[1]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. TISSUE=Fruit; DOI=10.1016/0378-1119(95)00198-F; PubMed=7665074 [NCBI, ExPASy, EBI, Israel, Japan] Masuda Y., Nirasawa S., Nakaya K., Kurihara Y.; "Cloning and sequencing of a cDNA encoding a taste-modifying protein, miraculin."; Gene 161:175-177(1995).
[2]	PROTEIN SEQUENCE OF 30-220. PubMed=2708331 [NCBI, ExPASy, EBI, Israel, Japan] Theerasilp S., Hitotsuya H., Nakajo S., Nakaja K., Nakamura Y., Kurihara Y.; "Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin."; J. Biol. Chem. 264:6655-6659(1989).
[3]	PROTEIN SEQUENCE OF 30-50. PubMed=3403544 [NCBI, ExPASy, EBI, Israel, Japan] Theerasilp S., Kurihara Y.; "Complete purification and characterization of the taste-modifying protein, miraculin, from miracle fruit."; J. Biol. Chem. 263:11536-11539(1988).
[4]	DISULFIDE BONDS. DOI=10.1016/0167-4838(91)90073-9; PubMed=1911854 [NCBI, ExPASy, EBI, Israel, Japan] Igeta H., Tamura Y., Nakaya K., Nakmura Y., Kurihara Y.; "Determination of disulfide array and subunit structure of taste-modifying protein, miraculin."; Biochim. Biophys. Acta 1079:303-307(1991).
[5]	GLYCOSYLATION AT ASN-71 AND ASN-215. PubMed=2335505 [NCBI, ExPASy, EBI, Israel, Japan] Takahashi N., Hitotsuya H., Hanzawa H., Arata Y., Kurihara Y.; "Structural study of asparagine-linked oligosaccharide moiety of taste-modifying protein, miraculin."; J. Biol. Chem. 265:7793-7798(1990).

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: Homotetramer; dimer of homodimer.
TISSUE SPECIFICITY: Expressed in fruit pulp after pollination. Not expressed in seeds, stems or leaves.
PTM: Glycosylated; contains as much as 13,9% of sugars (glucosamine, mannose, galactose, xylose, and fucose).
SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-type inhibitor) family [view classification].
WEB RESOURCE: Name=Protein Spotlight; Note=The sweet side of life - Issue 17 of December 2001; URL="http://www.expasy.org/spotlight/back_issues/sptlt017.shtml";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D38598; BAA07603.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC4232; A33872.

3D structure databases

HSSP

P01070; 1AVU. [HSSP ENTRY / PDB]

ModBase

P13087.

PTM databases

GlycoSuiteDB

P13087; -.

Ontologies

GO:0004866;	Molecular function: endopeptidase inhibitor activity (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002160; Prot_inh_Kunz-lg.
Graphical view of domain structure.

Pfam

PF00197; Kunitz_legume; 1.
Pfam graphical view of domain structure.

PRINTS

PR00291; KUNITZINHBTR.

ProDom

PD000891; Prot_inh_Kunz-lg; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00452; STI; 1.
SMART graphical view of domain structure.

PROSITE

PS00283; SOYBEAN_KUNITZ; 1.

ProtoNet

P13087.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Signal; Taste-modifying protein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 29`	`29`
`CHAIN`	`30 220`	`191`	`Miraculin.`	`PRO_0000016935`
`CARBOHYD`	`71 71`		`N-linked (GlcNAc...) [GlycoSuiteDB].`	`CAR_000132`
`CARBOHYD`	`215 215`		`N-linked (GlcNAc...) [GlycoSuiteDB].`	`CAR_000133`
`DISULFID`	`76 121`
`DISULFID`	`167 167`		`Interchain.`
`DISULFID`	`177 188`
`DISULFID`	`181 184`
`CONFLICT`	`129 129`		`W -> S (in Ref. 2; AA sequence).`

Sequence information

Length: 220 AA [This is the length of the unprocessed precursor]

Molecular weight: 24367 Da [This is the MW of the unprocessed precursor]

CRC64: BD7E70CE1AAEE520 [This is a checksum on the sequence]

        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

P13087 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools