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P02881

- MONA_DIOCU

UniProt

P02881 - MONA_DIOCU

Protein

Monellin chain A

Gene
N/A
Organism
Dioscoreophyllum cumminsii (Serendipity berry) (Rhopalandria cumminsii)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Taste-modifying protein; intensely sweet-tasting protein.

    Keywords - Molecular functioni

    Taste-modifying protein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Monellin chain A
    Alternative name(s):
    Monellin chain I
    OrganismiDioscoreophyllum cumminsii (Serendipity berry) (Rhopalandria cumminsii)
    Taxonomic identifieri3457 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesMenispermaceaeTinosporoideaeDioscoreophyllum

    Pathology & Biotechi

    Biotechnological usei

    Natural monellin has not been mass marketed to the food industry, primarily due to the challenge of large-scale purification of the protein which is relatively sensitive to heat or acid treatment.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4545Monellin chain APRO_0000207165Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of an A chain and a B chain.

    Protein-protein interaction databases

    MINTiMINT-1542282.

    Structurei

    Secondary structure

    1
    45
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1512
    Beta strandi18 – 2710
    Turni28 – 303
    Beta strandi33 – 397

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FA3NMR-A1-45[»]
    1FUWNMR-A2-42[»]
    1IV7X-ray1.82A/B1-45[»]
    1IV9X-ray1.90A/B1-45[»]
    1KRLX-ray1.90A/C2-45[»]
    1M9GNMR-A1-45[»]
    1MNLNMR-A1-45[»]
    2GPKmodel-B2-45[»]
    3MONX-ray2.80A/C/E/G2-45[»]
    3PXMX-ray1.80A/B2-45[»]
    3PYJX-ray2.00A2-45[»]
    3Q2PX-ray2.34A/B/C/D2-45[»]
    4MONX-ray2.30A/C1-45[»]
    ProteinModelPortaliP02881.
    SMRiP02881. Positions 1-45.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02881.

    Family & Domainsi

    Family and domain databases

    InterProiIPR015283. Monellin.
    IPR000828. Monellin_A.
    [Graphical view]
    PfamiPF09200. Monellin. 1 hit.
    [Graphical view]
    PRINTSiPR00630. MONELLINA.

    Sequencei

    Sequence statusi: Complete.

    P02881-1 [UniParc]FASTAAdd to Basket

    « Hide

    FREIKGYEYQ LYVYASDKLF RADISEDYKT RGRKLLRFNG PVPPP        45
    Length:45
    Mass (Da):5,398
    Last modified:July 21, 1986 - v1
    Checksum:iE086DF18521EC5B6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231D → N AA sequence (PubMed:962914)Curated
    Sequence conflicti26 – 272ED → QN AA sequence (PubMed:962914)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1 – 11Missing in 90% of the chains.

    Sequence databases

    PIRiJH0209. MLDIA.

    Cross-referencesi

    Sequence databases

    PIRi JH0209. MLDIA.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FA3 NMR - A 1-45 [» ]
    1FUW NMR - A 2-42 [» ]
    1IV7 X-ray 1.82 A/B 1-45 [» ]
    1IV9 X-ray 1.90 A/B 1-45 [» ]
    1KRL X-ray 1.90 A/C 2-45 [» ]
    1M9G NMR - A 1-45 [» ]
    1MNL NMR - A 1-45 [» ]
    2GPK model - B 2-45 [» ]
    3MON X-ray 2.80 A/C/E/G 2-45 [» ]
    3PXM X-ray 1.80 A/B 2-45 [» ]
    3PYJ X-ray 2.00 A 2-45 [» ]
    3Q2P X-ray 2.34 A/B/C/D 2-45 [» ]
    4MON X-ray 2.30 A/C 1-45 [» ]
    ProteinModelPortali P02881.
    SMRi P02881. Positions 1-45.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1542282.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P02881.

    Family and domain databases

    InterProi IPR015283. Monellin.
    IPR000828. Monellin_A.
    [Graphical view ]
    Pfami PF09200. Monellin. 1 hit.
    [Graphical view ]
    PRINTSi PR00630. MONELLINA.
    ProtoNeti Search...

    Publicationsi

    1. "Complete amino acid sequence of the sweet protein monellin."
      Kohmura M., Nio N., Ariyoshi Y.
      Agric. Biol. Chem. 54:2219-2224(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "The complete amino acid sequences of both subunits of the sweet protein monellin."
      Frank G., Zuber H.
      Hoppe-Seyler's Z. Physiol. Chem. 357:585-592(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    3. "Mass spectrometric sequencing of proteins. The structure of subunit I of monellin."
      Hudson G., Biemann K.
      Biochem. Biophys. Res. Commun. 71:212-220(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    4. "The structure of monellin and its relation to the sweetness of the protein."
      Bohak Z., Li S.-L.
      Biochim. Biophys. Acta 427:153-170(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-28.
    5. "Crystal structure of the intensely sweet protein monellin."
      Ogata C., Hatada M., Tomlinson G., Shin W.-C., Kim S.-H.
      Nature 328:739-742(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    6. "Structure of monellin refined to 2.3-A resolution in the orthorhombic crystal form."
      Bujacz G., Miller M., Harrison R., Thanki N., Gilliland G.L., Ogata C., Kim S.-H., Wlodawer A.
      Acta Crystallogr. D 53:713-719(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    7. "Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors."
      Murzin A.G.
      J. Mol. Biol. 230:689-694(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO CYSTATINS.

    Entry informationi

    Entry nameiMONA_DIOCU
    AccessioniPrimary (citable) accession number: P02881
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 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

    External Data

    Dasty 3