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Protein

Monellin chain A

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

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 – 1512Combined sources
Beta strandi18 – 2710Combined sources
Turni28 – 303Combined sources
Beta strandi33 – 397Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40 
FREIKGYEYQ LYVYASDKLF RADISEDYKT RGRKLLRFNG PVPPP
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

PIRiJH0209. MLDIA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

MINTiMINT-1542282.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02881.

Family and domain databases

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

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: May 27, 2015
This is version 81 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

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.