Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Miraculin

Gene
N/A
Organism
Synsepalum dulcificum (Miracle fruit) (Richadella dulcifica)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. endopeptidase inhibitor activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Taste-modifying protein

Protein family/group databases

MEROPSiI03.030.

Names & Taxonomyi

Protein namesi
Recommended name:
Miraculin
Short name:
MIR
OrganismiSynsepalum dulcificum (Miracle fruit) (Richadella dulcifica)
Taxonomic identifieri3743 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridsEricalesSapotaceaeSynsepalum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29292 PublicationsAdd
BLAST
Chaini30 – 220191MiraculinPRO_0000016935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi71 – 711N-linked (GlcNAc...)1 PublicationCAR_000132
Disulfide bondi76 ↔ 1211 Publication
Disulfide bondi167 – 167Interchain1 Publication
Disulfide bondi177 ↔ 1881 Publication
Disulfide bondi181 ↔ 1841 Publication
Glycosylationi215 – 2151N-linked (GlcNAc...)1 PublicationCAR_000133

Post-translational modificationi

Glycosylated; contains as much as 13,9% of sugars (glucosamine, mannose, galactose, xylose, and fucose).1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP13087.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homotetramer; dimer of homodimer.

Structurei

3D structure databases

ProteinModelPortaliP13087.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR011065. Kunitz_inhibitor_ST1-like.
IPR002160. Prot_inh_Kunz-lg.
[Graphical view]
PfamiPF00197. Kunitz_legume. 1 hit.
[Graphical view]
PRINTSiPR00291. KUNITZINHBTR.
SMARTiSM00452. STI. 1 hit.
[Graphical view]
SUPFAMiSSF50386. SSF50386. 1 hit.
PROSITEiPS00283. SOYBEAN_KUNITZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKELTMLSLS FFFVSALLAA AANPLLSAAD SAPNPVLDID GEKLRTGTNY
60 70 80 90 100
YIVPVLRDHG GGLTVSATTP NGTFVCPPRV VQTRKEVDHD RPLAFFPENP
110 120 130 140 150
KEDVVRVSTD LNINFSAFMP CRWTSSTVWR LDKYDESTGQ YFVTIGGVKG
160 170 180 190 200
NPGPETISSW FKIEEFCGSG FYKLVFCPTV CGSCKVKCGD VGIYIDQKGR
210 220
RRLALSDKPF AFEFNKTVYF
Length:220
Mass (Da):24,367
Last modified:July 15, 1999 - v3
Checksum:iBD7E70CE1AAEE520
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291W → S AA sequence (PubMed:2708331).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38598 mRNA. Translation: BAA07603.1.
PIRiJC4232. A33872.

Cross-referencesi

Web resourcesi

Protein Spotlight

The sweet side of life - Issue 17 of December 2001

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38598 mRNA. Translation: BAA07603.1.
PIRiJC4232. A33872.

3D structure databases

ProteinModelPortaliP13087.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI03.030.

PTM databases

UniCarbKBiP13087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR011065. Kunitz_inhibitor_ST1-like.
IPR002160. Prot_inh_Kunz-lg.
[Graphical view]
PfamiPF00197. Kunitz_legume. 1 hit.
[Graphical view]
PRINTSiPR00291. KUNITZINHBTR.
SMARTiSM00452. STI. 1 hit.
[Graphical view]
SUPFAMiSSF50386. SSF50386. 1 hit.
PROSITEiPS00283. SOYBEAN_KUNITZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiMIRA_SYNDU
AccessioniPrimary (citable) accession number: P13087
Secondary accession number(s): Q41153
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 15, 1999
Last modified: October 29, 2014
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

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.