Helixi152 – 16211
    Helixi167 – 18620
    Helixi188 – 1958
    Beta strandi198 – 2003
    Helixi206 – 22520
    Turni226 – 2305
    Beta strandi231 – 2388
    Beta strandi242 – 2443
    Beta strandi246 – 2505
    Helixi254 – 2585
    Helixi266 – 2683

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MSRFSVLSFL ILAIFLGGSI VKGDVSFRLS GADPRSYGMF IKDLRNALPF    50
    REKVYNIPLL LPSVSGAGRY LLMHLFNYDG KTITVAVDVT NVYIMGYLAD 100
    TTSYFFNEPA AELASQYVFR DARRKITLPY SGNYERLQIA AGKPREKIPI 150
    GLPALDSAIS TLLHYDSTAA AGALLVLIQT TAEAARFKYI EQQIQERAYR 200
    DEVPSLATIS LENSWSGLSK QIQLAQGNNG IFRTPIVLVD NKGNRVQITN 250
    VTSKVVTSNI QLLLNTRNIA EGDNGDVSTT HGFSSY 286
    Length:286
    Mass (Da):31,532
    Last modified:December 1, 1992 - v2
    Checksum:iE1B013ABEBC216CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57682 mRNA. Translation: CAA40869.1.
    PIRiS14273. RLPUGG.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57682 mRNA. Translation: CAA40869.1 .
    PIRi S14273. RLPUGG.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AHA X-ray 2.20 A 24-269 [» ]
    1AHB X-ray 2.20 A 24-269 [» ]
    1AHC X-ray 2.00 A 24-269 [» ]
    1F8Q X-ray 2.20 A 24-286 [» ]
    1MOM X-ray 2.16 A 24-269 [» ]
    1MRG X-ray 1.80 A 24-286 [» ]
    1MRH X-ray 2.00 A 24-286 [» ]
    1MRI X-ray 2.20 A 24-286 [» ]
    ProteinModelPortali P16094.
    SMRi P16094. Positions 24-269.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00173. Adenine.

    Protein family/group databases

    Allergomei 2800. Mom c RIP.

    PTM databases

    UniCarbKBi P16094.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P16094.

    Family and domain databases

    Gene3Di 3.40.420.10. 1 hit.
    4.10.470.10. 1 hit.
    InterProi IPR001574. 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 ]
    Pfami PF00161. RIP. 1 hit.
    [Graphical view ]
    PRINTSi PR00396. SHIGARICIN.
    SUPFAMi SSF56371. SSF56371. 1 hit.
    PROSITEi PS00275. SHIGA_RICIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 91 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