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P19667 (CURC1_CURLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Curculin-1
Alternative name(s):
Neoculin basic subunit
Short name=NBS
Gene names
Name:CUR09
Synonyms:CUR37
OrganismCurculigo latifolia (Lumbah)
Taxonomic identifier4676 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Asparagales › Hypoxidaceae › Molineria

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Taste-modifying protein; sweet-tasting. After curculin, water elicits a sweet taste, and sour substances induce a stronger sense of sweetness.

Subunit structure

Homodimer and heterodimer with curculin-2; Disulfide-linked. Ref.3

Sequence similarities

Contains 1 bulb-type lectin domain.

Ontologies

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.2
Chain23 – 136114Curculin-1
PRO_0000021042
Propeptide137 – 15822
PRO_0000021043

Regions

Domain23 – 131109Bulb-type lectin

Amino acid modifications

Disulfide bond51 ↔ 74 Ref.3 Ref.4
Disulfide bond99Interchain (with C-131) Ref.3 Ref.4
Disulfide bond131Interchain (with C-99) Ref.3 Ref.4

Experimental info

Sequence conflict501K → N AA sequence Ref.2
Sequence conflict951W → N AA sequence Ref.2
Sequence conflict1001W → C AA sequence Ref.2
Sequence conflict1031N → A AA sequence Ref.2

Secondary structure

1 ............................. 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19667 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 65B51E742D34706E

FASTA15817,223
        10         20         30         40         50         60 
MAAKFLLTIL VTFAAVASLG MADNVLLSGQ TLHADHSLQA GAYTLTIQNK CNLVKYQNGR 

        70         80         90        100        110        120 
QIWASNTDRR GSGCRLTLLS DGNLVIYDHN NNDVWGSACW GDNGKYALVL QKDGRFVIYG 

       130        140        150 
PVLWSLGPNG CRRVNGGITV AKDSTEPQHE DIKMVINN

« Hide

References

[1]"Molecular cloning of curculin, a novel taste-modifying protein with a sweet taste."
Abe K., Yamashita H., Arai S., Kurihara Y.
Biochim. Biophys. Acta 1130:232-234(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Purification and complete amino acid sequence of a new type of sweet protein taste-modifying activity, curculin."
Yamashita H., Theerasilp S., Aiuchi T., Nakaya K., Nakamura Y., Kurihara Y.
J. Biol. Chem. 265:15770-15775(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-136.
Tissue: Fruit.
[3]"Crystal structure of neoculin: insights into its sweetness and taste-modifying activity."
Shimizu-Ibuka A., Morita Y., Terada T., Asakura T., Nakajima K., Iwata S., Misaka T., Sorimachi H., Arai S., Abe K.
J. Mol. Biol. 359:148-158(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 23-136 IN COMPLEX WITH NAS, SUBUNIT, DISULFIDE BONDS.
[4]"Curculin exhibits sweet-tasting and taste-modifying activities through its distinct molecular surfaces."
Kurimoto E., Suzuki M., Amemiya E., Yamaguchi Y., Nirasawa S., Shimba N., Xu N., Kashiwagi T., Kawai M., Suzuki E., Kato K.
J. Biol. Chem. 282:33252-33256(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 23-136, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X64110 mRNA. Translation: CAA45476.1.
X64111 mRNA. Translation: CAA45477.1.
PIRS22365.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D04X-ray2.76B/D/F/H23-136[»]
2DPFX-ray1.50A/B/C/D23-136[»]
ProteinModelPortalP19667.
SMRP19667. Positions 23-133.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.90.10.10. 1 hit.
InterProIPR001480. Bulb-type_lectin_dom.
[Graphical view]
PfamPF01453. B_lectin. 1 hit.
[Graphical view]
SMARTSM00108. B_lectin. 1 hit.
[Graphical view]
SUPFAMSSF51110. B_lectin. 1 hit.
PROSITEPS50927. BULB_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19667.

Entry information

Entry nameCURC1_CURLA
AccessionPrimary (citable) accession number: P19667
Secondary accession number(s): Q39530, Q39531
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 15, 1998
Last modified: April 3, 2013
This is version 66 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

SIMILARITY comments

Index of protein domains and families

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