Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P02882 (MONB_DIOCU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Monellin chain B
Alternative name(s):
Monellin chain II
OrganismDioscoreophyllum cumminsii (Serendipity berry) (Rhopalandria cumminsii)
Taxonomic identifier3457 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesMenispermaceaeTinosporoideaeDioscoreophyllum

Protein attributes

Sequence length50 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Taste-modifying protein; intensely sweet-tasting protein.

Subunit structure

Heterodimer of an A chain and a B chain.

Biotechnological use

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.

Ontologies

Keywords
   Molecular functionTaste-modifying protein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5050Monellin chain B
PRO_0000207166

Sites

Site411Blocking, abolishes the sweet taste

Experimental info

Sequence conflict49 – 502EN → NE AA sequence Ref.2

Secondary structure

......... 50
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02882 [UniParc].

Last modified August 1, 1991. Version 2.
Checksum: F08396DFCD480C81

FASTA505,835
        10         20         30         40         50 
GEWEIIDIGP FTQNLGKFAV DEENKIGQYG RLTFNKVIRP CMKKTIYEEN 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRMLDIB. JH0210.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP02882.
SMRP02882. Positions 1-50.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1542289.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR015283. Monellin.
IPR002095. Monellin_B.
[Graphical view]
PfamPF09200. Monellin. 1 hit.
[Graphical view]
PRINTSPR00631. MONELLINB.
ProtoNetSearch...

Other

EvolutionaryTraceP02882.

Entry information

Entry nameMONB_DIOCU
AccessionPrimary (citable) accession number: P02882
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references