P13087 (MIRA_RICDU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Miraculin Short name=MIR
Organism	Richadella dulcifica (Miracle fruit) (Synsepalum dulcificum)
Taxonomic identifier	3743 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › Ericales › Sapotaceae › Synsepalum

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Domain	Signal
Molecular function	Taste-modifying protein
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	endopeptidase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Ref.2 Ref.3
	Chain	30 – 220	191	Miraculin		PRO_0000016935
Amino acid modifications
	Glycosylation	71	1	N-linked (GlcNAc...) Ref.5		CAR_000132
	Glycosylation	215	1	N-linked (GlcNAc...) Ref.5		CAR_000133
	Disulfide bond	76 ↔ 121		Ref.4
	Disulfide bond	167		Interchain Ref.4
	Disulfide bond	177 ↔ 188		Ref.4
	Disulfide bond	181 ↔ 184		Ref.4
Experimental info
	Sequence conflict	129	1	W → S AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P13087 [UniParc]. Last modified July 15, 1999. Version 3. Checksum: BD7E70CE1AAEE520	FASTA	220	24,367
	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

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: 7665074] [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: 2708331] [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: 3403544] [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: 1911854] [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: 2335505] [Abstract] Cited for: GLYCOSYLATION AT ASN-71 AND ASN-215.
+	Additional computationally mapped references.

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.
PIR	A33872. JC4232.
3D structure databases
ProteinModelPortal	P13087.
ModBase	Search...
PTM databases
GlycoSuiteDB	P13087.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR011065. Kunitz_inhibitor_ST1-like. IPR002160. Prot_inh_Kunz-lg. [Graphical view]
Pfam	PF00197. Kunitz_legume. 1 hit. [Graphical view]
PRINTS	PR00291. KUNITZINHBTR.
SMART	SM00452. STI. 1 hit. [Graphical view]
SUPFAM	SSF50386. Kunitz_like. 1 hit.
PROSITE	PS00283. SOYBEAN_KUNITZ. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MIRA_RICDU

Accession

Primary (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:	September 21, 2011
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program