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

P13087 (MIRA_SYNDU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Miraculin has the property of modifying a sour taste into a sweet taste. This alteration of taste perception persists for many minutes.

Subunit structure

Homotetramer; dimer of homodimer.

Tissue specificity

Expressed in fruit pulp after pollination. Not expressed in seeds, stems or leaves. Ref.1

Post-translational modification

Glycosylated; contains as much as 13,9% of sugars (glucosamine, mannose, galactose, xylose, and fucose). Ref.5

Sequence similarities

Belongs to the protease inhibitor I3 (leguminous Kunitz-type inhibitor) family. [View classification]

Ontologies

Keywords
   DomainSignal
   Molecular functionTaste-modifying protein
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionendopeptidase inhibitor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.2 Ref.3
Chain30 – 220191Miraculin
PRO_0000016935

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Ref.5
CAR_000132
Glycosylation2151N-linked (GlcNAc...) Ref.5
CAR_000133
Disulfide bond76 ↔ 121 Ref.4
Disulfide bond167Interchain Ref.4
Disulfide bond177 ↔ 188 Ref.4
Disulfide bond181 ↔ 184 Ref.4

Experimental info

Sequence conflict1291W → S AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P13087 [UniParc].

Last modified July 15, 1999. Version 3.
Checksum: BD7E70CE1AAEE520

FASTA22024,367
        10         20         30         40         50         60 
MKELTMLSLS FFFVSALLAA AANPLLSAAD SAPNPVLDID GEKLRTGTNY YIVPVLRDHG 

        70         80         90        100        110        120 
GGLTVSATTP NGTFVCPPRV VQTRKEVDHD RPLAFFPENP KEDVVRVSTD LNINFSAFMP 

       130        140        150        160        170        180 
CRWTSSTVWR LDKYDESTGQ YFVTIGGVKG NPGPETISSW FKIEEFCGSG FYKLVFCPTV 

       190        200        210        220 
CGSCKVKCGD VGIYIDQKGR RRLALSDKPF AFEFNKTVYF 

« Hide

References

[1]"Cloning and sequencing of a cDNA encoding a taste-modifying protein, miraculin."
Masuda Y., Nirasawa S., Nakaya K., Kurihara Y.
Gene 161:175-177(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Fruit.
[2]"Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin."
Theerasilp S., Hitotsuya H., Nakajo S., Nakaja K., Nakamura Y., Kurihara Y.
J. Biol. Chem. 264:6655-6659(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-220.
[3]"Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit."
Theerasilp S., Kurihara Y.
J. Biol. Chem. 263:11536-11539(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-50.
[4]"Determination of disulfide array and subunit structure of taste-modifying protein, miraculin."
Igeta H., Tamura Y., Nakaya K., Nakmura Y., Kurihara Y.
Biochim. Biophys. Acta 1079:303-307(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[5]"Structural study of asparagine-linked oligosaccharide moiety of taste-modifying protein, miraculin."
Takahashi N., Hitotsuya H., Hanzawa H., Arata Y., Kurihara Y.
J. Biol. Chem. 265:7793-7798(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-71 AND ASN-215.

Web resources

Protein Spotlight

The sweet side of life - Issue 17 of December 2001

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38598 mRNA. Translation: BAA07603.1.
PIRA33872. JC4232.

3D structure databases

ProteinModelPortalP13087.
ModBaseSearch...
MobiDBSearch...

PTM databases

UniCarbKBP13087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011065. Kunitz_inhibitor_ST1-like.
IPR002160. Prot_inh_Kunz-lg.
[Graphical view]
PfamPF00197. Kunitz_legume. 1 hit.
[Graphical view]
PRINTSPR00291. KUNITZINHBTR.
SMARTSM00452. STI. 1 hit.
[Graphical view]
SUPFAMSSF50386. SSF50386. 1 hit.
PROSITEPS00283. SOYBEAN_KUNITZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMIRA_SYNDU
AccessionPrimary (citable) accession number: P13087
Secondary accession number(s): Q41153
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 15, 1999
Last modified: April 16, 2014
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries