ID   MIRA_SYNDU              Reviewed;         220 AA.
AC   P13087; Q41153;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 3.
DT   09-APR-2025, entry version 103.
DE   RecName: Full=Miraculin;
DE            Short=MIR;
DE   Flags: Precursor;
OS   Synsepalum dulcificum (Miracle fruit) (Richadella dulcifica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Sapotaceae; Chrysophylloideae; Synsepalum.
OX   NCBI_TaxID=3743;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Fruit;
RX   PubMed=7665074; DOI=10.1016/0378-1119(95)00198-f;
RA   Masuda Y., Nirasawa S., Nakaya K., Kurihara Y.;
RT   "Cloning and sequencing of a cDNA encoding a taste-modifying protein,
RT   miraculin.";
RL   Gene 161:175-177(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 30-220.
RX   PubMed=2708331; DOI=10.1016/s0021-9258(18)83477-9;
RA   Theerasilp S., Hitotsuya H., Nakajo S., Nakaja K., Nakamura Y.,
RA   Kurihara Y.;
RT   "Complete amino acid sequence and structure characterization of the taste-
RT   modifying protein, miraculin.";
RL   J. Biol. Chem. 264:6655-6659(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 30-50.
RX   PubMed=3403544; DOI=10.1016/s0021-9258(18)37991-2;
RA   Theerasilp S., Kurihara Y.;
RT   "Complete purification and characterization of the taste-modifying protein,
RT   miraculin, from miracle fruit.";
RL   J. Biol. Chem. 263:11536-11539(1988).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=1911854; DOI=10.1016/0167-4838(91)90073-9;
RA   Igeta H., Tamura Y., Nakaya K., Nakmura Y., Kurihara Y.;
RT   "Determination of disulfide array and subunit structure of taste-modifying
RT   protein, miraculin.";
RL   Biochim. Biophys. Acta 1079:303-307(1991).
RN   [5]
RP   GLYCOSYLATION AT ASN-71 AND ASN-215.
RX   PubMed=2335505; DOI=10.1016/s0021-9258(19)38998-7;
RA   Takahashi N., Hitotsuya H., Hanzawa H., Arata Y., Kurihara Y.;
RT   "Structural study of asparagine-linked oligosaccharide moiety of taste-
RT   modifying protein, miraculin.";
RL   J. Biol. Chem. 265:7793-7798(1990).
CC   -!- FUNCTION: Miraculin has the property of modifying a sour taste into a
CC       sweet taste. This alteration of taste perception persists for many
CC       minutes.
CC   -!- SUBUNIT: Homotetramer; dimer of homodimer.
CC   -!- TISSUE SPECIFICITY: Expressed in fruit pulp after pollination. Not
CC       expressed in seeds, stems or leaves. {ECO:0000269|PubMed:7665074}.
CC   -!- PTM: Glycosylated; contains as much as 13,9% of sugars (glucosamine,
CC       mannose, galactose, xylose, and fucose). {ECO:0000269|PubMed:2335505}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC       type inhibitor) family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The sweet side of life
CC       - Issue 17 of December 2001;
CC       URL="https://www.proteinspotlight.org/back_issues/017";
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DR   EMBL; D38598; BAA07603.1; -; mRNA.
DR   PIR; JC4232; A33872.
DR   AlphaFoldDB; P13087; -.
DR   SMR; P13087; -.
DR   MEROPS; I03.030; -.
DR   GlyConnect; 369; 5 N-Linked glycans (2 sites).
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd23375; beta-trefoil_STI_VvMLP-like; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR   InterPro; IPR002160; Prot_inh_Kunz-lg.
DR   PANTHER; PTHR33107; KUNITZ TRYPSIN INHIBITOR 2; 1.
DR   PANTHER; PTHR33107:SF5; KUNITZ TRYPSIN INHIBITOR 5; 1.
DR   Pfam; PF00197; Kunitz_legume; 1.
DR   PRINTS; PR00291; KUNITZINHBTR.
DR   SMART; SM00452; STI; 1.
DR   SUPFAM; SSF50386; STI-like; 1.
DR   PROSITE; PS00283; SOYBEAN_KUNITZ; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Signal;
KW   Taste-modifying protein.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:2708331,
FT                   ECO:0000269|PubMed:3403544"
FT   CHAIN           30..220
FT                   /note="Miraculin"
FT                   /id="PRO_0000016935"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2335505"
FT                   /id="CAR_000132"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2335505"
FT                   /id="CAR_000133"
FT   DISULFID        76..121
FT                   /evidence="ECO:0000269|PubMed:1911854"
FT   DISULFID        167
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:1911854"
FT   DISULFID        177..188
FT                   /evidence="ECO:0000269|PubMed:1911854"
FT   DISULFID        181..184
FT                   /evidence="ECO:0000269|PubMed:1911854"
FT   CONFLICT        129
FT                   /note="W -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   220 AA;  24367 MW;  BD7E70CE1AAEE520 CRC64;
     MKELTMLSLS FFFVSALLAA AANPLLSAAD SAPNPVLDID GEKLRTGTNY YIVPVLRDHG
     GGLTVSATTP NGTFVCPPRV VQTRKEVDHD RPLAFFPENP KEDVVRVSTD LNINFSAFMP
     CRWTSSTVWR LDKYDESTGQ YFVTIGGVKG NPGPETISSW FKIEEFCGSG FYKLVFCPTV
     CGSCKVKCGD VGIYIDQKGR RRLALSDKPF AFEFNKTVYF
//