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P02882

- MONB_DIOCU

UniProt

P02882 - MONB_DIOCU

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Protein

Monellin chain B

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

Functioni

Taste-modifying protein; intensely sweet-tasting protein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei41 – 411Blocking, abolishes the sweet taste

Keywords - Molecular functioni

Taste-modifying protein

Names & Taxonomyi

Protein namesi
Recommended name:
Monellin chain B
Alternative name(s):
Monellin chain II
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 – 5050Monellin chain BPRO_0000207166Add
BLAST

Interactioni

Subunit structurei

Heterodimer of an A chain and a B chain.

Protein-protein interaction databases

MINTiMINT-1542289.

Structurei

Secondary structure

1
50
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63
Helixi10 – 2617
Beta strandi28 – 303
Beta strandi34 – 4714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FA3NMR-A1-48[»]
1FUWNMR-A1-48[»]
1IV7X-ray1.82A/B1-48[»]
1IV9X-ray1.90A/B1-50[»]
1KRLX-ray1.90B/D1-50[»]
1M9GNMR-A1-48[»]
1MNLNMR-A1-48[»]
1MOLX-ray1.70A/B1-48[»]
2O9UX-ray1.15X1-48[»]
3MONX-ray2.80B/D/F/H1-48[»]
3PXMX-ray1.80A/B1-48[»]
3PYJX-ray2.00A1-48[»]
3Q2PX-ray2.34A/B/C/D1-48[»]
4MONX-ray2.30B/D1-48[»]
ProteinModelPortaliP02882.
SMRiP02882. Positions 1-50.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02882.

Family & Domainsi

Family and domain databases

InterProiIPR015283. Monellin.
IPR002095. Monellin_B.
[Graphical view]
PfamiPF09200. Monellin. 1 hit.
[Graphical view]
PRINTSiPR00631. MONELLINB.

Sequencei

Sequence statusi: Complete.

P02882-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
GEWEIIDIGP FTQNLGKFAV DEENKIGQYG RLTFNKVIRP CMKKTIYEEN
Length:50
Mass (Da):5,835
Last modified:August 1, 1991 - v2
Checksum:iF08396DFCD480C81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 502EN → NE AA sequence (PubMed:964918)Curated

Sequence databases

PIRiJH0210. MLDIB.

Cross-referencesi

Sequence databases

PIRi JH0210. MLDIB.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FA3 NMR - A 1-48 [» ]
1FUW NMR - A 1-48 [» ]
1IV7 X-ray 1.82 A/B 1-48 [» ]
1IV9 X-ray 1.90 A/B 1-50 [» ]
1KRL X-ray 1.90 B/D 1-50 [» ]
1M9G NMR - A 1-48 [» ]
1MNL NMR - A 1-48 [» ]
1MOL X-ray 1.70 A/B 1-48 [» ]
2O9U X-ray 1.15 X 1-48 [» ]
3MON X-ray 2.80 B/D/F/H 1-48 [» ]
3PXM X-ray 1.80 A/B 1-48 [» ]
3PYJ X-ray 2.00 A 1-48 [» ]
3Q2P X-ray 2.34 A/B/C/D 1-48 [» ]
4MON X-ray 2.30 B/D 1-48 [» ]
ProteinModelPortali P02882.
SMRi P02882. Positions 1-50.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1542289.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P02882.

Family and domain databases

InterProi IPR015283. Monellin.
IPR002095. Monellin_B.
[Graphical view ]
Pfami PF09200. Monellin. 1 hit.
[Graphical view ]
PRINTSi PR00631. MONELLINB.
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. "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.
  4. "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).
  5. "Two crystal structures of a potently sweet protein. Natural monellin at 2.75-A resolution and single-chain monellin at 1.7-A resolution."
    Somoza J.R., Jiang F., Tong L., Kang C.-H., Cho J.M., Kim S.-H.
    J. Mol. Biol. 234:390-404(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 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 nameiMONB_DIOCU
AccessioniPrimary (citable) accession number: P02882
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: October 1, 2014
This is version 82 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

External Data

Dasty 3